The extracellular matrix in tumor progression and metastasis

  • Johannes A. EbleEmail author
  • Stephan Niland


The extracellular matrix (ECM) constitutes the scaffold of tissues and organs. It is a complex network of extracellular proteins, proteoglycans and glycoproteins, which form supramolecular aggregates, such as fibrils and sheet-like networks. In addition to its biochemical composition, including the covalent intermolecular cross-linkages, the ECM is also characterized by its biophysical parameters, such as topography, molecular density, stiffness/rigidity and tension. Taking these biochemical and biophysical parameters into consideration, the ECM is very versatile and undergoes constant remodeling. This review focusses on this remodeling of the ECM under the influence of a primary solid tumor mass. Within this tumor stroma, not only the cancer cells but also the resident fibroblasts, which differentiate into cancer-associated fibroblasts (CAFs), modify the ECM. Growth factors and chemokines, which are tethered to and released from the ECM, as well as metabolic changes of the cells within the tumor bulk, add to the tumor-supporting tumor microenvironment. Metastasizing cancer cells from a primary tumor mass infiltrate into the ECM, which variably may facilitate cancer cell migration or act as barrier, which has to be proteolytically breached by the infiltrating tumor cell. The biochemical and biophysical properties therefore determine the rates and routes of metastatic dissemination. Moreover, primed by soluble factors of the primary tumor, the ECM of distant organs may be remodeled in a way to facilitate the engraftment of metastasizing cancer cells. Such premetastatic niches are responsible for the organotropic preference of certain cancer entities to colonize at certain sites in distant organs and to establish a metastasis. Translational application of our knowledge about the cancer-primed ECM is sparse with respect to therapeutic approaches, whereas tumor-induced ECM alterations such as increased tissue stiffness and desmoplasia, as well as breaching the basement membrane are hallmark of malignancy and diagnostically and histologically harnessed.


Extracellular matrix Tumor progression Tumor microenvironment Cancer-associated fibroblast Metastatic cascade Cell migration Cell infiltration Invadopodia Metastatic niche Metastasis 



A disintegrin and metalloproteinase with thrombospondin motifs


Cancer-associated fibroblast


CTGF, Cyr61, and NOV


Connective tissue growth

CXCL12 = SDF.1

C-X-X chemokine 12 = stroma cell-derived factor-1


Cysteine-rich angiogenic protein 61


Discoidin domain receptor


Extracellular matrix

ED-A, -B

Extra domain-A, -B


Epidermal growth factor-like


Epidermal growth factor receptor


Neutrophil elastase


Elastin receptor complex


Endocytic receptor 180 = C-type mannose receptor 2


Fibronectin fragment




Glycoprotein VI


Hepatocyte growth factor


Insulin-like growth factor 1 receptor




Kirsten rat sarcoma oncogene


Leukocyte-associated immunoglobulin-like receptor 1

LG3, 4

Laminin globular domain 3, 4


Lysyl oxidase/lysyl oxidase-like


Low-density lipoprotein receptor-related protein 6


Lymphocyte antigen 75 (CD205, DEC-205)


Mesenchymal-epithelial transition factor proto-oncogene, hepatocyte growth factor receptor, HGFR


Matrix metalloproteinase


Mannose receptor


Muscle-specific kinase


Non-collagenous domain 1


Neural cell adhesion molecule L1


Nephroblastoma overexpressed gene


Neuron-glial related cell adhesion molecule


Protease-activated receptor


Programmed death-1/programmed death ligand-1


Platelet-derived growth factor




Semaphorin 3F


Small integrin-binding ligand-N-linked glycoprotein


Small leucine-rich proteoglycan


Secreted protein, acid and rich in cysteine


Tumor-associated macrophage


Tissue factor

TLR-2, -4

Toll-like receptor-2, -4


Tumor microenvironment


Transforming growth factor-β


Regulatory T cell


Vascular endothelial growth factor


Vascular endothelial growth factor receptor 2


Vasculogenic mimicry



To study different aspect of tumor biology, J.A.E. receives financial support from Deutsche Forschungsgemeinschaft (SFB1009 A09) (MMP14 in invadopodia), from the People Programme (Marie Curie Actions) of the European Union’s Seventh Framework Programme FP7/2007-2013/under the REA Grant agreement n° [316610] (CAF differentiation in tumor stroma), and from the Wilhelm Sander Stiftung (grant:2016.113.1 to J.A.E.) (Interactions between tumor and endothelial cells).

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.


  1. 1.
    Hanahan D, Weinberg RA (2000) The hallmarks of cancer. Cell 100(1):57–70CrossRefPubMedGoogle Scholar
  2. 2.
    Hanahan D, Weinberg RA (2011) Hallmarks of cancer: the next generation. Cell 144(5):646–674. CrossRefGoogle Scholar
  3. 3.
    Paul CD, Mistriotis P, Konstantopoulos K (2017) Cancer cell motility: lessons from migration in confined spaces. Nat Rev Cancer 17(2):131–140. CrossRefPubMedGoogle Scholar
  4. 4.
    Theocharis AD, Skandalis SS, Gialeli C, Karamanos NK (2016) Extracellular matrix structure. Adv Drug Deliv Rev 97:4–27. CrossRefPubMedGoogle Scholar
  5. 5.
    Chang TT, Thakar D, Weaver VM (2017) Force-dependent breaching of the basement membrane. Matrix Biol 57–58:178–189. CrossRefPubMedGoogle Scholar
  6. 6.
    Walker C, Mojares E, Del Rio Hernandez A (2018) Role of extracellular matrix in development and cancer progression. Int J Mol Sci 19(10):3028. CrossRefPubMedCentralGoogle Scholar
  7. 7.
    Kalluri R (2016) The biology and function of fibroblasts in cancer. Nat Rev Cancer 16(9):582–598. CrossRefGoogle Scholar
  8. 8.
    Rozario T, DeSimone DW (2010) The extracellular matrix in development and morphogenesis: a dynamic view. Dev Biol 341(1):126–140. CrossRefPubMedGoogle Scholar
  9. 9.
    Halper J, Kjaer M (2014) Basic components of connective tissues and extracellular matrix: elastin, fibrillin, fibulins, fibrinogen, fibronectin, laminin, tenascins and thrombospondins. Adv Exp Med Biol 802:31–47. CrossRefPubMedGoogle Scholar
  10. 10.
    Singh B, Fleury C, Jalalvand F, Riesbeck K (2012) Human pathogens utilize host extracellular matrix proteins laminin and collagen for adhesion and invasion of the host. FEMS Microbiol Rev 36(6):1122–1180. CrossRefPubMedGoogle Scholar
  11. 11.
    Halfter W, Oertle P, Monnier CA, Camenzind L, Reyes-Lua M, Hu H, Candiello J, Labilloy A, Balasubramani M, Henrich PB, Plodinec M (2015) New concepts in basement membrane biology. FEBS J 282(23):4466–4479. CrossRefPubMedGoogle Scholar
  12. 12.
    Mak KM, Mei R (2017) Basement membrane type IV collagen and laminin: an overview of their biology and value as fibrosis biomarkers of liver disease. Anat Rec (Hoboken) 300(8):1371–1390. CrossRefGoogle Scholar
  13. 13.
    McCarthy KJ (2015) The basement membrane proteoglycans perlecan and agrin: something old, something new. Curr Top Membr 76:255–303. CrossRefPubMedGoogle Scholar
  14. 14.
    Miller RT (2017) Mechanical properties of basement membrane in health and disease. Matrix Biol 57–58:366–373. CrossRefPubMedGoogle Scholar
  15. 15.
    Randles MJ, Humphries MJ, Lennon R (2017) Proteomic definitions of basement membrane composition in health and disease. Matrix Biol 57–58:12–28. CrossRefPubMedGoogle Scholar
  16. 16.
    Liang J, Jiang D, Noble PW (2016) Hyaluronan as a therapeutic target in human diseases. Adv Drug Deliv Rev 97:186–203. CrossRefPubMedGoogle Scholar
  17. 17.
    Iozzo RV, Schaefer L (2015) Proteoglycan form and function: a comprehensive nomenclature of proteoglycans. Matrix Biol 42:11–55. CrossRefPubMedPubMedCentralGoogle Scholar
  18. 18.
    Schaefer L, Tredup C, Gubbiotti MA, Iozzo RV (2017) Proteoglycan neofunctions: regulation of inflammation and autophagy in cancer biology. FEBS J 284(1):10–26. CrossRefPubMedGoogle Scholar
  19. 19.
    Ricard-Blum S (2011) The collagen family. Cold Spring Harb Perspect Biol 3(1):a004978. CrossRefPubMedPubMedCentralGoogle Scholar
  20. 20.
    An B, Lin YS, Brodsky B (2016) Collagen interactions: drug design and delivery. Adv Drug Deliv Rev 97:69–84. CrossRefPubMedGoogle Scholar
  21. 21.
    Mao M, Alavi MV, Labelle-Dumais C, Gould DB (2015) Type IV collagens and basement membrane diseases: cell biology and pathogenic mechanisms. Curr Top Membr 76:61–116. CrossRefPubMedGoogle Scholar
  22. 22.
    Bhattacharjee A, Bansal M (2005) Collagen structure: the Madras triple helix and the current scenario. IUBMB Life 57(3):161–172. CrossRefPubMedGoogle Scholar
  23. 23.
    Brodsky B, Persikov AV (2005) Molecular structure of the collagen triple helix. Adv Protein Chem 70:301–339. CrossRefPubMedGoogle Scholar
  24. 24.
    Beck K, Brodsky B (1998) Supercoiled protein motifs: the collagen triple-helix and the α-helical coiled coil. J Struct Biol 122(1–2):17–29. CrossRefPubMedGoogle Scholar
  25. 25.
    Provenzano PP, Vanderby R Jr (2006) Collagen fibril morphology and organization: implications for force transmission in ligament and tendon. Matrix Biol 25(2):71–84. CrossRefPubMedGoogle Scholar
  26. 26.
    Boudko SP, Danylevych N, Hudson BG, Pedchenko VK (2018) Basement membrane collagen IV: isolation of functional domains. Methods Cell Biol 143:171–185. CrossRefPubMedGoogle Scholar
  27. 27.
    Cummings CF, Pedchenko V, Brown KL, Colon S, Rafi M, Jones-Paris C, Pokydeshava E, Liu M, Pastor-Pareja JC, Stothers C, Ero-Tolliver IA, McCall AS, Vanacore R, Bhave G, Santoro S, Blackwell TS, Zent R, Pozzi A, Hudson BG (2016) Extracellular chloride signals collagen IV network assembly during basement membrane formation. J Cell Biol 213(4):479–494. CrossRefPubMedPubMedCentralGoogle Scholar
  28. 28.
    Vanacore RM, Friedman DB, Ham AJ, Sundaramoorthy M, Hudson BG (2005) Identification of S-hydroxylysyl-methionine as the covalent cross-link of the noncollagenous (NC1) hexamer of the α1α1α2 collagen IV network: a role for the post-translational modification of lysine 211 to hydroxylysine 211 in hexamer assembly. J Biol Chem 280(32):29300–29310. CrossRefPubMedGoogle Scholar
  29. 29.
    Heljasvaara R, Aikio M, Ruotsalainen H, Pihlajaniemi T (2017) Collagen XVIII in tissue homeostasis and dysregulation—lessons learned from model organisms and human patients. Matrix Biol 57–58:55–75. CrossRefPubMedGoogle Scholar
  30. 30.
    Shaw LM, Olsen BR (1991) FACIT collagens: diverse molecular bridges in extracellular matrices. Trends Biochem Sci 16(5):191–194CrossRefPubMedGoogle Scholar
  31. 31.
    Has C, Bruckner-Tuderman L (2006) Molecular and diagnostic aspects of genetic skin fragility. J Dermatol Sci 44(3):129–144. CrossRefPubMedGoogle Scholar
  32. 32.
    Barker HE, Cox TR, Erler JT (2012) The rationale for targeting the LOX family in cancer. Nat Rev Cancer 12(8):540–552. CrossRefPubMedGoogle Scholar
  33. 33.
    Eckert RL, Fisher ML, Grun D, Adhikary G, Xu W, Kerr C (2015) Transglutaminase is a tumor cell and cancer stem cell survival factor. Mol Carcinog 54(10):947–958. CrossRefPubMedPubMedCentralGoogle Scholar
  34. 34.
    Li B, Cerione RA, Antonyak M (2011) Tissue transglutaminase and its role in human cancer progression. Adv Enzymol Relat Areas Mol Biol 78:247–293CrossRefPubMedGoogle Scholar
  35. 35.
    Saitow CB, Wise SG, Weiss AS, Castellot JJ, Kaplan DL (2013) Elastin biology and tissue engineering with adult cells. Biomol Concepts 4(2):173–185. CrossRefPubMedGoogle Scholar
  36. 36.
    Kim YM, Kim EC, Kim Y (2011) The human lysyl oxidase-like 2 protein functions as an amine oxidase toward collagen and elastin. Mol Biol Rep 38(1):145–149. CrossRefPubMedGoogle Scholar
  37. 37.
    Mezzenga R, Mitsi M (2018) The molecular dance of fibronectin: conformational flexibility leads to functional versatility. Biomacromol. CrossRefGoogle Scholar
  38. 38.
    White ES, Muro AF (2011) Fibronectin splice variants: understanding their multiple roles in health and disease using engineered mouse models. IUBMB Life 63(7):538–546. CrossRefPubMedGoogle Scholar
  39. 39.
    Kumra H, Reinhardt DP (2016) Fibronectin-targeted drug delivery in cancer. Adv Drug Deliv Rev 97:101–110. CrossRefPubMedGoogle Scholar
  40. 40.
    Woods A, Longley RL, Tumova S, Couchman JR (2000) Syndecan-4 binding to the high affinity heparin-binding domain of fibronectin drives focal adhesion formation in fibroblasts. Arch Biochem Biophys 374(1):66–72. CrossRefPubMedGoogle Scholar
  41. 41.
    Prasad A, Clark RA (2018) Fibronectin interaction with growth factors in the context of general ways extracellular matrix molecules regulate growth factor signaling. G Ital Dermatol Venereol 153(3):361–374. CrossRefPubMedGoogle Scholar
  42. 42.
    Dosio F, Arpicco S, Stella B, Fattal E (2016) Hyaluronic acid for anticancer drug and nucleic acid delivery. Adv Drug Deliv Rev 97:204–236. CrossRefPubMedGoogle Scholar
  43. 43.
    Neill T, Schaefer L, Iozzo RV (2016) Decorin as a multivalent therapeutic agent against cancer. Adv Drug Deliv Rev 97:174–185. CrossRefPubMedGoogle Scholar
  44. 44.
    Gubbiotti MA, Neill T, Iozzo RV (2017) A current view of perlecan in physiology and pathology: a mosaic of functions. Matrix Biol 57–58:285–298. CrossRefPubMedGoogle Scholar
  45. 45.
    Harvey SJ, Miner JH (2008) Revisiting the glomerular charge barrier in the molecular era. Curr Opin Nephrol Hypertens 17(4):393–398. CrossRefPubMedGoogle Scholar
  46. 46.
    Aumailley M (2013) The laminin family. Cell Adhes Migr 7(1):48–55. CrossRefGoogle Scholar
  47. 47.
    Hohenester E, Engel J (2002) Domain structure and organisation in extracellular matrix proteins. Matrix Biol 21(2):115–128CrossRefPubMedGoogle Scholar
  48. 48.
    Rousselle P, Beck K (2013) Laminin 332 processing impacts cellular behavior. Cell Adhes Migr 7(1):122–134. CrossRefGoogle Scholar
  49. 49.
    Hohenester E, Yurchenco PD (2013) Laminins in basement membrane assembly. Cell Adhes Migr 7(1):56–63. CrossRefGoogle Scholar
  50. 50.
    Thakur R, Mishra DP (2016) Matrix reloaded: CCN, tenascin and SIBLING group of matricellular proteins in orchestrating cancer hallmark capabilities. Pharmacol Ther 168:61–74. CrossRefPubMedGoogle Scholar
  51. 51.
    Viloria K, Hill NJ (2016) Embracing the complexity of matricellular proteins: the functional and clinical significance of splice variation. Biomol Concepts 7(2):117–132. CrossRefPubMedGoogle Scholar
  52. 52.
    Sawyer AJ, Kyriakides TR (2016) Matricellular proteins in drug delivery: therapeutic targets, active agents, and therapeutic localization. Adv Drug Deliv Rev 97:56–68. CrossRefPubMedPubMedCentralGoogle Scholar
  53. 53.
    Sofeu Feugaing DD, Gotte M, Viola M (2013) More than matrix: the multifaceted role of decorin in cancer. Eur J Cell Biol 92(1):1–11. CrossRefPubMedGoogle Scholar
  54. 54.
    Yoshida T, Akatsuka T, Imanaka-Yoshida K (2015) Tenascin-C and integrins in cancer. Cell Adhes Migr 9(1–2):96–104. CrossRefGoogle Scholar
  55. 55.
    Brellier F, Martina E, Degen M, Heuze-Vourc’h N, Petit A, Kryza T, Courty Y, Terracciano L, Ruiz C, Chiquet-Ehrismann R (2012) Tenascin-W is a better cancer biomarker than tenascin-C for most human solid tumors. BMC Clin Pathol 12:14. CrossRefPubMedPubMedCentralGoogle Scholar
  56. 56.
    Chiquet-Ehrismann R, Hagios C, Matsumoto K (1994) The tenascin gene family. Perspect Dev Neurobiol 2(1):3–7PubMedGoogle Scholar
  57. 57.
    Bellahcene A, Castronovo V, Ogbureke KU, Fisher LW, Fedarko NS (2008) Small integrin-binding ligand N-linked glycoproteins (SIBLINGs): multifunctional proteins in cancer. Nat Rev Cancer 8(3):212–226. CrossRefPubMedPubMedCentralGoogle Scholar
  58. 58.
    Kamili NA, Arthur CM, Gerner-Smidt C, Tafesse E, Blenda A, Dias-Baruffi M, Stowell SR (2016) Key regulators of galectin-glycan interactions. Proteomics 16(24):3111–3125. CrossRefPubMedPubMedCentralGoogle Scholar
  59. 59.
    Naschberger E, Liebl A, Schellerer VS, Schutz M, Britzen-Laurent N, Kolbel P, Schaal U, Haep L, Regensburger D, Wittmann T, Klein-Hitpass L, Rau TT, Dietel B, Meniel VS, Clarke AR, Merkel S, Croner RS, Hohenberger W, Sturzl M (2016) Matricellular protein SPARCL1 regulates tumor microenvironment-dependent endothelial cell heterogeneity in colorectal carcinoma. J Clin Invest 126(11):4187–4204. CrossRefPubMedPubMedCentralGoogle Scholar
  60. 60.
    Roberts DD, Kaur S, Isenberg JS (2017) Regulation of cellular redox signaling by matricellular proteins in vascular biology, immunology, and cancer. Antioxid Redox Signal 27(12):874–911. CrossRefPubMedPubMedCentralGoogle Scholar
  61. 61.
    Gonzalez-Gonzalez L, Alonso J (2018) Periostin: a matricellular protein with multiple functions in cancer development and progression. Front Oncol 8:225. CrossRefPubMedPubMedCentralGoogle Scholar
  62. 62.
    Vincent KM, Postovit LM (2018) Matricellular proteins in cancer: a focus on secreted Frizzled-related proteins. J Cell Commun Signal 12(1):103–112. CrossRefPubMedGoogle Scholar
  63. 63.
    Grosche J, Meissner J, Eble JA (2018) More than a syllable in fib-ROS-is: the role of ROS on the fibrotic extracellular matrix and on cellular contacts. Mol Aspects Med 63:30–46. CrossRefPubMedGoogle Scholar
  64. 64.
    Holle AW, Young JL, Van Vliet KJ, Kamm RD, Discher D, Janmey P, Spatz JP, Saif T (2018) Cell-extracellular matrix mechanobiology: forceful tools and emerging needs for basic and translational research. Nano Lett 18(1):1–8. CrossRefPubMedGoogle Scholar
  65. 65.
    Stroka KM, Konstantopoulos K (2014) Physical biology in cancer. 4. Physical cues guide tumor cell adhesion and migration. Am J Physiol Cell Physiol 306(2):C98–C109. CrossRefPubMedGoogle Scholar
  66. 66.
    Barczyk M, Carracedo S, Gullberg D (2010) Integrins. Cell Tissue Res 339(1):269–280. CrossRefPubMedGoogle Scholar
  67. 67.
    Campbell ID, Humphries MJ (2011) Integrin structure, activation, and interactions. Cold Spring Harb Perspect Biol 3(3):a004994. CrossRefPubMedPubMedCentralGoogle Scholar
  68. 68.
    Humphries JD, Chastney MR, Askari JA, Humphries MJ (2018) Signal transduction via integrin adhesion complexes. Curr Opin Cell Biol 56:14–21. CrossRefPubMedGoogle Scholar
  69. 69.
    Horton ER, Humphries JD, James J, Jones MC, Askari JA, Humphries MJ (2016) The integrin adhesome network at a glance. J Cell Sci 129(22):4159–4163. CrossRefPubMedPubMedCentralGoogle Scholar
  70. 70.
    Kanchanawong P, Shtengel G, Pasapera AM, Ramko EB, Davidson MW, Hess HF, Waterman CM (2010) Nanoscale architecture of integrin-based cell adhesions. Nature 468(7323):580–584. CrossRefPubMedPubMedCentralGoogle Scholar
  71. 71.
    Winograd-Katz SE, Fassler R, Geiger B, Legate KR (2014) The integrin adhesome: from genes and proteins to human disease. Nat Rev Mol Cell Biol 15(4):273–288. CrossRefPubMedGoogle Scholar
  72. 72.
    Geiger B, Yamada KM (2011) Molecular architecture and function of matrix adhesions. Cold Spring Harb Perspect Biol 3(5):a005033. CrossRefPubMedPubMedCentralGoogle Scholar
  73. 73.
    Zaidel-Bar R, Geiger B (2010) The switchable integrin adhesome. J Cell Sci 123(Pt 9):1385–1388. CrossRefPubMedPubMedCentralGoogle Scholar
  74. 74.
    Carulli S, Beck K, Dayan G, Boulesteix S, Lortat-Jacob H, Rousselle P (2012) Cell surface proteoglycans syndecan-1 and -4 bind overlapping but distinct sites in laminin α3 LG45 protein domain. J Biol Chem 287(15):12204–12216. CrossRefPubMedPubMedCentralGoogle Scholar
  75. 75.
    Bachy S, Letourneur F, Rousselle P (2008) Syndecan-1 interaction with the LG4/5 domain in laminin-332 is essential for keratinocyte migration. J Cell Physiol 214(1):238–249. CrossRefPubMedGoogle Scholar
  76. 76.
    Soares MA, Teixeira FC, Fontes M, Areas AL, Leal MG, Pavao MS, Stelling MP (2015) Heparan sulfate proteoglycans may promote or inhibit cancer progression by interacting with integrins and affecting cell migration. Biomed Res Int 2015:453801. CrossRefPubMedPubMedCentralGoogle Scholar
  77. 77.
    Pantazaka E, Papadimitriou E (2014) Chondroitin sulfate-cell membrane effectors as regulators of growth factor-mediated vascular and cancer cell migration. Biochim Biophys Acta 1840(8):2643–2650. CrossRefPubMedGoogle Scholar
  78. 78.
    Hinz B, Phan SH, Thannickal VJ, Prunotto M, Desmouliere A, Varga J, De Wever O, Mareel M, Gabbiani G (2012) Recent developments in myofibroblast biology: paradigms for connective tissue remodeling. Am J Pathol 180(4):1340–1355. CrossRefPubMedPubMedCentralGoogle Scholar
  79. 79.
    Otranto M, Sarrazy V, Bonte F, Hinz B, Gabbiani G, Desmouliere A (2012) The role of the myofibroblast in tumor stroma remodeling. Cell Adh Migr 6(3):203–219. CrossRefPubMedPubMedCentralGoogle Scholar
  80. 80.
    Dvorak HF (1986) Tumors: wounds that do not heal. Similarities between tumor stroma generation and wound healing. N Engl J Med 315(26):1650–1659. CrossRefPubMedGoogle Scholar
  81. 81.
    Dvorak HF (2015) Tumors: wounds that do not heal-redux. Cancer Immunol Res 3(1):1–11. CrossRefPubMedPubMedCentralGoogle Scholar
  82. 82.
    Kuzet SE, Gaggioli C (2016) Fibroblast activation in cancer: when seed fertilizes soil. Cell Tissue Res 365(3):607–619. CrossRefPubMedGoogle Scholar
  83. 83.
    Desmouliere A, Guyot C, Gabbiani G (2004) The stroma reaction myofibroblast: a key player in the control of tumor cell behavior. Int J Dev Biol 48(5–6):509–517. CrossRefPubMedGoogle Scholar
  84. 84.
    Caja L, Dituri F, Mancarella S, Caballero-Diaz D, Moustakas A, Giannelli G, Fabregat I (2018) TGF-β and the tissue microenvironment: relevance in fibrosis and cancer. Int J Mol Sci 19(5):1294. CrossRefPubMedCentralGoogle Scholar
  85. 85.
    Khan Z, Marshall JF (2016) The role of integrins in TGFβ activation in the tumour stroma. Cell Tissue Res 365(3):657–673. CrossRefPubMedPubMedCentralGoogle Scholar
  86. 86.
    Wang M, Zhao J, Zhang L, Wei F, Lian Y, Wu Y, Gong Z, Zhang S, Zhou J, Cao K, Li X, Xiong W, Li G, Zeng Z, Guo C (2017) Role of tumor microenvironment in tumorigenesis. J Cancer 8(5):761–773. CrossRefPubMedPubMedCentralGoogle Scholar
  87. 87.
    Crotti S, Piccoli M, Rizzolio F, Giordano A, Nitti D, Agostini M (2017) Extracellular matrix and colorectal cancer: how surrounding microenvironment affects cancer cell behavior? J Cell Physiol 232(5):967–975. CrossRefPubMedGoogle Scholar
  88. 88.
    Erdogan B, Webb DJ (2017) Cancer-associated fibroblasts modulate growth factor signaling and extracellular matrix remodeling to regulate tumor metastasis. Biochem Soc Trans 45(1):229–236. CrossRefPubMedPubMedCentralGoogle Scholar
  89. 89.
    Cunderlikova B (2016) Clinical significance of immunohistochemically detected extracellular matrix proteins and their spatial distribution in primary cancer. Crit Rev Oncol Hematol 105:127–144. CrossRefPubMedGoogle Scholar
  90. 90.
    Rizzacasa B, Morini E, Pucci S, Murdocca M, Novelli G, Amati F (2017) LOX-1 and its splice variants: a new challenge for atherosclerosis and cancer-targeted therapies. Int J Mol Sci 18(2):290. CrossRefPubMedCentralGoogle Scholar
  91. 91.
    Huang L, Xu AM, Liu W (2015) Transglutaminase 2 in cancer. Am J Cancer Res 5(9):2756–2776PubMedPubMedCentralGoogle Scholar
  92. 92.
    Rojas A, Anazco C, Gonzalez I, Araya P (2018) Extracellular matrix glycation and receptor for advanced glycation end-products activation: a missing piece in the puzzle of the association between diabetes and cancer. Carcinogenesis 39(4):515–521. CrossRefPubMedGoogle Scholar
  93. 93.
    Malik R, Lelkes PI, Cukierman E (2015) Biomechanical and biochemical remodeling of stromal extracellular matrix in cancer. Trends Biotechnol 33(4):230–236. CrossRefPubMedPubMedCentralGoogle Scholar
  94. 94.
    Malik R, Luong T, Cao X, Han B, Shah N, Franco-Barraza J, Han L, Shenoy VB, Lelkes PI, Cukierman E (2018) Rigidity controls human desmoplastic matrix anisotropy to enable pancreatic cancer cell spread via extracellular signal-regulated kinase 2. Matrix Biol 1:2. CrossRefGoogle Scholar
  95. 95.
    Tolle RC, Gaggioli C, Dengjel J (2018) Three-dimensional cell culture conditions affect the proteome of cancer-associated fibroblasts. J Proteome Res 17(8):2780–2789. CrossRefPubMedGoogle Scholar
  96. 96.
    Ronca R, Sozzani S, Presta M, Alessi P (2009) Delivering cytokines at tumor site: the immunocytokine-conjugated anti-EDB-fibronectin antibody case. Immunobiology 214(9–10):800–810. CrossRefPubMedGoogle Scholar
  97. 97.
    Ramamonjisoa N, Ackerstaff E (2017) Characterization of the tumor microenvironment and tumor-stroma interaction by non-invasive preclinical imaging. Front Oncol 7:3. CrossRefPubMedPubMedCentralGoogle Scholar
  98. 98.
    Micke P, Ostman A (2004) Tumour-stroma interaction: cancer-associated fibroblasts as novel targets in anti-cancer therapy? Lung Cancer 45(Suppl 2):S163–S175. CrossRefPubMedGoogle Scholar
  99. 99.
    Hirata E, Sahai E (2017) Tumor microenvironment and differential responses to therapy. Cold Spring Harb Perspect Med 7(7):a026781. CrossRefPubMedGoogle Scholar
  100. 100.
    Topalovski M, Brekken RA (2016) Matrix control of pancreatic cancer: new insights into fibronectin signaling. Cancer Lett 381(1):252–258. CrossRefPubMedGoogle Scholar
  101. 101.
    Zollinger AJ, Smith ML (2017) Fibronectin, the extracellular glue. Matrix Biol 60–61:27–37. CrossRefPubMedGoogle Scholar
  102. 102.
    Han Z, Lu ZR (2017) Targeting fibronectin for cancer imaging and therapy. J Mater Chem B 5(4):639–654. CrossRefPubMedGoogle Scholar
  103. 103.
    Wang K, Seo BR, Fischbach C, Gourdon D (2016) Fibronectin mechanobiology regulates tumorigenesis. Cell Mol Bioeng 9:1–11. CrossRefPubMedGoogle Scholar
  104. 104.
    Bachman H, Nicosia J, Dysart M, Barker TH (2015) Utilizing fibronectin integrin-binding specificity to control cellular responses. Adv Wound Care (New Rochelle) 4(8):501–511. CrossRefGoogle Scholar
  105. 105.
    Kanchanawong P, Waterman CM (2012) Advances in light-based imaging of three-dimensional cellular ultrastructure. Curr Opin Cell Biol 24(1):125–133. CrossRefPubMedGoogle Scholar
  106. 106.
    Chiovaro F, Martina E, Bottos A, Scherberich A, Hynes NE, Chiquet-Ehrismann R (2015) Transcriptional regulation of tenascin-W by TGF-β signaling in the bone metastatic niche of breast cancer cells. Int J Cancer 137(8):1842–1854. CrossRefPubMedPubMedCentralGoogle Scholar
  107. 107.
    Adams JC, Chiquet-Ehrismann R, Tucker RP (2015) The evolution of tenascins and fibronectin. Cell Adhes Migr 9(1–2):22–33. CrossRefGoogle Scholar
  108. 108.
    Martina E, Chiquet-Ehrismann R, Brellier F (2010) Tenascin-W: an extracellular matrix protein associated with osteogenesis and cancer. Int J Biochem Cell Biol 42(9):1412–1415. CrossRefPubMedGoogle Scholar
  109. 109.
    Degen M, Brellier F, Schenk S, Driscoll R, Zaman K, Stupp R, Tornillo L, Terracciano L, Chiquet-Ehrismann R, Ruegg C, Seelentag W (2008) Tenascin-W, a new marker of cancer stroma, is elevated in sera of colon and breast cancer patients. Int J Cancer 122(11):2454–2461. CrossRefPubMedGoogle Scholar
  110. 110.
    Degen M, Brellier F, Kain R, Ruiz C, Terracciano L, Orend G, Chiquet-Ehrismann R (2007) Tenascin-W is a novel marker for activated tumor stroma in low-grade human breast cancer and influences cell behavior. Cancer Res 67(19):9169–9179. CrossRefPubMedGoogle Scholar
  111. 111.
    Kim BG, An HJ, Kang S, Choi YP, Gao MQ, Park H, Cho NH (2011) Laminin-332-rich tumor microenvironment for tumor invasion in the interface zone of breast cancer. Am J Pathol 178(1):373–381. CrossRefPubMedPubMedCentralGoogle Scholar
  112. 112.
    Tsuruta D, Kobayashi H, Imanishi H, Sugawara K, Ishii M, Jones JC (2008) Laminin-332-integrin interaction: a target for cancer therapy? Curr Med Chem 15(20):1968–1975CrossRefPubMedPubMedCentralGoogle Scholar
  113. 113.
    Marinkovich MP (2007) Tumour microenvironment: laminin 332 in squamous-cell carcinoma. Nat Rev Cancer 7(5):370–380. CrossRefPubMedGoogle Scholar
  114. 114.
    Guess CM, Lafleur BJ, Weidow BL, Quaranta V (2009) A decreased ratio of laminin-332 β3 to gamma2 subunit mRNA is associated with poor prognosis in colon cancer. Cancer Epidemiol Biomark Prev 18(5):1584–1590. CrossRefGoogle Scholar
  115. 115.
    Guess CM, Quaranta V (2009) Defining the role of laminin-332 in carcinoma. Matrix Biol 28(8):445–455. CrossRefPubMedPubMedCentralGoogle Scholar
  116. 116.
    Chen J, Wang W, Wei J, Zhou D, Zhao X, Song W, Sun Q, Huang P, Zheng S (2015) Overexpression of β3 chains of laminin-332 is associated with clinicopathologic features and decreased survival in patients with pancreatic adenocarcinoma. Appl Immunohistochem Mol Morphol 23(7):516–521. CrossRefPubMedPubMedCentralGoogle Scholar
  117. 117.
    Katayama M, Funakoshi A, Sumii T, Sanzen N, Sekiguchi K (2005) Laminin gamma2-chain fragment circulating level increases in patients with metastatic pancreatic ductal cell adenocarcinomas. Cancer Lett 225(1):167–176. CrossRefPubMedGoogle Scholar
  118. 118.
    Ramovs V, Te Molder L, Sonnenberg A (2017) The opposing roles of laminin-binding integrins in cancer. Matrix Biol 57–58:213–243. CrossRefPubMedGoogle Scholar
  119. 119.
    Yamada M, Sekiguchi K (2015) Molecular basis of laminin-integrin interactions. Curr Top Membr 76:197–229. CrossRefPubMedGoogle Scholar
  120. 120.
    Tripathi M, Nandana S, Yamashita H, Ganesan R, Kirchhofer D, Quaranta V (2008) Laminin-332 is a substrate for hepsin, a protease associated with prostate cancer progression. J Biol Chem 283(45):30576–30584. CrossRefPubMedPubMedCentralGoogle Scholar
  121. 121.
    Tripathi M, Potdar AA, Yamashita H, Weidow B, Cummings PT, Kirchhofer D, Quaranta V (2011) Laminin-332 cleavage by matriptase alters motility parameters of prostate cancer cells. Prostate 71(2):184–196. CrossRefPubMedPubMedCentralGoogle Scholar
  122. 122.
    Cavaco ACM, Rezaei M, Caliandro MF, Lima AM, Stehling M, Dhayat SA, Haier J, Brakebusch C, Eble JA (2018) The interaction between laminin-332 and α3β1 integrin determines differentiation and maintenance of CAFs, and supports invasion of pancreatic duct adenocarcinoma cells. Cancers (Basel) 11(1):14. CrossRefGoogle Scholar
  123. 123.
    Luo Z, Wang Q, Lau WB, Lau B, Xu L, Zhao L, Yang H, Feng M, Xuan Y, Yang Y, Lei L, Wang C, Yi T, Zhao X, Wei Y, Zhou S (2016) Tumor microenvironment: the culprit for ovarian cancer metastasis? Cancer Lett 377(2):174–182. CrossRefPubMedGoogle Scholar
  124. 124.
    Paszek MJ, Zahir N, Johnson KR, Lakins JN, Rozenberg GI, Gefen A, Reinhart-King CA, Margulies SS, Dembo M, Boettiger D, Hammer DA, Weaver VM (2005) Tensional homeostasis and the malignant phenotype. Cancer Cell 8(3):241–254. CrossRefPubMedGoogle Scholar
  125. 125.
    Giussani M, Merlino G, Cappelletti V, Tagliabue E, Daidone MG (2015) Tumor-extracellular matrix interactions: identification of tools associated with breast cancer progression. Semin Cancer Biol 35:3–10. CrossRefPubMedGoogle Scholar
  126. 126.
    Sundquist E, Renko O, Salo S, Magga J, Cervigne NK, Nyberg P, Risteli J, Sormunen R, Vuolteenaho O, Zandonadi F, Paes Leme AF, Coletta RD, Ruskoaho H, Salo T (2016) Neoplastic extracellular matrix environment promotes cancer invasion in vitro. Exp Cell Res 344(2):229–240. CrossRefPubMedGoogle Scholar
  127. 127.
    Te Boekhorst V, Friedl P (2016) plasticity of cancer cell invasion-mechanisms and implications for therapy. Adv Cancer Res 132:209–264. CrossRefGoogle Scholar
  128. 128.
    Bhowmick NA, Neilson EG, Moses HL (2004) Stromal fibroblasts in cancer initiation and progression. Nature 432(7015):332–337. CrossRefPubMedPubMedCentralGoogle Scholar
  129. 129.
    Cavaco A, Rezaei M, Niland S, Eble JA (2017) Collateral damage intended: cancer-associated fibroblasts and vasculature are potential targets in cancer therapy. Int J Mol Sci 18(11):2355. CrossRefPubMedCentralGoogle Scholar
  130. 130.
    Marchiq I, Pouyssegur J (2016) Hypoxia, cancer metabolism and the therapeutic benefit of targeting lactate/H(+) symporters. J Mol Med (Berl) 94(2):155–171. CrossRefGoogle Scholar
  131. 131.
    Nielsen N, Lindemann O, Schwab A (2014) TRP channels and STIM/ORAI proteins: sensors and effectors of cancer and stroma cell migration. Br J Pharmacol 171(24):5524–5540. CrossRefPubMedPubMedCentralGoogle Scholar
  132. 132.
    Tochhawng L, Deng S, Pervaiz S, Yap CT (2013) Redox regulation of cancer cell migration and invasion. Mitochondrion 13(3):246–253. CrossRefPubMedGoogle Scholar
  133. 133.
    Xing Y, Zhao S, Zhou BP, Mi J (2015) Metabolic reprogramming of the tumour microenvironment. FEBS J 282(20):3892–3898. CrossRefPubMedGoogle Scholar
  134. 134.
    Baluna RG, Eng TY, Thomas CR (2006) Adhesion molecules in radiotherapy. Radiat Res 166(6):819–831. CrossRefPubMedGoogle Scholar
  135. 135.
    Borek C (2004) Dietary antioxidants and human cancer. Integr Cancer Ther 3(4):333–341. CrossRefPubMedGoogle Scholar
  136. 136.
    Westbury CB, Yarnold JR (2012) Radiation fibrosis–current clinical and therapeutic perspectives. Clin Oncol (R Coll Radiol) 24(10):657–672. CrossRefGoogle Scholar
  137. 137.
    Yahyapour R, Motevaseli E, Rezaeyan A, Abdollahi H, Farhood B, Cheki M, Rezapoor S, Shabeeb D, Musa AE, Najafi M, Villa V (2018) Reduction-oxidation (redox) system in radiation-induced normal tissue injury: molecular mechanisms and implications in radiation therapeutics. Clin Transl Oncol 20(8):975–988. CrossRefPubMedGoogle Scholar
  138. 138.
    Polanska UM, Orimo A (2013) Carcinoma-associated fibroblasts: non-neoplastic tumour-promoting mesenchymal cells. J Cell Physiol 228(8):1651–1657. CrossRefPubMedGoogle Scholar
  139. 139.
    Koch S, Claesson-Welsh L (2012) Signal transduction by vascular endothelial growth factor receptors. Cold Spring Harb Perspect Med 2(7):a006502. CrossRefPubMedPubMedCentralGoogle Scholar
  140. 140.
    Melincovici CS, Bosca AB, Susman S, Marginean M, Mihu C, Istrate M, Moldovan IM, Roman AL, Mihu CM (2018) Vascular endothelial growth factor (VEGF) - key factor in normal and pathological angiogenesis. Rom J Morphol Embryol 59(2):455–467PubMedGoogle Scholar
  141. 141.
    Miyazono K, Katsuno Y, Koinuma D, Ehata S, Morikawa M (2018) Intracellular and extracellular TGF-β signaling in cancer: some recent topics. Front Med 12(4):387–411. CrossRefPubMedGoogle Scholar
  142. 142.
    Crafts TD, Jensen AR, Blocher-Smith EC, Markel TA (2015) Vascular endothelial growth factor: therapeutic possibilities and challenges for the treatment of ischemia. Cytokine 71(2):385–393. CrossRefPubMedGoogle Scholar
  143. 143.
    Iozzo RV, Sanderson RD (2011) Proteoglycans in cancer biology, tumour microenvironment and angiogenesis. J Cell Mol Med 15(5):1013–1031. CrossRefPubMedPubMedCentralGoogle Scholar
  144. 144.
    Zanotelli MR, Reinhart-King CA (2018) Mechanical forces in tumor angiogenesis. Adv Exp Med Biol 1092:91–112. CrossRefPubMedGoogle Scholar
  145. 145.
    Edgar LT, Maas SA, Guilkey JE, Weiss JA (2015) A coupled model of neovessel growth and matrix mechanics describes and predicts angiogenesis in vitro. Biomech Model Mechanobiol 14(4):767–782. CrossRefPubMedGoogle Scholar
  146. 146.
    Sund M, Xie L, Kalluri R (2004) The contribution of vascular basement membranes and extracellular matrix to the mechanics of tumor angiogenesis. APMIS 112(7–8):450–462. CrossRefPubMedGoogle Scholar
  147. 147.
    Knopik-Skrocka A, Kręplewska P, Jarmołowska-Jurczyszyn D (2017) Tumor blood vessels and vasculogenic mimicry – Current knowledge and searching for new cellular/molecular targets of anti-angiogenic therapy. Adv Cell Biol 5(1):50–71. CrossRefGoogle Scholar
  148. 148.
    Zuazo-Gaztelu I, Casanovas O (2018) Unraveling the role of angiogenesis in cancer ecosystems. Front Oncol 8:248. CrossRefPubMedPubMedCentralGoogle Scholar
  149. 149.
    Dudley AC (2012) Tumor endothelial cells. Cold Spring Harb Perspect Med 2(3):a006536. CrossRefPubMedPubMedCentralGoogle Scholar
  150. 150.
    Angara K, Borin TF, Arbab AS (2017) Vascular mimicry: a novel neovascularization mechanism driving anti-angiogenic therapy (AAT) resistance in glioblastoma. Transl Oncol 10(4):650–660. CrossRefPubMedPubMedCentralGoogle Scholar
  151. 151.
    Dunleavey JM, Dudley AC (2012) Vascular mimicry: concepts and implications for anti-angiogenic therapy. Curr Angiogenes 1(2):133–138. CrossRefPubMedPubMedCentralGoogle Scholar
  152. 152.
    Seftor RE, Hess AR, Seftor EA, Kirschmann DA, Hardy KM, Margaryan NV, Hendrix MJ (2012) Tumor cell vasculogenic mimicry: from controversy to therapeutic promise. Am J Pathol 181(4):1115–1125. CrossRefPubMedPubMedCentralGoogle Scholar
  153. 153.
    Reid SE, Kay EJ, Neilson LJ, Henze AT, Serneels J, McGhee EJ, Dhayade S, Nixon C, Mackey JB, Santi A, Swaminathan K, Athineos D, Papalazarou V, Patella F, Roman-Fernandez A, ElMaghloob Y, Hernandez-Fernaud JR, Adams RH, Ismail S, Bryant DM, Salmeron-Sanchez M, Machesky LM, Carlin LM, Blyth K, Mazzone M, Zanivan S (2017) Tumor matrix stiffness promotes metastatic cancer cell interaction with the endothelium. EMBO J 36(16):2373–2389. CrossRefPubMedPubMedCentralGoogle Scholar
  154. 154.
    Folberg R, Maniotis AJ (2004) Vasculogenic mimicry. APMIS 112(7–8):508–525. CrossRefPubMedGoogle Scholar
  155. 155.
    Cao Z, Bao M, Miele L, Sarkar FH, Wang Z, Zhou Q (2013) Tumour vasculogenic mimicry is associated with poor prognosis of human cancer patients: a systemic review and meta-analysis. Eur J Cancer 49(18):3914–3923. CrossRefPubMedGoogle Scholar
  156. 156.
    Hutchenreuther J, Vincent K, Norley C, Racanelli M, Gruber SB, Johnson TM, Fullen DR, Raskin L, Perbal B, Holdsworth DW, Postovit LM, Leask A (2018) Activation of cancer-associated fibroblasts is required for tumor neovascularization in a murine model of melanoma. Matrix Biol. CrossRefPubMedGoogle Scholar
  157. 157.
    Seftor RE, Seftor EA, Kirschmann DA, Hendrix MJ (2002) Targeting the tumor microenvironment with chemically modified tetracyclines: inhibition of laminin 5 gamma2 chain promigratory fragments and vasculogenic mimicry. Mol Cancer Ther 1(13):1173–1179PubMedGoogle Scholar
  158. 158.
    Qiao L, Liang N, Zhang J, Xie J, Liu F, Xu D, Yu X, Tian Y (2015) Advanced research on vasculogenic mimicry in cancer. J Cell Mol Med 19(2):315–326. CrossRefPubMedPubMedCentralGoogle Scholar
  159. 159.
    Velez DO, Tsui B, Goshia T, Chute CL, Han A, Carter H, Fraley SI (2017) 3D collagen architecture induces a conserved migratory and transcriptional response linked to vasculogenic mimicry. Nat Commun 8(1):1651. CrossRefPubMedPubMedCentralGoogle Scholar
  160. 160.
    Labelle M, Hynes RO (2012) The initial hours of metastasis: the importance of cooperative host-tumor cell interactions during hematogenous dissemination. Cancer Discov 2(12):1091–1099. CrossRefPubMedPubMedCentralGoogle Scholar
  161. 161.
    Sleeman JP, Cady B, Pantel K (2012) The connectivity of lymphogenous and hematogenous tumor cell dissemination: biological insights and clinical implications. Clin Exp Metastasis 29(7):737–746. CrossRefPubMedGoogle Scholar
  162. 162.
    Zhu T, Hu X, Wei P, Shan G (2018) Molecular background of the regional lymph node metastasis of gastric cancer. Oncol Lett 15(3):3409–3414. CrossRefPubMedPubMedCentralGoogle Scholar
  163. 163.
    Jones D, Pereira ER, Padera TP (2018) Growth and immune evasion of lymph node metastasis. Front Oncol 8:36. CrossRefPubMedPubMedCentralGoogle Scholar
  164. 164.
    Pircher A, Wolf D, Heidenreich A, Hilbe W, Pichler R, Heidegger I (2017) Synergies of targeting tumor angiogenesis and immune checkpoints in non-small cell lung cancer and renal cell cancer: from basic concepts to clinical reality. Int J Mol Sci 18(11):2291. CrossRefPubMedCentralGoogle Scholar
  165. 165.
    Schito L (2018) Bridging angiogenesis and immune evasion in the hypoxic tumor microenvironment. Am J Physiol Regul Integr Comp Physiol 1:4. CrossRefGoogle Scholar
  166. 166.
    Cimpean AM, Tamma R, Ruggieri S, Nico B, Toma A, Ribatti D (2017) Mast cells in breast cancer angiogenesis. Crit Rev Oncol Hematol 115:23–26. CrossRefPubMedGoogle Scholar
  167. 167.
    Gajewski TF, Schreiber H, Fu YX (2013) Innate and adaptive immune cells in the tumor microenvironment. Nat Immunol 14(10):1014–1022. CrossRefPubMedPubMedCentralGoogle Scholar
  168. 168.
    Quail DF, Joyce JA (2013) Microenvironmental regulation of tumor progression and metastasis. Nat Med 19(11):1423–1437. CrossRefPubMedPubMedCentralGoogle Scholar
  169. 169.
    Sangaletti S, Chiodoni C, Tripodo C, Colombo MP (2017) The good and bad of targeting cancer-associated extracellular matrix. Curr Opin Pharmacol 35:75–82. CrossRefPubMedGoogle Scholar
  170. 170.
    Hao NB, Lu MH, Fan YH, Cao YL, Zhang ZR, Yang SM (2012) Macrophages in tumor microenvironments and the progression of tumors. Clin Dev Immunol 2012:948098. CrossRefPubMedPubMedCentralGoogle Scholar
  171. 171.
    Shevach EM (2009) Mechanisms of foxp3 + T regulatory cell-mediated suppression. Immunity 30(5):636–645. CrossRefPubMedGoogle Scholar
  172. 172.
    Sica A, Massarotti M (2017) Myeloid suppressor cells in cancer and autoimmunity. J Autoimmun 85:117–125. CrossRefPubMedGoogle Scholar
  173. 173.
    Zhao H, Liao X, Kang Y (2017) Tregs: where we are and what comes next? Front Immunol 8:1578. CrossRefPubMedPubMedCentralGoogle Scholar
  174. 174.
    Dermani FK, Samadi P, Rahmani G, Kohlan AK, Najafi R (2019) PD-1/PD-L1 immune checkpoint: potential target for cancer therapy. J Cell Physiol 234(2):1313–1325. CrossRefPubMedGoogle Scholar
  175. 175.
    Hahn AW, Gill DM, Pal SK, Agarwal N (2017) The future of immune checkpoint cancer therapy after PD-1 and CTLA-4. Immunotherapy 9(8):681–692. CrossRefPubMedGoogle Scholar
  176. 176.
    Hatae R, Chamoto K (2016) Immune checkpoint inhibitors targeting programmed cell death-1 (PD-1) in cancer therapy. Rinsho Ketsueki 57(10):2224–2231. CrossRefPubMedGoogle Scholar
  177. 177.
    Chakravarthy A, Khan L, Bensler NP, Bose P, De Carvalho DD (2018) TGF-β-associated extracellular matrix genes link cancer-associated fibroblasts to immune evasion and immunotherapy failure. Nat Commun 9(1):4692. CrossRefPubMedPubMedCentralGoogle Scholar
  178. 178.
    Rhee I (2016) Diverse macrophages polarization in tumor microenvironment. Arch Pharm Res 39(11):1588–1596. CrossRefPubMedGoogle Scholar
  179. 179.
    Torcellan T, Stolp J, Chtanova T (2017) In vivo imaging sheds light on immune cell migration and function in cancer. Front Immunol 8:309. CrossRefPubMedPubMedCentralGoogle Scholar
  180. 180.
    Jacquemet G, Hamidi H, Ivaska J (2015) Filopodia in cell adhesion, 3D migration and cancer cell invasion. Curr Opin Cell Biol 36:23–31. CrossRefPubMedGoogle Scholar
  181. 181.
    Angst BD, Marcozzi C, Magee AI (2001) The cadherin superfamily. J Cell Sci 114(Pt 4):625–626PubMedGoogle Scholar
  182. 182.
    Bertocchi C, Wang Y, Ravasio A, Hara Y, Wu Y, Sailov T, Baird MA, Davidson MW, Zaidel-Bar R, Toyama Y, Ladoux B, Mege RM, Kanchanawong P (2017) Nanoscale architecture of cadherin-based cell adhesions. Nat Cell Biol 19(1):28–37. CrossRefPubMedGoogle Scholar
  183. 183.
    Gloushankova NA, Rubtsova SN, Zhitnyak IY (2017) Cadherin-mediated cell-cell interactions in normal and cancer cells. Tissue Barriers 5(3):e1356900. CrossRefPubMedPubMedCentralGoogle Scholar
  184. 184.
    Harrison OJ, Jin X, Hong S, Bahna F, Ahlsen G, Brasch J, Wu Y, Vendome J, Felsovalyi K, Hampton CM, Troyanovsky RB, Ben-Shaul A, Frank J, Troyanovsky SM, Shapiro L, Honig B (2011) The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. Structure 19(2):244–256. CrossRefPubMedPubMedCentralGoogle Scholar
  185. 185.
    Leckband DE, de Rooij J (2014) Cadherin adhesion and mechanotransduction. Annu Rev Cell Dev Biol 30:291–315. CrossRefPubMedGoogle Scholar
  186. 186.
    Cichon MA, Radisky DC (2014) Extracellular matrix as a contextual determinant of transforming growth factor-β signaling in epithelial-mesenchymal transition and in cancer. Cell Adhes Migr 8(6):588–594. CrossRefGoogle Scholar
  187. 187.
    Pietila M, Ivaska J, Mani SA (2016) Whom to blame for metastasis, the epithelial-mesenchymal transition or the tumor microenvironment? Cancer Lett 380(1):359–368. CrossRefPubMedGoogle Scholar
  188. 188.
    Yu Y, Xiao CH, Tan LD, Wang QS, Li XQ, Feng YM (2014) Cancer-associated fibroblasts induce epithelial-mesenchymal transition of breast cancer cells through paracrine TGF-β signalling. Br J Cancer 110(3):724–732. CrossRefPubMedGoogle Scholar
  189. 189.
    Eatemadi A, Aiyelabegan HT, Negahdari B, Mazlomi MA, Daraee H, Daraee N, Eatemadi R, Sadroddiny E (2017) Role of protease and protease inhibitors in cancer pathogenesis and treatment. Biomed Pharmacother 86:221–231. CrossRefPubMedGoogle Scholar
  190. 190.
    Wolf K, Friedl P (2011) Extracellular matrix determinants of proteolytic and non-proteolytic cell migration. Trends Cell Biol 21(12):736–744. CrossRefPubMedGoogle Scholar
  191. 191.
    Stefanidakis M, Koivunen E (2006) Cell-surface association between matrix metalloproteinases and integrins: role of the complexes in leukocyte migration and cancer progression. Blood 108(5):1441–1450. CrossRefPubMedGoogle Scholar
  192. 192.
    Nagase H, Visse R, Murphy G (2006) Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc Res 69(3):562–573. CrossRefPubMedGoogle Scholar
  193. 193.
    Jacob A, Prekeris R (2015) The regulation of MMP targeting to invadopodia during cancer metastasis. Front Cell Dev Biol 3:4. CrossRefPubMedPubMedCentralGoogle Scholar
  194. 194.
    Ren F, Tang R, Zhang X, Madushi WM, Luo D, Dang Y, Li Z, Wei K, Chen G (2015) Overexpression of MMP family members functions as prognostic biomarker for breast cancer patients: a systematic review and meta-analysis. PLoS ONE 10(8):e0135544. CrossRefPubMedPubMedCentralGoogle Scholar
  195. 195.
    Vandooren J, Van den Steen PE, Opdenakker G (2013) Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9): the next decade. Crit Rev Biochem Mol Biol 48(3):222–272. CrossRefPubMedGoogle Scholar
  196. 196.
    Huang H (2018) Matrix metalloproteinase-9 (MMP-9) as a cancer biomarker and MMP-9 biosensors: recent advances. Sensors (Basel) 18(10):3249. CrossRefGoogle Scholar
  197. 197.
    Zhang X, Huang S, Guo J, Zhou L, You L, Zhang T, Zhao Y (2016) Insights into the distinct roles of MMP-11 in tumor biology and future therapeutics (review). Int J Oncol 48(5):1783–1793. CrossRefPubMedGoogle Scholar
  198. 198.
    Castro-Castro A, Marchesin V, Monteiro P, Lodillinsky C, Rosse C, Chavrier P (2016) Cellular and molecular mechanisms of MT1-MMP-dependent cancer cell invasion. Annu Rev Cell Dev Biol 32:555–576. CrossRefPubMedGoogle Scholar
  199. 199.
    Pahwa S, Stawikowski MJ, Fields GB (2014) Monitoring and inhibiting MT1-MMP during cancer initiation and progression. Cancers (Basel) 6(1):416–435. CrossRefGoogle Scholar
  200. 200.
    Alcantara MB, Dass CR (2013) Regulation of MT1-MMP and MMP-2 by the serpin PEDF: a promising new target for metastatic cancer. Cell Physiol Biochem 31(4–5):487–494. CrossRefPubMedGoogle Scholar
  201. 201.
    Poincloux R, Lizarraga F, Chavrier P (2009) Matrix invasion by tumour cells: a focus on MT1-MMP trafficking to invadopodia. J Cell Sci 122(Pt 17):3015–3024. CrossRefPubMedGoogle Scholar
  202. 202.
    Radisky ES, Radisky DC (2015) Matrix metalloproteinases as breast cancer drivers and therapeutic targets. Front Biosci 20:1144–1163. CrossRefGoogle Scholar
  203. 203.
    Parvanescu V, Georgescu M, Georgescu I, Surlin V, Patrascu S, Picleanu AM, Georgescu E (2015) The role of matrix metalloproteinase-9 (MMP-9) as a prognostic factor in epithelial and lymphatic neoplasia. Chirurgia (Bucur) 110(6):506–510Google Scholar
  204. 204.
    Tam EM, Moore TR, Butler GS, Overall CM (2004) Characterization of the distinct collagen binding, helicase and cleavage mechanisms of matrix metalloproteinase 2 and 14 (gelatinase A and MT1-MMP): the differential roles of the MMP hemopexin c domains and the MMP-2 fibronectin type II modules in collagen triple helicase activities. J Biol Chem 279(41):43336–43344. CrossRefPubMedGoogle Scholar
  205. 205.
    Farina AR, Mackay AR (2014) Gelatinase B/MMP-9 in tumour pathogenesis and progression. Cancers (Basel) 6(1):240–296. CrossRefGoogle Scholar
  206. 206.
    Overall CM (2001) Matrix metalloproteinase substrate binding domains, modules and exosites. Overview and experimental strategies. Methods Mol Biol 151:79–120PubMedGoogle Scholar
  207. 207.
    Thakur V, Bedogni B (2016) The membrane tethered matrix metalloproteinase MT1-MMP at the forefront of melanoma cell invasion and metastasis. Pharmacol Res 111:17–22. CrossRefPubMedGoogle Scholar
  208. 208.
    Sato H, Takino T (2010) Coordinate action of membrane-type matrix metalloproteinase-1 (MT1-MMP) and MMP-2 enhances pericellular proteolysis and invasion. Cancer Sci 101(4):843–847. CrossRefPubMedGoogle Scholar
  209. 209.
    Saad S, Gottlieb DJ, Bradstock KF, Overall CM, Bendall LJ (2002) Cancer cell-associated fibronectin induces release of matrix metalloproteinase-2 from normal fibroblasts. Cancer Res 62(1):283–289PubMedGoogle Scholar
  210. 210.
    Itoh Y (2006) MT1-MMP: a key regulator of cell migration in tissue. IUBMB Life 58(10):589–596. CrossRefPubMedPubMedCentralGoogle Scholar
  211. 211.
    Itoh Y, Seiki M (2006) MT1-MMP: a potent modifier of pericellular microenvironment. J Cell Physiol 206(1):1–8. CrossRefPubMedGoogle Scholar
  212. 212.
    Eddy RJ, Weidmann MD, Sharma VP, Condeelis JS (2017) Tumor cell invadopodia: invasive protrusions that orchestrate metastasis. Trends Cell Biol 27(8):595–607. CrossRefPubMedPubMedCentralGoogle Scholar
  213. 213.
    Revach OY, Geiger B (2014) The interplay between the proteolytic, invasive, and adhesive domains of invadopodia and their roles in cancer invasion. Cell Adhes Migr 8(3):215–225CrossRefGoogle Scholar
  214. 214.
    Bagnato A, Rosano L (2018) Endothelin-1 receptor drives invadopodia: exploiting how β-arrestin-1 guides the way. Small GTPases 9(5):394–398. CrossRefPubMedGoogle Scholar
  215. 215.
    Alekhina O, Burstein E, Billadeau DD (2017) Cellular functions of WASP family proteins at a glance. J Cell Sci 130(14):2235–2241. CrossRefPubMedPubMedCentralGoogle Scholar
  216. 216.
    Frugtniet B, Jiang WG, Martin TA (2015) Role of the WASP and WAVE family proteins in breast cancer invasion and metastasis. Breast Cancer (Dove Med Press) 7:99–109. CrossRefPubMedCentralGoogle Scholar
  217. 217.
    Parekh A, Weaver AM (2016) Regulation of invadopodia by mechanical signaling. Exp Cell Res 343(1):89–95. CrossRefPubMedGoogle Scholar
  218. 218.
    Jeannot P, Besson A (2017) Cortactin function in invadopodia. Small GTPases. CrossRefPubMedGoogle Scholar
  219. 219.
    Linder S (2007) The matrix corroded: podosomes and invadopodia in extracellular matrix degradation. Trends Cell Biol 17(3):107–117. CrossRefPubMedGoogle Scholar
  220. 220.
    Nicholas NS, Pipili A, Lesjak MS, Wells CM (2017) Differential role for PAK1 and PAK4 during the invadopodia lifecycle. Small GTPases. CrossRefPubMedGoogle Scholar
  221. 221.
    Seano G, Primo L (2015) Podosomes and invadopodia: tools to breach vascular basement membrane. Cell Cycle 14(9):1370–1374. CrossRefPubMedPubMedCentralGoogle Scholar
  222. 222.
    Deryugina EI, Quigley JP (2015) Tumor angiogenesis: MMP-mediated induction of intravasation- and metastasis-sustaining neovasculature. Matrix Biol 44–46:94–112. CrossRefPubMedPubMedCentralGoogle Scholar
  223. 223.
    Genis L, Galvez BG, Gonzalo P, Arroyo AG (2006) MT1-MMP: universal or particular player in angiogenesis? Cancer Metastasis Rev 25(1):77–86. CrossRefPubMedGoogle Scholar
  224. 224.
    Binder MJ, McCoombe S, Williams ED, McCulloch DR, Ward AC (2017) The extracellular matrix in cancer progression: role of hyalectan proteoglycans and ADAMTS enzymes. Cancer Lett 385:55–64. CrossRefPubMedGoogle Scholar
  225. 225.
    Branch KM, Hoshino D, Weaver AM (2012) Adhesion rings surround invadopodia and promote maturation. Biol Open 1(8):711–722. CrossRefPubMedPubMedCentralGoogle Scholar
  226. 226.
    Zara M, Canobbio I, Visconte C, Canino J, Torti M, Guidetti GF (2018) Molecular mechanisms of platelet activation and aggregation induced by breast cancer cells. Cell Signal 48:45–53. CrossRefPubMedGoogle Scholar
  227. 227.
    Covic L, Kuliopulos A (2018) Protease-activated receptor 1 as therapeutic target in breast, lung, and ovarian cancer: pepducin approach. Int J Mol Sci 19(8):2237. CrossRefPubMedCentralGoogle Scholar
  228. 228.
    Liu X, Yu J, Song S, Yue X, Li Q (2017) Protease-activated receptor-1 (PAR-1): a promising molecular target for cancer. Oncotarget 8(63):107334–107345. CrossRefPubMedPubMedCentralGoogle Scholar
  229. 229.
    Monboisse JC, Oudart JB, Ramont L, Brassart-Pasco S (1840) Maquart FX (2014) Matrikines from basement membrane collagens: a new anti-cancer strategy. Biochim Biophys Acta 8:2589–2598. CrossRefGoogle Scholar
  230. 230.
    Tran KT, Lamb P, Deng JS (2005) Matrikines and matricryptins: implications for cutaneous cancers and skin repair. J Dermatol Sci 40(1):11–20. CrossRefPubMedGoogle Scholar
  231. 231.
    Hornebeck W, Maquart FX (2003) Proteolyzed matrix as a template for the regulation of tumor progression. Biomed Pharmacother 57(5–6):223–230CrossRefPubMedGoogle Scholar
  232. 232.
    Ramont L, Brassart-Pasco S, Thevenard J, Deshorgue A, Venteo L, Laronze JY, Pluot M, Monboisse JC, Maquart FX (2007) The NC1 domain of type XIX collagen inhibits in vivo melanoma growth. Mol Cancer Ther 6(2):506–514. CrossRefPubMedGoogle Scholar
  233. 233.
    Brassart-Pasco S, Senechal K, Thevenard J, Ramont L, Devy J, Di Stefano L, Dupont-Deshorgue A, Brezillon S, Feru J, Jazeron JF, Diebold MD, Ricard-Blum S, Maquart FX, Monboisse JC (2012) Tetrastatin, the NC1 domain of the α4(IV) collagen chain: a novel potent anti-tumor matrikine. PLoS ONE 7(4):e29587. CrossRefPubMedPubMedCentralGoogle Scholar
  234. 234.
    Folkman J (2006) Antiangiogenesis in cancer therapy–endostatin and its mechanisms of action. Exp Cell Res 312(5):594–607. CrossRefPubMedGoogle Scholar
  235. 235.
    Liu X, Nie W, Xie Q, Chen G, Li X, Jia Y, Yin B, Qu X, Li Y, Liang J (2018) Endostatin reverses immunosuppression of the tumor microenvironment in lung carcinoma. Oncol Lett 15(2):1874–1880. CrossRefPubMedGoogle Scholar
  236. 236.
    Hope C, Emmerich PB, Papadas A, Pagenkopf A, Matkowskyj KA, Van De Hey DR, Payne SN, Clipson L, Callander NS, Hematti P, Miyamoto S, Johnson MG, Deming DA, Asimakopoulos F (2017) Versican-derived matrikines regulate Batf3-dendritic cell differentiation and promote T cell infiltration in colorectal cancer. J Immunol 199(5):1933–1941. CrossRefPubMedPubMedCentralGoogle Scholar
  237. 237.
    Poluzzi C, Iozzo RV, Schaefer L (2016) Endostatin and endorepellin: a common route of action for similar angiostatic cancer avengers. Adv Drug Deliv Rev 97:156–173. CrossRefPubMedGoogle Scholar
  238. 238.
    Woodall BP, Nystrom A, Iozzo RA, Eble JA, Niland S, Krieg T, Eckes B, Pozzi A, Iozzo RV (2008) Integrin α2β1 is the required receptor for endorepellin angiostatic activity. J Biol Chem 283(4):2335–2343. CrossRefPubMedGoogle Scholar
  239. 239.
    Grahovac J, Wells A (2014) Matrikine and matricellular regulators of EGF receptor signaling on cancer cell migration and invasion. Lab Invest 94(1):31–40. CrossRefPubMedGoogle Scholar
  240. 240.
    Da Silva J, Lameiras P, Beljebbar A, Berquand A, Villemin M, Ramont L, Dukic S, Nuzillard JM, Molinari M, Gautier M, Brassart-Pasco S, Brassart B (2018) Structural characterization and in vivo pro-tumor properties of a highly conserved matrikine. Oncotarget 9(25):17839–17857. CrossRefPubMedPubMedCentralGoogle Scholar
  241. 241.
    Scandolera A, Odoul L, Salesse S, Guillot A, Blaise S, Kawecki C, Maurice P, El Btaouri H, Romier-Crouzet B, Martiny L, Debelle L, Duca L (2016) The elastin receptor complex: a unique matricellular receptor with high anti-tumoral potential. Front Pharmacol 7:32. CrossRefPubMedPubMedCentralGoogle Scholar
  242. 242.
    Duca L, Floquet N, Alix AJ, Haye B, Debelle L (2004) Elastin as a matrikine. Crit Rev Oncol Hematol 49(3):235–244. CrossRefPubMedGoogle Scholar
  243. 243.
    Alexander S, Friedl P (2012) Cancer invasion and resistance: interconnected processes of disease progression and therapy failure. Trends Mol Med 18(1):13–26. CrossRefPubMedGoogle Scholar
  244. 244.
    Devreotes P, Horwitz AR (2015) Signaling networks that regulate cell migration. Cold Spring Harb Perspect Biol 7(8):a005959. CrossRefPubMedPubMedCentralGoogle Scholar
  245. 245.
    Ridley AJ, Schwartz MA, Burridge K, Firtel RA, Ginsberg MH, Borisy G, Parsons JT, Horwitz AR (2003) Cell migration: integrating signals from front to back. Science 302(5651):1704–1709. CrossRefPubMedGoogle Scholar
  246. 246.
    Schwartz MA, Horwitz AR (2006) Integrating adhesion, protrusion, and contraction during cell migration. Cell 125(7):1223–1225. CrossRefPubMedGoogle Scholar
  247. 247.
    Vicente-Manzanares M, Horwitz AR (2011) Cell migration: an overview. Methods Mol Biol 769:1–24. CrossRefPubMedGoogle Scholar
  248. 248.
    Vicente-Manzanares M, Webb DJ, Horwitz AR (2005) Cell migration at a glance. J Cell Sci 118(Pt 21):4917–4919. CrossRefPubMedGoogle Scholar
  249. 249.
    Aguilar-Cuenca R, Juanes-Garcia A, Vicente-Manzanares M (2014) Myosin II in mechanotransduction: master and commander of cell migration, morphogenesis, and cancer. Cell Mol Life Sci 71(3):479–492. CrossRefPubMedGoogle Scholar
  250. 250.
    Vicente-Manzanares M, Ma X, Adelstein RS, Horwitz AR (2009) Non-muscle myosin II takes centre stage in cell adhesion and migration. Nat Rev Mol Cell Biol 10(11):778–790. CrossRefPubMedPubMedCentralGoogle Scholar
  251. 251.
    Vicente-Manzanares M, Choi CK, Horwitz AR (2009) Integrins in cell migration–the actin connection. J Cell Sci 122(Pt 2):199–206. CrossRefPubMedGoogle Scholar
  252. 252.
    Yamaguchi H, Condeelis J (2007) Regulation of the actin cytoskeleton in cancer cell migration and invasion. Biochim Biophys Acta 1773(5):642–652. CrossRefPubMedGoogle Scholar
  253. 253.
    Ungefroren H, Witte D, Lehnert H (2018) The role of small GTPases of the Rho/Rac family in TGF-β-induced EMT and cell motility in cancer. Dev Dyn 247(3):451–461. CrossRefPubMedGoogle Scholar
  254. 254.
    Lawson CD, Ridley AJ (2018) Rho GTPase signaling complexes in cell migration and invasion. J Cell Biol 217(2):447–457. CrossRefPubMedPubMedCentralGoogle Scholar
  255. 255.
    Casalou C, Faustino A, Barral DC (2016) Arf proteins in cancer cell migration. Small GTPases 7(4):270–282. CrossRefPubMedPubMedCentralGoogle Scholar
  256. 256.
    Kale VP, Hengst JA, Desai DH, Amin SG, Yun JK (2015) The regulatory roles of ROCK and MRCK kinases in the plasticity of cancer cell migration. Cancer Lett 361(2):185–196. CrossRefPubMedGoogle Scholar
  257. 257.
    Huttenlocher A, Horwitz AR (2011) Integrins in cell migration. Cold Spring Harb Perspect Biol 3(9):a005074. CrossRefPubMedPubMedCentralGoogle Scholar
  258. 258.
    Bays JL, DeMali KA (2017) Vinculin in cell-cell and cell-matrix adhesions. Cell Mol Life Sci 74(16):2999–3009. CrossRefPubMedPubMedCentralGoogle Scholar
  259. 259.
    Goldmann WH (2016) Role of vinculin in cellular mechanotransduction. Cell Biol Int 40(3):241–256. CrossRefPubMedGoogle Scholar
  260. 260.
    Grashoff C, Hoffman BD, Brenner MD, Zhou R, Parsons M, Yang MT, McLean MA, Sligar SG, Chen CS, Ha T, Schwartz MA (2010) Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics. Nature 466(7303):263–266. CrossRefPubMedPubMedCentralGoogle Scholar
  261. 261.
    Ehrlicher AJ, Krishnan R, Guo M, Bidan CM, Weitz DA, Pollak MR (2015) Α-actinin binding kinetics modulate cellular dynamics and force generation. Proc Natl Acad Sci U S A 112(21):6619–6624. CrossRefPubMedPubMedCentralGoogle Scholar
  262. 262.
    Roca-Cusachs P, del Rio A, Puklin-Faucher E, Gauthier NC, Biais N, Sheetz MP (2013) Integrin-dependent force transmission to the extracellular matrix by α-actinin triggers adhesion maturation. Proc Natl Acad Sci USA 110(15):E1361–E1370. CrossRefPubMedGoogle Scholar
  263. 263.
    Carisey A, Tsang R, Greiner AM, Nijenhuis N, Heath N, Nazgiewicz A, Kemkemer R, Derby B, Spatz J, Ballestrem C (2013) Vinculin regulates the recruitment and release of core focal adhesion proteins in a force-dependent manner. Curr Biol 23(4):271–281. CrossRefPubMedPubMedCentralGoogle Scholar
  264. 264.
    Zaidel-Bar R, Milo R, Kam Z, Geiger B (2007) A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions. J Cell Sci 120(Pt 1):137–148. CrossRefPubMedGoogle Scholar
  265. 265.
    Bays JL, Peng X, Tolbert CE, Guilluy C, Angell AE, Pan Y, Superfine R, Burridge K, DeMali KA (2014) Vinculin phosphorylation differentially regulates mechanotransduction at cell-cell and cell-matrix adhesions. J Cell Biol 205(2):251–263. CrossRefPubMedPubMedCentralGoogle Scholar
  266. 266.
    Dobrokhotov O, Samsonov M, Sokabe M, Hirata H (2018) Mechanoregulation and pathology of YAP/TAZ via Hippo and non-Hippo mechanisms. Clin Transl Med 7(1):23. CrossRefPubMedPubMedCentralGoogle Scholar
  267. 267.
    Noguchi S, Saito A, Nagase T (2018) YAP/TAZ signaling as a molecular link between fibrosis and cancer. Int J Mol Sci 19(11):3674. CrossRefPubMedCentralGoogle Scholar
  268. 268.
    Zanconato F, Cordenonsi M, Piccolo S (2016) YAP/TAZ at the roots of cancer. Cancer Cell 29(6):783–803. CrossRefPubMedPubMedCentralGoogle Scholar
  269. 269.
    Palecek SP, Loftus JC, Ginsberg MH, Lauffenburger DA, Horwitz AF (1997) Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness. Nature 385(6616):537–540. CrossRefPubMedGoogle Scholar
  270. 270.
    Gritsenko PG, Ilina O, Friedl P (2012) Interstitial guidance of cancer invasion. J Pathol 226(2):185–199. CrossRefPubMedGoogle Scholar
  271. 271.
    Wolf K, Alexander S, Schacht V, Coussens LM, von Andrian UH, van Rheenen J, Deryugina E, Friedl P (2009) Collagen-based cell migration models in vitro and in vivo. Semin Cell Dev Biol 20(8):931–941. CrossRefPubMedPubMedCentralGoogle Scholar
  272. 272.
    Deng J, Zhao C, Spatz JP, Wei Q (2017) Nanopatterned adhesive, stretchable hydrogel to control ligand spacing and regulate cell spreading and migration. ACS Nano 11(8):8282–8291. CrossRefPubMedGoogle Scholar
  273. 273.
    Arnold M, Hirschfeld-Warneken VC, Lohmuller T, Heil P, Blummel J, Cavalcanti-Adam EA, Lopez-Garcia M, Walther P, Kessler H, Geiger B, Spatz JP (2008) Induction of cell polarization and migration by a gradient of nanoscale variations in adhesive ligand spacing. Nano Lett 8(7):2063–2069. CrossRefPubMedGoogle Scholar
  274. 274.
    Alfano M, Nebuloni M, Allevi R, Zerbi P, Longhi E, Luciano R, Locatelli I, Pecoraro A, Indrieri M, Speziali C, Doglioni C, Milani P, Montorsi F, Salonia A (2016) Linearized texture of three-dimensional extracellular matrix is mandatory for bladder cancer cell invasion. Sci Rep 6:36128. CrossRefPubMedPubMedCentralGoogle Scholar
  275. 275.
    Krause M, Wolf K (2015) Cancer cell migration in 3D tissue: negotiating space by proteolysis and nuclear deformability. Cell Adh Migr 9(5):357–366. CrossRefPubMedPubMedCentralGoogle Scholar
  276. 276.
    Wolf K, Te Lindert M, Krause M, Alexander S, Te Riet J, Willis AL, Hoffman RM, Figdor CG, Weiss SJ, Friedl P (2013) Physical limits of cell migration: control by ECM space and nuclear deformation and tuning by proteolysis and traction force. J Cell Biol 201(7):1069–1084. CrossRefPubMedPubMedCentralGoogle Scholar
  277. 277.
    Denais CM, Gilbert RM, Isermann P, McGregor AL, te Lindert M, Weigelin B, Davidson PM, Friedl P, Wolf K, Lammerding J (2016) Nuclear envelope rupture and repair during cancer cell migration. Science 352(6283):353–358. CrossRefPubMedPubMedCentralGoogle Scholar
  278. 278.
    Petrie RJ, Yamada KM (2016) Multiple mechanisms of 3D migration: the origins of plasticity. Curr Opin Cell Biol 42:7–12. CrossRefPubMedPubMedCentralGoogle Scholar
  279. 279.
    Doyle AD, Petrie RJ, Kutys ML, Yamada KM (2013) Dimensions in cell migration. Curr Opin Cell Biol 25(5):642–649. CrossRefPubMedPubMedCentralGoogle Scholar
  280. 280.
    Petrie RJ, Harlin HM, Korsak LI, Yamada KM (2017) Activating the nuclear piston mechanism of 3D migration in tumor cells. J Cell Biol 216(1):93–100. CrossRefPubMedPubMedCentralGoogle Scholar
  281. 281.
    Friedl P, Locker J, Sahai E, Segall JE (2012) Classifying collective cancer cell invasion. Nat Cell Biol 14(8):777–783. CrossRefPubMedGoogle Scholar
  282. 282.
    Friedl P, Gilmour D (2009) Collective cell migration in morphogenesis, regeneration and cancer. Nat Rev Mol Cell Biol 10(7):445–457. CrossRefPubMedGoogle Scholar
  283. 283.
    Khalil AA, Ilina O, Gritsenko PG, Bult P, Span PN, Friedl P (2017) Collective invasion in ductal and lobular breast cancer associates with distant metastasis. Clin Exp Metastasis 34(6–7):421–429. CrossRefPubMedPubMedCentralGoogle Scholar
  284. 284.
    Das T, Spatz JP (2016) Getting a grip on collective cell migration. Nat Cell Biol 18(12):1265–1267. CrossRefPubMedGoogle Scholar
  285. 285.
    Park JA, Atia L, Mitchel JA, Fredberg JJ, Butler JP (2016) Collective migration and cell jamming in asthma, cancer and development. J Cell Sci 129(18):3375–3383. CrossRefPubMedPubMedCentralGoogle Scholar
  286. 286.
    Ramos Gde O, Bernardi L, Lauxen I, Sant’Ana Filho M, Horwitz AR, Lamers ML (2016) Fibronectin modulates cell adhesion and signaling to promote single cell migration of highly invasive oral squamous cell carcinoma. PLoS ONE 11(3):e0151338. CrossRefPubMedGoogle Scholar
  287. 287.
    Wolf K, Wu YI, Liu Y, Geiger J, Tam E, Overall C, Stack MS, Friedl P (2007) Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion. Nat Cell Biol 9(8):893–904. CrossRefPubMedGoogle Scholar
  288. 288.
    Han T, Kang D, Ji D, Wang X, Zhan W, Fu M, Xin HB, Wang JB (2013) How does cancer cell metabolism affect tumor migration and invasion? Cell Adh Migr 7(5):395–403. CrossRefPubMedPubMedCentralGoogle Scholar
  289. 289.
    Lehmann S, Te Boekhorst V, Odenthal J, Bianchi R, van Helvert S, Ikenberg K, Ilina O, Stoma S, Xandry J, Jiang L, Grenman R, Rudin M, Friedl P (2017) Hypoxia induces a HIF-1-dependent transition from collective-to-amoeboid dissemination in epithelial cancer cells. Curr Biol 27(3):392–400. CrossRefPubMedGoogle Scholar
  290. 290.
    Gaggioli C, Hooper S, Hidalgo-Carcedo C, Grosse R, Marshall JF, Harrington K, Sahai E (2007) Fibroblast-led collective invasion of carcinoma cells with differing roles for RhoGTPases in leading and following cells. Nat Cell Biol 9(12):1392–1400. CrossRefPubMedGoogle Scholar
  291. 291.
    Erpenbeck L, Schön MP (2010) Deadly allies: the fatal interplay between platelets and metastizing cancer cells. Blood 115(17):3427–3436CrossRefPubMedPubMedCentralGoogle Scholar
  292. 292.
    Camerer E (2004) Platelets, protease-activated receptors, and fibrinogen in hematogenous metastasis. Blood 104:397–401CrossRefPubMedGoogle Scholar
  293. 293.
    Weisel JW, Litvinov RI (2017) Fibrin formation, structure and properties. Subcell Biochem 82:405–456. CrossRefPubMedPubMedCentralGoogle Scholar
  294. 294.
    O’Sullivan JM, Preston RJS, Robson T, O’Donnell JS (2018) Emerging Roles for von Willebrand Factor in Cancer Cell Biology. Semin Thromb Hemost 44(2):159–166. CrossRefPubMedGoogle Scholar
  295. 295.
    Bauer AT, Suckau J, Frank K, Desch A, Goertz L, Wagner AH, Hecker M, Goerge T, Umansky L, Beckhove P, Utikal J, Gorzelanny C, Diaz-Valdes N, Umansky V, Schneider SW (2015) von Willebrand factor fibers promote cancer-associated platelet aggregation in malignant melanoma of mice and humans. Blood 125(20):3153–3163. CrossRefPubMedPubMedCentralGoogle Scholar
  296. 296.
    Peinado H, Zhang H, Matei IR, Costa-Silva B, Hoshino A, Rodrigues G, Psaila B, Kaplan RN, Bromberg JF, Kang Y, Bissell MJ, Cox TR, Giaccia AJ, Erler JT, Hiratsuka S, Ghajar CM, Lyden D (2017) Pre-metastatic niches: organ-specific homes for metastases. Nat Rev Cancer 17(5):302–317. CrossRefPubMedGoogle Scholar
  297. 297.
    Psaila B, Lyden D (2009) The metastatic niche: adapting the foreign soil. Nat Rev Cancer 9(4):285–293. CrossRefPubMedPubMedCentralGoogle Scholar
  298. 298.
    Hoshino A, Costa-Silva B, Shen TL, Rodrigues G, Hashimoto A, Tesic Mark M, Molina H, Kohsaka S, Di Giannatale A, Ceder S, Singh S, Williams C, Soplop N, Uryu K, Pharmer L, King T, Bojmar L, Davies AE, Ararso Y, Zhang T, Zhang H, Hernandez J, Weiss JM, Dumont-Cole VD, Kramer K, Wexler LH, Narendran A, Schwartz GK, Healey JH, Sandstrom P, Labori KJ, Kure EH, Grandgenett PM, Hollingsworth MA, de Sousa M, Kaur S, Jain M, Mallya K, Batra SK, Jarnagin WR, Brady MS, Fodstad O, Muller V, Pantel K, Minn AJ, Bissell MJ, Garcia BA, Kang Y, Rajasekhar VK, Ghajar CM, Matei I, Peinado H, Bromberg J, Lyden D (2015) Tumour exosome integrins determine organotropic metastasis. Nature 527(7578):329–335. CrossRefPubMedPubMedCentralGoogle Scholar
  299. 299.
    Geraud C, Koch PS, Damm F, Schledzewski K, Goerdt S (2014) The metastatic cycle: metastatic niches and cancer cell dissemination. J Dtsch Dermatol Ges 12(11):1012–1019. CrossRefPubMedGoogle Scholar
  300. 300.
    Aguado BA, Bushnell GG, Rao SS, Jeruss JS, Shea LD (2017) Engineering the pre-metastatic niche. Nat Biomed Eng 1.
  301. 301.
    Liu Y, Cao X (2016) Characteristics and significance of the pre-metastatic niche. Cancer Cell 30(5):668–681. CrossRefPubMedGoogle Scholar
  302. 302.
    Rezaeeyan H, Shirzad R, McKee TD, Saki N (2018) Role of chemokines in metastatic niche: new insights along with a diagnostic and prognostic approach. APMIS 126(5):359–370. CrossRefPubMedGoogle Scholar
  303. 303.
    Nogues L, Benito-Martin A, Hergueta-Redondo M, Peinado H (2018) The influence of tumour-derived extracellular vesicles on local and distal metastatic dissemination. Mol Aspects Med 60:15–26. CrossRefPubMedGoogle Scholar
  304. 304.
    Lobb RJ, Lima LG, Moller A (2017) Exosomes: key mediators of metastasis and pre-metastatic niche formation. Semin Cell Dev Biol 67:3–10. CrossRefPubMedGoogle Scholar
  305. 305.
    Gartland A, Erler JT, Cox TR (2016) The role of lysyl oxidase, the extracellular matrix and the pre-metastatic niche in bone metastasis. J Bone Oncol 5(3):100–103. CrossRefPubMedPubMedCentralGoogle Scholar
  306. 306.
    Peinado H, Lavotshkin S, Lyden D (2011) The secreted factors responsible for pre-metastatic niche formation: old sayings and new thoughts. Semin Cancer Biol 21(2):139–146. CrossRefPubMedGoogle Scholar
  307. 307.
    Hoye AM, Erler JT (2016) Structural ECM components in the premetastatic and metastatic niche. Am J Physiol Cell Physiol 310(11):C955–C967. CrossRefPubMedGoogle Scholar
  308. 308.
    Descot A, Oskarsson T (2013) The molecular composition of the metastatic niche. Exp Cell Res 319(11):1679–1686. CrossRefPubMedGoogle Scholar
  309. 309.
    Cox TR, Rumney RMH, Schoof EM, Perryman L, Hoye AM, Agrawal A, Bird D, Latif NA, Forrest H, Evans HR, Huggins ID, Lang G, Linding R, Gartland A, Erler JT (2015) The hypoxic cancer secretome induces pre-metastatic bone lesions through lysyl oxidase. Nature 522(7554):106–110. CrossRefPubMedPubMedCentralGoogle Scholar
  310. 310.
    El-Haibi CP, Bell GW, Zhang J, Collmann AY, Wood D, Scherber CM, Csizmadia E, Mariani O, Zhu C, Campagne A, Toner M, Bhatia SN, Irimia D, Vincent-Salomon A, Karnoub AE (2012) Critical role for lysyl oxidase in mesenchymal stem cell-driven breast cancer malignancy. Proc Natl Acad Sci USA 109(43):17460–17465. CrossRefPubMedGoogle Scholar
  311. 311.
    Pickup MW, Laklai H, Acerbi I, Owens P, Gorska AE, Chytil A, Aakre M, Weaver VM, Moses HL (2013) Stromally derived lysyl oxidase promotes metastasis of transforming growth factor-β-deficient mouse mammary carcinomas. Cancer Res 73(17):5336–5346. CrossRefPubMedPubMedCentralGoogle Scholar
  312. 312.
    Jablonska J, Lang S, Sionov RV, Granot Z (2017) The regulation of pre-metastatic niche formation by neutrophils. Oncotarget 8(67):112132–112144. CrossRefPubMedPubMedCentralGoogle Scholar
  313. 313.
    Yumoto K, Eber MR, Berry JE, Taichman RS, Shiozawa Y (2014) Molecular pathways: niches in metastatic dormancy. Clin Cancer Res 20(13):3384–3389. CrossRefPubMedPubMedCentralGoogle Scholar
  314. 314.
    Oskarsson T, Batlle E, Massague J (2014) Metastatic stem cells: sources, niches, and vital pathways. Cell Stem Cell 14(3):306–321. CrossRefPubMedPubMedCentralGoogle Scholar
  315. 315.
    Leprini A, Querze G, Zardi L (1994) Tenascin isoforms: possible targets for diagnosis and therapy of cancer and mechanisms regulating their expression. Perspect Dev Neurobiol 2(1):117–123PubMedGoogle Scholar
  316. 316.
    Nicolo G, Salvi S, Oliveri G, Borsi L, Castellani P, Zardi L (1990) Expression of tenascin and of the ED-B containing oncofetal fibronectin isoform in human cancer. Cell Differ Dev 32(3):401–408CrossRefPubMedGoogle Scholar
  317. 317.
    Vandooren J, Opdenakker G, Loadman PM, Edwards DR (2016) Proteases in cancer drug delivery. Adv Drug Deliv Rev 97:144–155. CrossRefPubMedGoogle Scholar
  318. 318.
    Piperigkou Z, Manou D, Karamanou K, Theocharis AD (2018) Strategies to target matrix metalloproteinases as therapeutic approach in cancer. Methods Mol Biol 1731:325–348. CrossRefPubMedGoogle Scholar
  319. 319.
    Gingras D, Batist G, Beliveau R (2001) AE-941 (Neovastat): a novel multifunctional antiangiogenic compound. Expert Rev Anticancer Ther 1(3):341–347. CrossRefPubMedGoogle Scholar
  320. 320.
    Gingras D, Boivin D, Deckers C, Gendron S, Barthomeuf C, Beliveau R (2003) Neovastat–a novel antiangiogenic drug for cancer therapy. Anticancer Drugs 14(2):91–96. CrossRefPubMedGoogle Scholar
  321. 321.
    Lu C, Lee JJ, Komaki R, Herbst RS, Feng L, Evans WK, Choy H, Desjardins P, Esparaz BT, Truong MT, Saxman S, Kelaghan J, Bleyer A, Fisch MJ (2010) Chemoradiotherapy with or without AE-941 in stage III non-small cell lung cancer: a randomized phase III trial. J Natl Cancer Inst 102(12):859–865. CrossRefPubMedPubMedCentralGoogle Scholar
  322. 322.
    Rizvi NA, Humphrey JS, Ness EA, Johnson MD, Gupta E, Williams K, Daly DJ, Sonnichsen D, Conway D, Marshall J, Hurwitz H (2004) A phase I study of oral BMS-275291, a novel nonhydroxamate sheddase-sparing matrix metalloproteinase inhibitor, in patients with advanced or metastatic cancer. Clin Cancer Res 10(6):1963–1970CrossRefPubMedGoogle Scholar
  323. 323.
    Leighl NB, Paz-Ares L, Douillard JY, Peschel C, Arnold A, Depierre A, Santoro A, Betticher DC, Gatzemeier U, Jassem J, Crawford J, Tu D, Bezjak A, Humphrey JS, Voi M, Galbraith S, Hann K, Seymour L, Shepherd FA (2005) Randomized phase III study of matrix metalloproteinase inhibitor BMS-275291 in combination with paclitaxel and carboplatin in advanced non-small-cell lung cancer: National Cancer Institute of Canada-Clinical Trials Group Study BR.18. J Clin Oncol 23(12):2831–2839. CrossRefPubMedGoogle Scholar
  324. 324.
    Hirte H, Vergote IB, Jeffrey JR, Grimshaw RN, Coppieters S, Schwartz B, Tu D, Sadura A, Brundage M, Seymour L (2006) A phase III randomized trial of BAY 12-9566 (tanomastat) as maintenance therapy in patients with advanced ovarian cancer responsive to primary surgery and paclitaxel/platinum containing chemotherapy: a National Cancer Institute of Canada Clinical Trials Group Study. Gynecol Oncol 102(2):300–308. CrossRefPubMedGoogle Scholar
  325. 325.
    Hande KR, Collier M, Paradiso L, Stuart-Smith J, Dixon M, Clendeninn N, Yeun G, Alberti D, Binger K, Wilding G (2004) Phase I and pharmacokinetic study of prinomastat, a matrix metalloprotease inhibitor. Clin Cancer Res 10(3):909–915CrossRefPubMedGoogle Scholar
  326. 326.
    Bissett D, O’Byrne KJ, von Pawel J, Gatzemeier U, Price A, Nicolson M, Mercier R, Mazabel E, Penning C, Zhang MH, Collier MA, Shepherd FA (2005) Phase III study of matrix metalloproteinase inhibitor prinomastat in non-small-cell lung cancer. J Clin Oncol 23(4):842–849. CrossRefPubMedGoogle Scholar
  327. 327.
    Paemen L, Martens E, Masure S, Opdenakker G (1995) Monoclonal antibodies specific for natural human neutrophil gelatinase B used for affinity purification, quantitation by two-site ELISA and inhibition of enzymatic activity. Eur J Biochem 234(3):759–765CrossRefPubMedGoogle Scholar
  328. 328.
    Martens E, Leyssen A, Van Aelst I, Fiten P, Piccard H, Hu J, Descamps FJ, Van den Steen PE, Proost P, Van Damme J, Liuzzi GM, Riccio P, Polverini E, Opdenakker G (2007) A monoclonal antibody inhibits gelatinase B/MMP-9 by selective binding to part of the catalytic domain and not to the fibronectin or zinc binding domains. Biochim Biophys Acta 1770(2):178–186. CrossRefPubMedGoogle Scholar
  329. 329.
    Devy L, Huang L, Naa L, Yanamandra N, Pieters H, Frans N, Chang E, Tao Q, Vanhove M, Lejeune A, van Gool R, Sexton DJ, Kuang G, Rank D, Hogan S, Pazmany C, Ma YL, Schoonbroodt S, Nixon AE, Ladner RC, Hoet R, Henderikx P, Tenhoor C, Rabbani SA, Valentino ML, Wood CR, Dransfield DT (2009) Selective inhibition of matrix metalloproteinase-14 blocks tumor growth, invasion, and angiogenesis. Cancer Res 69(4):1517–1526. CrossRefPubMedGoogle Scholar
  330. 330.
    Lemaitre V, D’Armiento J (2006) Matrix metalloproteinases in development and disease. Birth Defects Res C 78(1):1–10. CrossRefGoogle Scholar
  331. 331.
    Li L, Li H (2013) Role of microRNA-mediated MMP regulation in the treatment and diagnosis of malignant tumors. Cancer Biol Ther 14(9):796–805. CrossRefPubMedPubMedCentralGoogle Scholar
  332. 332.
    Gabriely G, Wurdinger T, Kesari S, Esau CC, Burchard J, Linsley PS, Krichevsky AM (2008) MicroRNA 21 promotes glioma invasion by targeting matrix metalloproteinase regulators. Mol Cell Biol 28(17):5369–5380. CrossRefPubMedPubMedCentralGoogle Scholar
  333. 333.
    Costa PM, Cardoso AL, Custodia C, Cunha P, Pereira de Almeida L, Pedroso de Lima MC (2015) MiRNA-21 silencing mediated by tumor-targeted nanoparticles combined with sunitinib: a new multimodal gene therapy approach for glioblastoma. J Control Release 207:31–39. CrossRefPubMedGoogle Scholar
  334. 334.
    Chan N, Willis A, Kornhauser N, Ward MM, Lee SB, Nackos E, Seo BR, Chuang E, Cigler T, Moore A, Donovan D, Vallee Cobham M, Fitzpatrick V, Schneider S, Wiener A, Guillaume-Abraham J, Aljom E, Zelkowitz R, Warren JD, Lane ME, Fischbach C, Mittal V, Vahdat L (2017) Influencing the tumor microenvironment: a phase II study of copper depletion using tetrathiomolybdate in patients with breast cancer at high risk for recurrence and in preclinical models of lung metastases. Clin Cancer Res 23(3):666–676. CrossRefPubMedGoogle Scholar
  335. 335.
    Hecht JR, Benson AB 3rd, Vyushkov D, Yang Y, Bendell J, Verma U (2017) A phase II, randomized, double-blind, placebo-controlled study of simtuzumab in combination with FOLFIRI for the second-line treatment of metastatic KRAS mutant colorectal adenocarcinoma. Oncologist 22(3):243-e223. CrossRefGoogle Scholar
  336. 336.
    Benson AB 3rd, Wainberg ZA, Hecht JR, Vyushkov D, Dong H, Bendell J, Kudrik F (2017) A phase II randomized, double-blind, placebo-controlled study of simtuzumab or placebo in combination with gemcitabine for the first-line treatment of pancreatic adenocarcinoma. Oncologist 22(3):241-e215. CrossRefGoogle Scholar
  337. 337.
    Barry-Hamilton V, Spangler R, Marshall D, McCauley S, Rodriguez HM, Oyasu M, Mikels A, Vaysberg M, Ghermazien H, Wai C, Garcia CA, Velayo AC, Jorgensen B, Biermann D, Tsai D, Green J, Zaffryar-Eilot S, Holzer A, Ogg S, Thai D, Neufeld G, Van Vlasselaer P, Smith V (2010) Allosteric inhibition of lysyl oxidase-like-2 impedes the development of a pathologic microenvironment. Nat Med 16(9):1009–1017. CrossRefPubMedGoogle Scholar
  338. 338.
    Rodriguez HM, Vaysberg M, Mikels A, McCauley S, Velayo AC, Garcia C, Smith V (2010) Modulation of lysyl oxidase-like 2 enzymatic activity by an allosteric antibody inhibitor. J Biol Chem 285(27):20964–20974. CrossRefPubMedPubMedCentralGoogle Scholar
  339. 339.
    Rasmussen HS, McCann PP (1997) Matrix metalloproteinase inhibition as a novel anticancer strategy: a review with special focus on batimastat and marimastat. Pharmacol Ther 75(1):69–75CrossRefPubMedGoogle Scholar
  340. 340.
    Cathcart J, Pulkoski-Gross A, Cao J (2015) Targeting matrix metalloproteinases in cancer: bringing new life to old ideas. Genes Dis 2(1):26–34. CrossRefPubMedPubMedCentralGoogle Scholar
  341. 341.
    Rao BG (2005) Recent developments in the design of specific matrix metalloproteinase inhibitors aided by structural and computational studies. Curr Pharm Des 11(3):295–322CrossRefPubMedGoogle Scholar
  342. 342.
    Au JL, Yeung BZ, Wientjes MG, Lu Z, Wientjes MG (2016) Delivery of cancer therapeutics to extracellular and intracellular targets: determinants, barriers, challenges and opportunities. Adv Drug Deliv Rev 97:280–301. CrossRefPubMedGoogle Scholar
  343. 343.
    Rodriguez-Cabello JC, Arias FJ, Rodrigo MA, Girotti A (2016) Elastin-like polypeptides in drug delivery. Adv Drug Deliv Rev 97:85–100. CrossRefPubMedGoogle Scholar
  344. 344.
    Arosio D, Casagrande C (2016) Advancement in integrin facilitated drug delivery. Adv Drug Deliv Rev 97:111–143. CrossRefPubMedGoogle Scholar
  345. 345.
    Multhaupt HA, Leitinger B, Gullberg D, Couchman JR (2016) Extracellular matrix component signaling in cancer. Adv Drug Deliv Rev 97:28–40. CrossRefPubMedGoogle Scholar
  346. 346.
    Hinderer S, Layland SL, Schenke-Layland K (2016) ECM and ECM-like materials—biomaterials for applications in regenerative medicine and cancer therapy. Adv Drug Deliv Rev 97:260–269. CrossRefPubMedGoogle Scholar
  347. 347.
    Celia-Terrassa T, Kang Y (2018) Metastatic niche functions and therapeutic opportunities. Nat Cell Biol 20(8):868–877. CrossRefPubMedGoogle Scholar
  348. 348.
    Ordonez-Moran P, Huelsken J (2014) Complex metastatic niches: already a target for therapy? Curr Opin Cell Biol 31:29–38. CrossRefPubMedGoogle Scholar
  349. 349.
    Horton ER, Astudillo P, Humphries MJ, Humphries JD (2016) Mechanosensitivity of integrin adhesion complexes: role of the consensus adhesome. Exp Cell Res 343(1):7–13. CrossRefPubMedGoogle Scholar
  350. 350.
    Murphy DA, Courtneidge SA (2011) The ‘ins’ and ‘outs’ of podosomes and invadopodia: characteristics, formation and function. Nat Rev Mol Cell Biol 12(7):413–426. CrossRefPubMedPubMedCentralGoogle Scholar
  351. 351.
    Leitinger B, Hohenester E (2007) Mammalian collagen receptors. Matrix Biol 26(3):146–155. CrossRefPubMedGoogle Scholar
  352. 352.
    Torres PH, Sousa GL, Pascutti PG (2011) Structural analysis of the N-terminal fragment of the antiangiogenic protein endostatin: a molecular dynamics study. Proteins 79(9):2684–2692. CrossRefPubMedGoogle Scholar
  353. 353.
    Oudart JB, Monboisse JC, Maquart FX, Brassart B, Brassart-Pasco S, Ramont L (2017) Type XIX collagen: a new partner in the interactions between tumor cells and their microenvironment. Matrix Biol 57–58:169–177. CrossRefPubMedGoogle Scholar
  354. 354.
    Nagase H, Fields GB (1996) Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides. Biopolymers 40(4):399–416.;2-R CrossRefPubMedGoogle Scholar
  355. 355.
    Mithieux SM, Weiss AS (2005) Elastin. Adv Protein Chem 70:437–461. CrossRefPubMedGoogle Scholar
  356. 356.
    Wells JM, Gaggar A, Blalock JE (2015) MMP generated matrikines. Matrix Biol 44–46:122–129. CrossRefPubMedPubMedCentralGoogle Scholar
  357. 357.
    Cain SA, Mularczyk EJ, Singh M, Massam-Wu T, Kielty CM (2016) ADAMTS-10 and -6 differentially regulate cell-cell junctions and focal adhesions. Sci Rep 6:35956. CrossRefPubMedPubMedCentralGoogle Scholar
  358. 358.
    Bax DV, Mahalingam Y, Cain S, Mellody K, Freeman L, Younger K, Shuttleworth CA, Humphries MJ, Couchman JR, Kielty CM (2007) Cell adhesion to fibrillin-1: identification of an Arg-Gly-Asp-dependent synergy region and a heparin-binding site that regulates focal adhesion formation. J Cell Sci 120(Pt 8):1383–1392. CrossRefPubMedGoogle Scholar
  359. 359.
    Jovanovic J, Iqbal S, Jensen S, Mardon H, Handford P (2008) Fibrillin-integrin interactions in health and disease. Biochem Soc Trans 36(Pt 2):257–262. CrossRefPubMedGoogle Scholar
  360. 360.
    Joshi R, Goihberg E, Ren W, Pilichowska M, Mathew P (2017) Proteolytic fragments of fibronectin function as matrikines driving the chemotactic affinity of prostate cancer cells to human bone marrow mesenchymal stromal cells via the α5β1 integrin. Cell Adh Migr 11(4):305–315. CrossRefPubMedGoogle Scholar
  361. 361.
    White ES, Baralle FE, Muro AF (2008) New insights into form and function of fibronectin splice variants. J Pathol 216(1):1–14. CrossRefPubMedPubMedCentralGoogle Scholar
  362. 362.
    Faron G, Balepa L, Parra J, Fils JF, Gucciardo L (2018) The fetal fibronectin test: 25 years after its development, what is the evidence regarding its clinical utility? A systematic review and meta-analysis. J Matern Fetal Neonatal Med. CrossRefPubMedGoogle Scholar
  363. 363.
    Sawicka KM, Seeliger M, Musaev T, Macri LK, Clark RA (2015) Fibronectin interaction and enhancement of growth factors: importance for wound healing. Adv Wound Care (New Rochelle) 4(8):469–478. CrossRefGoogle Scholar
  364. 364.
    Wang Y, Ni H (2016) Fibronectin maintains the balance between hemostasis and thrombosis. Cell Mol Life Sci 73(17):3265–3277. CrossRefPubMedGoogle Scholar
  365. 365.
    Mercuri FA, Maciewicz RA, Tart J, Last K, Fosang AJ (2000) Mutations in the interglobular domain of aggrecan alter matrix metalloproteinase and aggrecanase cleavage patterns Evidence that matrix metalloproteinase cleavage interferes with aggrecanase activity. J Biol Chem 275(42):33038–33045CrossRefPubMedGoogle Scholar
  366. 366.
    Viapiano MS, Hockfield S, Matthews RT (2008) BEHAB/brevican requires ADAMTS-mediated proteolytic cleavage to promote glioma invasion. J Neurooncol 88(3):261–272. CrossRefPubMedPubMedCentralGoogle Scholar
  367. 367.
    Demircan K, Topcu V, Takigawa T, Akyol S, Yonezawa T, Ozturk G, Ugurcu V, Hasgul R, Yigitoglu MR, Akyol O, McCulloch DR, Hirohata S (2014) ADAMTS4 and ADAMTS5 knockout mice are protected from versican but not aggrecan or brevican proteolysis during spinal cord injury. Biomed Res Int 2014:693746. CrossRefPubMedPubMedCentralGoogle Scholar
  368. 368.
    Li H, Leung TC, Hoffman S, Balsamo J, Lilien J (2000) Coordinate regulation of cadherin and integrin function by the chondroitin sulfate proteoglycan neurocan. J Cell Biol 149(6):1275–1288CrossRefPubMedPubMedCentralGoogle Scholar
  369. 369.
    Mohan V, Wyatt EV, Gotthard I, Phend KD, Diestel S, Duncan BW, Weinberg RJ, Tripathy A, Maness PF (2018) Neurocan inhibits semaphorin 3F induced dendritic spine remodeling through NrCAM in cortical neurons. Front Cell Neurosci 12:346. CrossRefPubMedPubMedCentralGoogle Scholar
  370. 370.
    Wu Y, Chen L, Zheng PS, Yang BB (2002) β 1-Integrin-mediated glioma cell adhesion and free radical-induced apoptosis are regulated by binding to a C-terminal domain of PG-M/versican. J Biol Chem 277(14):12294–12301. CrossRefPubMedGoogle Scholar
  371. 371.
    Overall CM (2002) Molecular determinants of metalloproteinase substrate specificity: matrix metalloproteinase substrate binding domains, modules, and exosites. Mol Biotechnol 22(1):51–86. CrossRefPubMedGoogle Scholar
  372. 372.
    Iozzo RV, Moscatello DK, McQuillan DJ, Eichstetter I (1999) Decorin is a biological ligand for the epidermal growth factor receptor. J Biol Chem 274(8):4489–4492CrossRefPubMedGoogle Scholar
  373. 373.
    Moreth K, Iozzo RV, Schaefer L (2012) Small leucine-rich proteoglycans orchestrate receptor crosstalk during inflammation. Cell Cycle 11(11):2084–2091. CrossRefPubMedPubMedCentralGoogle Scholar
  374. 374.
    Goldoni S, Humphries A, Nystrom A, Sattar S, Owens RT, McQuillan DJ, Ireton K, Iozzo RV (2009) Decorin is a novel antagonistic ligand of the Met receptor. J Cell Biol 185(4):743–754. CrossRefPubMedPubMedCentralGoogle Scholar
  375. 375.
    Khan GA, Girish GV, Lala N, Di Guglielmo GM, Lala PK (2011) Decorin is a novel VEGFR-2-binding antagonist for the human extravillous trophoblast. Mol Endocrinol 25(8):1431–1443. CrossRefPubMedPubMedCentralGoogle Scholar
  376. 376.
    Hausser H, Wedekind P, Sperber T, Peters R, Hasilik A, Kresse H (1996) Isolation and cellular localization of the decorin endocytosis receptor. Eur J Cell Biol 71(4):325–331PubMedGoogle Scholar
  377. 377.
    Nastase MV, Young MF, Schaefer L (2012) Biglycan: a multivalent proteoglycan providing structure and signals. J Histochem Cytochem 60(12):963–975. CrossRefPubMedPubMedCentralGoogle Scholar
  378. 378.
    Grindel B, Li Q, Arnold R, Petros J, Zayzafoon M, Muldoon M, Stave J, Chung LW, Farach-Carson MC (2016) Perlecan/HSPG2 and matrilysin/MMP-7 as indices of tissue invasion: tissue localization and circulating perlecan fragments in a cohort of 288 radical prostatectomy patients. Oncotarget 7(9):10433–10447. CrossRefPubMedPubMedCentralGoogle Scholar
  379. 379.
    Eble JA, Wucherpfennig KW, Gauthier L, Dersch P, Krukonis E, Isberg RR, Hemler ME (1998) Recombinant soluble human α3β1 integrin: purification, processing, regulation, and specific binding to laminin-5 and invasin in a mutually exclusive manner. Biochemistry 37(31):10945–10955. CrossRefPubMedGoogle Scholar
  380. 380.
    Kaasboll OJ, Gadicherla AK, Wang JH, Monsen VT, Hagelin EMV, Dong MQ, Attramadal H (2018) Connective tissue growth factor (CCN2) is a matricellular preproprotein controlled by proteolytic activation. J Biol Chem 293(46):17953–17970. CrossRefPubMedGoogle Scholar
  381. 381.
    Su JL, Chiou J, Tang CH, Zhao M, Tsai CH, Chen PS, Chang YW, Chien MH, Peng CY, Hsiao M, Kuo ML, Yen ML (2010) CYR61 regulates BMP-2-dependent osteoblast differentiation through the αvβ3 integrin/integrin-linked kinase/ERK pathway. J Biol Chem 285(41):31325–31336. CrossRefPubMedPubMedCentralGoogle Scholar
  382. 382.
    Crockett JC, Schutze N, Tosh D, Jatzke S, Duthie A, Jakob F, Rogers MJ (2007) The matricellular protein CYR61 inhibits osteoclastogenesis by a mechanism independent of αvβ3 and αvβ5. Endocrinology 148(12):5761–5768. CrossRefPubMedGoogle Scholar
  383. 383.
    Chen CC, Young JL, Monzon RI, Chen N, Todorovic V, Lau LF (2007) Cytotoxicity of TNFα is regulated by integrin-mediated matrix signaling. EMBO J 26(5):1257–1267. CrossRefPubMedPubMedCentralGoogle Scholar
  384. 384.
    Tsai HC, Chang AC, Tsai CH, Huang YL, Gan L, Chen CK, Liu SC, Huang TY, Fong YC, Tang CH (2019) CCN2 promotes drug resistance in osteosarcoma by enhancing ABCG2 expression. J Cell Physiol 234(6):9297–9307. CrossRefPubMedGoogle Scholar
  385. 385.
    Babic AM, Chen CC, Lau LF (1999) Fisp12/mouse connective tissue growth factor mediates endothelial cell adhesion and migration through integrin αvβ3, promotes endothelial cell survival, and induces angiogenesis in vivo. Mol Cell Biol 19(4):2958–2966CrossRefPubMedPubMedCentralGoogle Scholar
  386. 386.
    Scherberich A, Tucker RP, Degen M, Brown-Luedi M, Andres AC, Chiquet-Ehrismann R (2005) Tenascin-W is found in malignant mammary tumors, promotes α8 integrin-dependent motility and requires p38MAPK activity for BMP-2 and TNF-α induced expression in vitro. Oncogene 24(9):1525–1532. CrossRefPubMedGoogle Scholar
  387. 387.
    Martina E, Degen M, Ruegg C, Merlo A, Lino MM, Chiquet-Ehrismann R, Brellier F (2010) Tenascin-W is a specific marker of glioma-associated blood vessels and stimulates angiogenesis in vitro. FASEB J 24(3):778–787. CrossRefPubMedPubMedCentralGoogle Scholar
  388. 388.
    Gillan L, Matei D, Fishman DA, Gerbin CS, Karlan BY, Chang DD (2002) Periostin secreted by epithelial ovarian carcinoma is a ligand for αVβ3 and αVβ5 integrins and promotes cell motility. Cancer Res 62(18):5358–5364PubMedGoogle Scholar
  389. 389.
    Kakizaki Y, Makino N, Tozawa T, Honda T, Matsuda A, Ikeda Y, Ito M, Saito Y, Kimura W, Ueno Y (2016) Stromal fibrosis and expression of matricellular proteins correlate with histological grade of intraductal papillary mucinous neoplasm of the pancreas. Pancreas 45(8):1145–1152. CrossRefPubMedPubMedCentralGoogle Scholar
  390. 390.
    Thijssen VL, Rabinovich GA, Griffioen AW (2013) Vascular galectins: regulators of tumor progression and targets for cancer therapy. Cytokine Growth Factor Rev 24(6):547–558. CrossRefPubMedGoogle Scholar
  391. 391.
    Mendez-Huergo SP, Blidner AG, Rabinovich GA (2017) Galectins: emerging regulatory checkpoints linking tumor immunity and angiogenesis. Curr Opin Immunol 45:8–15. CrossRefPubMedGoogle Scholar
  392. 392.
    Agnihotri R, Crawford HC, Haro H, Matrisian LM, Havrda MC, Liaw L (2001) Osteopontin, a novel substrate for matrix metalloproteinase-3 (stromelysin-1) and matrix metalloproteinase-7 (matrilysin). J Biol Chem 276(30):28261–28267. CrossRefPubMedGoogle Scholar
  393. 393.
    Takafuji V, Forgues M, Unsworth E, Goldsmith P, Wang XW (2007) An osteopontin fragment is essential for tumor cell invasion in hepatocellular carcinoma. Oncogene 26(44):6361–6371. CrossRefPubMedGoogle Scholar
  394. 394.
    Furger KA, Allan AL, Wilson SM, Hota C, Vantyghem SA, Postenka CO, Al-Katib W, Chambers AF, Tuck AB (2003) Β3 integrin expression increases breast carcinoma cell responsiveness to the malignancy-enhancing effects of osteopontin. Mol Cancer Res 1(11):810–819PubMedGoogle Scholar
  395. 395.
    Rangaswami H, Bulbule A, Kundu GC (2006) Osteopontin: role in cell signaling and cancer progression. Trends Cell Biol 16(2):79–87. CrossRefPubMedGoogle Scholar
  396. 396.
    Teramoto H, Castellone MD, Malek RL, Letwin N, Frank B, Gutkind JS, Lee NH (2005) Autocrine activation of an osteopontin-CD44-Rac pathway enhances invasion and transformation by H-RasV12. Oncogene 24(3):489–501. CrossRefPubMedGoogle Scholar
  397. 397.
    Ye QH, Qin LX, Forgues M, He P, Kim JW, Peng AC, Simon R, Li Y, Robles AI, Chen Y, Ma ZC, Wu ZQ, Ye SL, Liu YK, Tang ZY, Wang XW (2003) Predicting hepatitis B virus-positive metastatic hepatocellular carcinomas using gene expression profiling and supervised machine learning. Nat Med 9(4):416–423. CrossRefPubMedGoogle Scholar

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© Springer Nature B.V. 2019

Authors and Affiliations

  1. 1.Institute of Physiological Chemistry and PathobiochemistryUniversity of MünsterMünsterGermany

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