Abstract
Cell adhesion molecules, also termed cell adhesion receptors, are one of three classes of macromolecules – along with extracellular matrix molecules and adhesion plaque proteins – that mediate cell adhesion, an activity which is critical for the commencement and maintenance of the three-dimensional structure and normal function of tissues.1,2 Cell adhesion molecules are predominantly transmembrane glycoproteins that mediate binding to extracellular matrix molecules or to associated receptors on other cells, in a manner that determines the specificity of cell–cell or cell–extracellular matrix interactions.1 There are five families of adhesion receptors – integrins, cadherins, immunoglobulin cell adhesion molecules (Ig CAMs), selectins, and CD44.1,3–9 Complexes formed by cell adhesion receptors are not static, but are dynamic units capable of obtai-ning and incorporating extracellular environmental signals, and are indeed the foundation of two-way signaling between the cell and its external environment.1,10 These cell adhesion molecule families are also involved with signaling between the interior and exterior of the cell, and as such are important in cell growth, proliferation, spatial organization, motility, migration, signaling, differentiation, apoptosis, and gene transcription in normal physiological growth and development as well as in pathological conditions such as inflammation and wound healing.5,9
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Aplin AE, Howe A, Alahari SK, Juliano RL. Signal transduction and signal modulation by cell adhesion receptors: the role of integrins, cadherins, immunoglobulin-cell adhesion molecules, and selectins. Pharmacol Rev. 1998;50:197–263.
Gumbiner BM. Cell adhesion: the molecular basis of tissue architecture and morphogenesis. Cell. 1996;84:345–357.
Gogali A, Charalabopoulos K, Constantopoulos S. Integrin receptors in primary lung cancer. Exp Oncol. 2004;26:106–110.
Petruzzelli L, Takami M, Humes HD. Structure and function of cell adhesion molecules. Am J Med. 1999;106:467–476.
Nair KS, Naidoo R, Chetty R. Expression of cell adhesion molecules in oesophageal carcinoma and its prognostic value. J Clin Pathol. 2005;58:343–351.
Charalabopoulos K, Gogali A, Kostoula OK, Constantopoulos SH. Cadherin superfamily of adhesion molecules in primary lung cancer. Exp Oncol. 2004;26:256–260.
Meyer T, Hart IR. Mechanisms of tumour metastasis. Eur J Cancer. 1998;34:214–221.
Mousa SA. Cell adhesion molecules: potential therapeutic & diagnostic implications. Mol Biotechnol. 2008;38:33–40.
Lyons AJ, Jones J. Cell adhesion molecules, the extracellular matrix and oral squamous carcinoma. Int J Oral Maxillofac Surg. 2007;36:671–679.
Rosales C, O’Brian V, Kornberg L, Juliano RL. Signal transduction by cell adhesion receptors. Biochim Biophys Acta. 1995;1242:77–98.
Nicolson GL. Cancer metastasis: tumor cell and host organ properties important in metastasis to specific secondary sites. Biochim Biophys Acta. 1988;948:175–224.
Hynes RO. Integrins: versatility, modulation, and signalling in cell adhesion. Cell. 1992;69:11–25.
Han SW, Roman J. COX-2 inhibitors suppress integrin α5 expression in human lung carcinoma cells through activation of Erk: involvement of Sp1 and AP-1 sites. Int J Cancer. 2005;116:536–546.
Watt FM. Role of integrins in regulating epidermal adhesion, growth and differentiation. EMBO J. 2002;21:3919–3926.
Okegawa T, Li Y, Pong RC, Hsieh JT. Cell adhesion proteins as tumor suppressors. J Urol. 2002;167:1836–1843.
Mukhopadhyay NK, Gordon GJ, Chen CJ, et al. Activation of focal adhesion kinase in human lung cancer cells involves multiple and potentially parallel signaling events. J Cell Mol Med. 2005;9:387–397.
Damjanovich L, Albelda SM, Mette SA. Distribution of integrin cell adhesion receptors in normal and malignant lung tissue. Am J Respir Cell Mol Biol. 1992;6:197–206.
Hanby AN, Gilet CE, Pignatelli M, Stamp GW. Beta1 and beta4 integrin expression in metacarn and formalin fixed material from in situ ductal carcinoma of the breast. J Pathol. 1993;171:257–262.
Kitayama J, Nayawa H, Nakayama H, et al. Functional expression of beta1 and beta2 integrins on tumor infiltrating lymphocytes (TILs) in colorectal cancer. J Gastroenterol. 1999;34:327–333.
Bankhof H, Stein V, Remberger K. Differential expression of a6 and a2 very late-antigen integrins in the normal, hyperplastic and neoplastic prostate. Hum Pathol. 1993;24:243–248.
Damkisson YP, Wilding JC, Filipe M, Hall PA, Pignatelli M. Cell–matrix interactions in gastric carcinoma. J Pathol. 1993;169:120.
Elenrieder V, Alder G, Gress TM. Invasion and metastasis in pancreatic cancer. Ann Oncol. 1999;4:46–50.
Volpes R, Van der Oord J, Pesmet VJ. Distribution of the VLA family of integrins in normal and pathological human liver tissue. Gastroenterology. 1991;101:200–206.
Bichler KH, Wechsel HW. The problematic nature of metastasized cell carcinoma. Anticancer Res. 1999;19:1463–1466.
Stamb GW, Pignatelli M. Distribution of β1, α1, α2 and α3 integrin chains in basal cell carcinomas. J Pathol. 1991;103:307–313.
Strobel T, Cannisha SA. Beta-1 integrins partly mediate binding of ovarian cancer cells to perimetral mesothelium in vitro. Gynecol Oncol. 1999;73:362–367.
Vessey BA, Albelda S, Buck CA, et al. Distribution of integrin cell adhesion molecules in endometrial cancer. Am J Pathol. 1995;146:717–726.
Hehlgans S, Haase M, Cordes N. Signalling via integrins: implications for cell survival and anticancer strategies. Biochim Biophys Acta. 2007;1775:163–180.
Yamada KM, Kennedy DW, Yamada SS, et al. Monoclonal antibody and synthetic peptide inhibitors of human tumor cell migration. Cancer Res. 1990;50:4485–4496.
Albelda SM, Mette SA, Elder DE, et al. Integrin distribution in malignant melanoma: association of the beta 3 subunit with tumor progression. Cancer Res. 1990;50:6757–6764.
Hamann A, Andrew DP, Pablonski-Westrich D, Holzmann B, Butcher EC. Role of alpha-4-integrins in lymphocyte homing to mucosal tissues in vivo. J Immunol. 1994;152:3282–3293.
Yednock TA, Cannon C, Fritz LC, et al. Prevention of experimental autoimmune encephalomyelitis by antibodies against alpha-4-beta-1 integrin. Nature. 1992;356:63–66.
Springer TA. Traffic signals on endothelium for lymphocyte recirculation and leukocyte emigration. Annu Rev Physiol. 1995;57:827–872.
Hartmann TJ, Burger JA, Gloded A, Fujii N, Burger M. CXCR4 chemokine receptor and integrin signaling co-operate in mediating adhesion and chemoresistance in small cell lung cancer (SCLC) cells. Oncogene. 2005;24:4462–4471.
Dai DL, Makretsov N, Campos EI, et al. Increased expression of integrin-linked kinase is correlated with melanoma progression and poor patient survival. Clin Cancer Res. 2003;9:4409–4414.
Graff JR, Deddens JA, Konicek BW, et al. Integrin-linked kinase expression increases with prostate tumor grade. Clin Cancer Res. 2001;7:1987–1991.
Marotta A, Tan C, Gray V, et al. Dysregulation of integrin-linked kinase (ILK) signaling in colonic polyposis. Oncogene. 2001;20:6250–6257.
Takanami I. Increased expression of integrin-linked kinase is associated with shorter survival in non-small cell lung cancer. BMC Cancer. 2005;5:1.
Dedhar S. Cell-substrate interactions and signaling through ILK. Curr Opin Cell Biol. 2000;12:250–256.
Wu C, Dedhar S. Integrin-linked kinase (ILK) and its interactors: a new paradigm for the coupling of extracellular matrix to actin cytoskeleton and signaling complexes. J Cell Biol. 2001;155: 505–510.
Liotta LA, Stetler-Stevenson WG. Tumor invasion and metastasis: an imbalance of positive and negative regulation. Cancer Res. 1991;51:5054–5059.
Furuta SM, Ilic D, Kanazawa S, et al. Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase FAK. Oncogene. 1995;11:1989–1995.
Carelli S, Zadra G, Vaira V, et al. Up-regulation of focal adhesion kinase in non-small cell lung cancer. Lung Cancer. 2006;53:263–271.
Sanders MA, Basson MD. Collagen IV-dependent ERK activation in human Caco-2 intestinal epithelial cells requires focal adhesion kinase. J Biol Chem. 2000;275:38040–38047.
Guan JL, Shalloway D. Regulation of pp1256FAK both by cellular adhesion and by oncogenic transformation. Nature. 1992;358:690–692.
Bhattacharjee A, Richards WG, Staunton J, et al. Classification of human lung carcinomas by mRNA expression profiling reveals distinct adenocarcinoma subclasses. Proc Natl Acad Sci USA. 2001;98:13790–13795.
Yeoh EJ, Ross ME, Shurtleff SA, et al. Classification, subtype discovery, and prediction of outcome in pediatric acute lymphoblastic leukemia by gene expression profiling. Cancer Cell. 2002; 133-143.
Agochiya M, Brunton VG, Owens DW, et al. Increased dosage and amplification of the focal adhesion kinase gene in human cancer cells. Oncogene. 1999;18:5646–5653.
Hauck CR, Hsia DA, Ilic D, Schlaepfer DD. V-Src SH3-enhanced interaction with focal adhesion kinase at beta 1 integrin-containing invadopodia promotes cell invasion. J Biol Chem. 2002;277:12487–12490.
Hsia DA, Mitra SK, Hauck CR, et al. Differential regulation of cell motility and invasion by FAK. J Cell Biol. 2003;160:753–767.
Sethi T, Rintoul RC, Moore SM, et al. Extracellular matrix proteins protect small cell lung cancer cells against apoptosis: a mechanism for small cell lung cancer growth and drug resistance in vivo. Nat Med. 1999;5:662–668.
Aoudjit F, Vuori K. Integrin signaling inhibits paclitaxel-induced apoptosis in breast cancer cells. Oncogene 2001;20:4995–5004.
Cordes N. Overexpression of hyperactive integrin-linked kinase leads to increased cellular radiosensitivity. Cancer Res. 2004;64:5683–5692.
Takeichi M. Cadherin cell adhesion receptors as morphogenetic regulator. Science. 1991;251:1451–1459.
Kemler R. From cadherins to catenins: cytoplasmic protein inte-ractions and regulation of cell adhesion. Trends Genet. 1993;9:317–321.
Ozawa M, Baribault H, Kemler R. The cytoplasmic domain of the cell adhesion molecule uvamorulin associates with three independent proteins structurally related in different species. EMBO J. 1989;8:1711–1717.
Hirano S, Kinoto N, Shimoyama Y, Hirohashi S, Takeichi M. Identification of a neural α-catenin as a key regulator of cadherin function and multicellular organization. Cell. 1992;70:293–301.
Breier G, Breviario F, Caveda L, et al. Molecular cloning and expression of murine vascular endothelial cadherin in early stage development of cardiovascular system. Blood. 1996;87:630–641.
Mayer B, Johnson JP, Leitl F, et al. E-cadherin expression in primary and metastatic gastric cancer: down-regulation correlates with cellular dedifferentiation and glandular disintegration. Cancer Res. 1993;53:1690–1695.
Schipper JH, Frixen UH, Behrens J, et al. E-cadherin expression in squamous cell carcinomas of head and neck: inverse correlation with tumor dedifferentiation and lymph node metastasis. Cancer Res. 1991;51:6328–6337.
Bringuier PP, Umbas R, Schaafsma HE, et al. Decreased E-cadherin immunoreactivity correlates with poor survival in patients with bladder tumors. Cancer Res. 1993;53:2341–2345.
Dorudi S, Sheffield JP, Poulsom R, Northover JM, Hart IR. E-cadherin expression in colorectal cancer. An immunocytochemical and in situ hybridization study. Am J Pathol. 1993;142:981–986.
Oka H, Shiozaki H, Kobayashi K, et al. Expression of E-cadherin cell adhesion molecules in human breast cancer tissues and its relationship to metastasis. Cancer Res. 1993;53:1696–1701.
Ochiai A, Akimoto S, Shimoyama Y, et al. Frequent loss of α-catenin expression in scirrhous carcinomas with scattered cell growth. Jpn J Cancer Res. 1994;85:266–273.
Kadowaki T, Shiozaki H, Inoue M, et al. E-cadherin and α-catenin expression in human esophageal cancer. Cancer Res. 1994;54:291–296.
Takayama T, Shinozaki H, Shibamoto S, et al. β-Catenin expression in human cancer. Am J Pathol. 1996;148:39–46.
Benjamin JM, Nelson WJ. Bench to bedside and back again: molecular mechanisms of alpha-catenin function and roles in tumorigenesis. Semin Cancer Biol. 2008;18:53–64.
Gavert N, Ben-Ze’ev A. Beta-catenin signaling in biological control and cancer. J Cell Biochem. 2007;1102:820–828.
Avizienyte E, Frame MC. Src and FAK signalling controls adhesion fate and the epithelial-to-mesenchymal transition. Curr Opin Cell Biol. 2005;17:542–547.
Hajra KM, Fearon ER. Cadherin and catenin alterations in human cancer. Genes Chromosomes Cancer. 2002;34:255–268.
Kanai Y, Oda T, Shimoyama Y, et al. Alterations of the cadherin–catenin cell adhesion system in cancers. Princess Takamatsu Symp. 1994;24:51–62.
Watabe M, Nagafuchi A, Tsukita S, Takeichi M. Induction of polarized cell-cell association and retardation of growth by activation of the E-cadherin-catenin adhesion system in a dispersed carcinoma line. J Cell Biol. 1994;127:247–256.
Lien WH, Klezovich O, Fernandez TE, Delrow J, Vasioukhin V. Alpha E-catenin controls cerebral cortical size by regulating the hedgehog signaling pathway. Science. 2006;311:1609–1612.
Vasioukhin V, Bauer C, Degenstein L, Wise B, Fuchs E. Hyperproliferation and defects in epithelial polarity upon conditional ablation of alpha-catenin in skin. Cell. 2001;104:605–617.
Kato Y, Hirano T, Yoshida K, et al. Frequent loss of E-cadherin and/or catenins in intrabronchial lesions during carcinogenesis of the bronchial epithelium. Lung Cancer. 2005;48:323–330.
Takeichi M. Functional correlation between cell adhesive properties and some cell surface proteins. J Cell Biol. 1997;75:464–474.
Hirano S, Nose A, Hatta K, et al. Calcium dependent cell-cell adhesion molecules (cadherins). J Cell Biol. 1987;105:2501–2510.
Scher RL, Koch WM, Richtsmeier WJ. Induction of the intercellular adhesion molecule (ICAM-1) on squamous carcinoma by interferon gamma. Arch Otolaryngol Head Neck Surg. 1993;119:432–438.
Takeichi M. Cadherins: a molecular family important in selective cell–cell adhesion. Annu Rev Biochem. 1990;59:237–252.
Behrens J, Mareel MM, Van Roy FM, Birchmeier W. Dissecting tumor cell invasion: epithelial cells acquire invasive properties after the loss of uvomorulin-mediated cell–cell adhesion. J Cell Biol. 1989;108:2435–2447.
Frixen UH, Behrens J, Sachs M, et al. E-cadherin-mediated cell–cell adhesion prevents invasiveness of human carcinoma cells. J Cell Biol. 1991;113:173–185.
Vleminckx K, Vakaet L Jr, Mareel M, Fiers W, Van Roy F. Genetic manipulation of E-cadherin expression by epithelial tumor cells reveals an invasion suppressor role. Cell. 1991;66:107–119.
Hirohashi S. Inactivation of the E-cadherin-mediated cell adhesion system in human cancers. Am J Pathol. 1998;153:333–339.
Akimoto S, Ochiai A, Inomata M, Hirohashi S. Expression of cadherin–catenin cell adhesion molecules, phosphorylated tyrosine residues and growth factor receptor-tyrosine kinases in gastric cancer. Jpn J Cancer Res. 1998;89:829–836.
Shimoyama Y, Nagafuchi A, Fujita S, et al. Cadherin dysfunction in a human cancer line: possible involvement of loss of α-catenin expression in reduced cell-cell adhesiveness. Cancer Res. 1992;52:5770–5774.
Oda T, Kanai Y, Shimoyama Y, et al. Cloning of the human α-catenin cDNA and its aberrant mRNA in a human cancer cell line. Biochem Biophys Res Commun. 1993;193:897–904.
Mattijssen V, Peters HM, Schalwijk L, et al. E-cadherin expression in head and neck squamous-cell carcinoma is associated with clinical outcome. Int J Cancer. 1993;55:580–585.
Umbas R, Isaacs WB, Bringuier PP, et al. Decreased E-cadherin expression is associated with poor prognosis in prostate cancer. Cancer Res. 1994;15:3929–3933.
Nakanishi Y, Ochiai A, Akimoto S, et al. Expression of E-cadherin, α-catenin, β-catenin, and plakoglobinin esophageal carcinomas and its prognostic significance: immunohistochemical analysis of 96 lesions. Oncology. 1997;54:158–165.
Oyama T, Kanai Y, Ochiai A, et al. A truncated β-catenin disrupts the interaction between E-cadherin and α-catenin: a cause of loss of intercellular adhesiveness in human cancer cell lines. Cancer Res. 1994;54:6282–6287.
Hoschuetzky H, Aberle H, Kemler R. β-Catenin mediates the interaction of the cadherin-catenin complex with epidermal growth factor receptor. J Cell Biol. 1994;127:1375–1380.
Ochiai A, Akimoto S, Kanai Y, et al. c-erbB-2 gene product associates with catenins in human cancer cells. Biochem Biophys Res Commun. 1994;205:73–78.
Kanai Y, Ochiai A, Shibata T, et al. c-erbB-2 gene product directly associates with β-catenin and plakoglobin. Biochem Biophys Res Commun. 1995;208:1067–1072.
Dohadwala M, Yan SC, Luo J, et al. Cyclooxygenase-2-dependent regulation of E-cadherin: prostaglandin E2 induces transcriptional repressors ZEB1 and Snail in non-small cell lung cancer. Cancer Res. 2006;66:5338–5345.
Brown JR, DuBois RN. Cyclooxygenase as a target in lung cancer. Clin Cancer Res. 2004;10:4266s–4269s.
Dubinett SM, Sharma S, Huang M, et al. Cyclooxygenase-2 in lung cancer. Prog Exp Tumor Res. 2003;37:138–162.
Dannenberg AJ, Zakim D. Chemoprevention of colorectal cancer through inhibition of cyclooxygenase-2. Semin Oncol. 1999;26:499–504.
Pold M, Zhu L, Sharma S, et al. Cyclooxygenase-2-dependent expression of angiogenic CXC chemokines ENA-78/CXC ligand (CXCL) 5 and interleukin 8/CXCL8 in human non-small cell lung cancer. Cancer Res. 2004;64:1853–1860.
Hilda T, Yatabe Y, Achiwa H, et al. Increased expression of cyclooxygenase 2 occurs frequently in human lung cancers, specifically in adenocarcinomas. Cancer Res. 1998;58:3761–3764.
Huang M, Stolina M, Sharma S, et al. Non-small cell lung cancer cyclooxygenase-2 dependent regulation of cytokine balance in lymphocytes and macrophages: up-regulation of interleukin 10 and down-regulation of interleukin 12 production. Cancer Res. 1998;58:1208–1216.
Sharma S, Yang SC, Zhu L, et al. Tumor cyclooxygenase-2/prostaglanding E2-dependent promotion of FOXP3expression and CD4+ CD25+ T regulatory cell activities in lung cancer. Cancer Res. 2005;65:5211–5220.
Sharma S, Zhu L, Yang SC, et al. Cyclooxygenase 2 inhibition promotes IFN-γ-dependent enhancement of antitumor responses. J Immunol. 2005;175:813–819.
Jungck M, Grunhage F, Spengler U, et al. E-cadherin expression is homogeneously reduced in adenoma from patients with familial adenomatous polyposis: an immunohistochemical study of E-cadherin, β-catenin and cyclooxygenase-2 expression. Int J Colorectal Dis. 2004;19:438–445.
Riedl K, Krysan K, Pold M, et al. Multifaceted roles of cyclooxygenase-2 in lung cancer. Drug Resist Updat. 2004;7:169–184.
Cavallaro U, Christofori G. Cell adhesion and signaling by cadherins and Ig-CAMs in cancer. Natl Rev Cancer. 2004;4:118–132.
Choi YS, Shim YM, Kim SH, et al. Prognostic significance of E-cadherin and β-catenin in resected stage I non-small cell lung cancer. Eur J Cardiothorac Surg. 2003;24:441–449.
Liu D, Huang C, Kameyama K, et al. E-cadherin expression associated with differentiation and prognosis in patients with non-small cell lung cancer. Ann Thorac Surg. 2001;71:949–951.discussion 954-955.
Witta SE, Gemmill RM, Hirsch FR, et al. Restoring E-cadherin expression increases sensitivity to epidermal growth factor receptor inhibitors in lung cancer cell lines. Cancer Res. 2006;66:944–950.
Fukuoka M, Yano S, Giaccone G, et al. Multi-institutional randomized phase II trial of gefitinib for previously treated patients with advanced non-small cell lung cancer (the IDEAL 1 Trial). J Clin Oncol. 2003;21:2237–2246.
Kris MG, Natale RB, Herbst RS, et al. Efficacy of gefitinib, an inhibitor of the epidermal growth factor receptor tyrosine kinase, in symptomatic patients with non-small cell lung cancer: a randomized trial. JAMA. 2003;290:2149–2158.
Shepherd FA, Rodrigues P, Jose C, et al. The National Cancer Institute of Canada Clinical Trials Group. Erlotinib in previously treated non-small-cell lung cancer. N Engl J Med. 2005;353:123–132.
Paez JG, Janne PA, Lee JC, et al. EGFR mutations in lung cancer: correlation with clinical response to gefitinib therapy. Science. 2004;304:1497–1500.
Tsao MS, Sakurada A, Cutz JC, et al. Erlotinib in lung cancer – molecular and clinical predictors of outcome. N Engl J Med. 2005;353:133–144.
Cappuzzo F, Magrini E, Ceresoli GL, et al. Akt phosphorylation and gefitinib efficacy in patients with advanced non-small-cell lung cancer. J Natl Cancer Inst. 2004;96:1133–1141.
Ohira T, Gemmill RM, Ferguson K, et al. WNT7a induces E-cadherin in lung cancer cells. Proc Natl Acad Sci USA. 2003;100:10429–10434.
Verschuren K, Remacle JE, Collart C, et al. SIP1, a novel zinc finger/homeodomain repressor, interacts with Smad proteins and binds to 5’-CACCT sequences in candidate target genes. J Biol Chem. 1999;27:20489–20498.
Chinnadurai G. CtBP, an unconventional transcriptional corepressor in development and oncogenesis. Mol Cell. 2002;9:213–224.
Zhong Y, Delgado Y, Gomez J, Lee SW, Perez-Soler R. Loss of H-cadherin protein expression in human non-small cell lung cancer is associated with tumorigenicity. Clin Cancer Res. 2001;7:1683–1687.
Agiostratidou G, Julit J, Phillips GR, Hazan RB. Differential cadherin expression: potential markers for epithelial to mesenchymal transformation during tumor progression. J Mammary Gland Biol Neoplasia. 2007;12:127–133.
Thiery JP. Epithelial–mesenchymal transitions in development and pathologies. Curr Opin Cell Biol. 2003;15:740–746.
Kneuer C, Ehrhardt C, Radomski MW, Bakowsky U. Selectins-potential pharmacological targets. Drug Discov Today 2006;11:1034–1040.
McEver RP. Properties of GMP-140, an inducible granule membrane protein of platelets and endothelium. Blood Cells. 1990;16:73–80.
Carlos TM, Harlan JM. Leukocyte-endothelial adhesion molecules. Blood. 1994;84:2068–2101.
Springer TA. Adhesion receptors of the immune system. Nature. 1990;346:425–434.
Springer TA. Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell. 1994;76:301–314.
Lowe JB, Ward PA. Therapeutic inhibition of carbohydrate–protein interactions in vivo. J Clin Invest. 1997;100:S47–S51.
Li L, Short HJ, Qian KX, et al. Characterization of glycoprotein ligands for P-selectin on a human small cell lung cancer cell line NCI-H345. Biochem Biophys Res Commun. 2001;288:637–644.
Tedder TF, Steeber DA, Chen A, Engle P. The selectins: vascular adhesion molecules. FASEB J. 1995;9:866–873.
Kim YG, Kim MJ, Lim JS, et al. ICAM-3-induced cancer cell proliferation through the PI3K/Akt pathway. Cancer Lett. 2006;239:103–110.
Stone JP, Wagner DD. P-selectin mediates adhesion of platelets to neuroblastoma and small cell lung cancer. J Clin Invest. 1993;92:804–813.
Yu CJ, Shih JY, Lee YC, et al. Sialyl Lewis antigens: association with MUC5AC protein and correlation with post-operative recurrence of non-small cell lung cancer. Lung Cancer. 2005;47:59–67.
Rosen SD, Bertozzi CR. The selectins and their ligands. Curr Opin Cell Biol. 1994;6:663–673.
Izumi Y, Taniuchi Y, Tsuji T, et al. Characterization of human colon carcinoma variant cells selected for sialyl Lex carbohydrate antigen: liver colonization and adhesion to vascular endothelial cells. Exp Cell Res. 1995;216:215–221.
Laack E, Nikbakht H, Peters A, et al. Expression of CEA-CAM1 in adenocarcinoma of the lung: a factor of independent prognostic significance. J Clin Oncol. 2002;20:4279–4284.
D’Amico TA, Brooks KR, Joshi MBM, et al. Serum protein expression predicts recurrence in patients with early-stage lung cancer after resection. Ann Thorac Surg. 2006;81:1982–1987.
Rosselli M, Mineo TC, Martini F, et al. Soluble selectin levels in patients with lung cancer. Int J Biol Marker. 2002;17:56–62.
Tsumatori G, Ozeki Y, Takagi K, Ogata T, Tanaka S. Relation between the serum E-selectin level and the survival rate of patients with resected non-small cell lung cancers. Jpn J Cancer Res. 1999;90:301–307.
Gao Y, Wei M, Zheng S, Ba X. Chemically modified heparin inhibits the in vitro adhesion of nonsmall cell lung cancer cells to P-selectin. J Cancer Res Clin Oncol. 2006;132:257–264.
Borsig L, Wong R, Hynes RQ, Varki NM, Varki A. synergistic effects of L- and P-selectin in facilitating tumor metastasis can involve non-mucin ligands and implicate leukocytes as enhancers of metastasis. Proc Natl Acad Sci. USA. 2002;99:2193–2198.
Borsig L, Wong R, Feramisco J, et al. Heparin and cancer revisited: mechanistic connections involving platelets, P-selectin, carcinoma mucins, and tumor metastasis. Proc Natl Acad Sci USA. 2001;98:3352–3357.
Tessier-Lavigne M, Goodman CS. The molecular biology of axon guidance. Science. 1996;274:1123–1133.
van Buul JD, Mul FP, van der Schoot CE, Hordijk PL. ICAM-3 activation modulates cell–cell contacts of human bone marrow endothelial cells. J Vasc Res. 2004;41:28–37.
Chung YM, Kim GB, Park CS, et al. Increased expression of ICAM3 is associated with radiation resistance in cervical cancer. Int J Cancer. 2005;117:194–201.
Yasuda M, Tanaka Y, Tamura M, et al. Stimulation of β1 integrin down-regulates ICAM-1 expression and ICAM-1-dependent adhesion of lung cancer cells through focal adhesion kinase. Cancer Res. 2001;61:2022–2030.
Schwartz RH. Models of T cell anergy: is there a common molecular mechanism? J Exp Med. 1996;184:1–8.
Shen J, Devery JM, King NJ. Adherence status regulates the primary cellular activation responses to the Flavivirus, West Nile. Immunology. 1995;84:254–264.
Mukai S, Kagamu H, Shu S, Plautz GE. Critical role of CD11a (LFA-1) in therapeutic efficacy of systemically transferred antitumor effector T cells. Cell Immunol. 1999;192:122–132.
Liu YJ, Yan PS, Li J, Jia JF. Expression and significance of CD44s, CD44v6, and nm23 mRNA in human cancer. World J Gastroenterol. 2005;11:6601–6606.
Liu J, Jiang G. CD44 and hematologic malignancies. Cell Mol Immunol. 2006;3:359–365.
Georgolios A, Batistatou A, Charalabopoulos A, Manolopoulos L, Charalabopoulos K. The role of CD44 adhesion molecule in oral cavity cancer. Exp Oncol. 2006;28:94–98.
Yasuda M, Nakano K, Yasumoto K, Tanaka Y. CD44: functional relevance to inflammation and malignancy. Histol Histopathol. 2002;17:945–950.
Guo, YJ, Liu G, Wang X, et al. Potential use of soluble CD44 in serum as indicator of tumor burden and metastasis in patients with gastric or colon cancer. Cancer Res. 1994;54:422–426.
Adamia S, Maxwell CA, Pilarski LM. Hyaluronan and hyaluronan synthases: potential therapeutic targets in cancer. Curr Drug Targets Cardiovasc Haematol Disord. 2005;5:3–14.
Wielenga VJM, Heider KH, Offerhaus JA, et al. Expression of cD44 variant proteins in human colorectal cancer is related to tumor progression. Cancer Res. 1993;53:4754–4756.
Takahashi K, Takahashi F, Hirama M, Tanabe KK, Fukuchi Y. Restoration of CD44S in non-small cell lung cancer cells enhanced their susceptibility to the macrophage cytotoxicity. Lung Cancer. 2003;41:145–153.
Li M, Amizuka N, Takeuchi K, et al. Histochemical evidence of osteoclastic degradation of extracellular matrix in osteolytic metastasis originating from human lung small carcinoma SBC-50 cells. Micro Res Tech. 2006;69:73–83.
Zhao Y, Sato Y, Isaji T, et al. Branched N-glycans regulate the biological functions of integrins and cadherins. FEBS J. 2008;275:1939–1948.
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Allen, T.C., Cagle, P.T. (2009). Cell Adhesion Molecules. In: Allen, T., Cagle, P.T. (eds) Basic Concepts of Molecular Pathology. Molecular Pathology Library, vol 2. Springer, Boston, MA. https://doi.org/10.1007/978-0-387-89626-7_3
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