Abstract
The implication of Hsp60 in cancer development is due to its participation in many metabolic and biomolecular mechanisms in cancer cells. Hsp60 interacts with various molecules that are responsible of apoptosis, cell proliferation and other mechanisms involved when a normal cell becomes malignant. Hsp60 expression was found to be increased in many types of cancer but in same tumors of different anatomical district was found decreased. The mechanism of action of Hsp60 is different depending on the type of tumor. Its involvement in the carcinogenetic process of some tumors, such as large bowel carcinoma or cervical carcinoma, seems to occur in the very early stages of disease. Hsp60 participates in the mechanism of modulation of the immune response the cancer cells use to invade surrounding tissues, and expand the tumor mass.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Abbreviations
- APCs:
-
Antigen-presenting cells
- Bax:
-
Bcl-2-associated X protein
- CD:
-
Cluster of differentiation
- c-myc:
-
Cancer myelocytomatosis
- COPD:
-
Chronic obstructive pulmonary disease
- DCs:
-
Dendritic cells
- G1:
-
Grading 1
- G2:
-
Grading 2
- G3:
-
Grading 3
- Hsp:
-
Heat shock protein
- IAP:
-
Inhibitors of apoptosis protein
- IFNγ:
-
Interferon gamma
- IKK:
-
IκB kinase
- IL:
-
Interleukin
- KA:
-
Keratoacantomas
- MMP9:
-
Matrix metallopeptidase 9
- mtHsp:
-
Mithocondrial Heat shock protein
- MyD88:
-
Myeloid differentiation primary response 88
- NCI-H292:
-
Human lung mucoepidermoid cell
- NF-kB:
-
Nuclear factor kappa-light-chain-enhancer of activated B cells
- NK:
-
Natural killer
- pC3:
-
Pro-caspase-3
- PIN:
-
Prostatic intraepithelial lesions
- ROS:
-
Reactive oxygen species
- SCC:
-
Squamous cell carcinomas
- SIL:
-
Squamous intraepithelial lesion
- Th1:
-
Type 1 T helper
- TLR:
-
Toll-like receptor
- VEGF:
-
Vascular endothelial growth factor
References
Barazi HO, Zhou L, Templeton NS, Krutzsch HC, Roberts DD (2002) Identification of heat shock protein 60 as molecular mediator of alpha 3 beta 1integrin activation. Cancer Res 62:1541–1548
Cabibi D, Conway de Macario E, Ingrao S et al (2015) CD1a-positive cells and Hsp60 (HSPD1) levels in keratoacantomas and squamous cell carcinoma. Cell Stress Chaperones 21:131–137
Campanella C, Bucchieri F, Ardizzone NM et al (2008) Upon oxidative stress, the antiapoptotic Hsp60/procaspase-3 complex persist in mucoepidermoid carcinoma cells. Eur J Histochem 52:221–228
Campanella C, Bucchieri F, Merendino AM et al (2012) The odyssey of Hsp60 from tumor cells to other destinations includes plasma membrane-associated stages and Golgi and exosomal proteintrafficking modalities. PLoS One 7:e42008
Campanella C, Rappa F, Sciumè C et al (2015) Heat shock protein 60 levels in tissue and circulating exosomes in human large bowel cancer before and after ablative surgery. Cancer 121:3230–3239
Cappello F, Zummo G (2005) HSP60 expression during carcinogenesis: a molecular “Proteus” of carcinogenesis? Cell Stress Chaperones 10:263–264
Cappello F, Bellafiore M, Palma A et al (2002) Expression of 60-kD heat shock protein increases during carcinogenesis in the uterine exocervix. Pathobiology 70:83–88
Cappello F, Bellafiore M, David S, Anzalone R, Zummo G (2003a) Ten kilodalton heat shock protein (HSP10) is overexpressed during carcinogenesis of large bowel and uterine exocervix. Cancer Lett 196:35–41
Cappello F, Bellafiore M, Palma A et al (2003b) 60kDa chaperonin (HSP60) is overexpressed during colorectal carcinogenesis. Eur J Histochem 47:105–110
Cappello F, Rappa F, David S, Anzalone R, Zummo G (2003c) Immunohistochemical evaluation of PCNA, p53, HSP60, HSP10 and MUC-2 presence and expression in prostate carcinogenesis. Anticancer Res 23:1325–1331
Cappello F, David S, Rappa F et al (2005a) The expression of HSP60 and HSP10 in large bowel carcinomas with lymph node metastase. BMC Cancer 5:139
Cappello F, Di Stefano A, D’Anna SE, Donner CF, Zummo G (2005b) Immunopositivity of heat shock protein 60 as a biomarker of bronchial carcinogenesis. Lancet Oncol 6:816
Cappello F, David S, Ardizzone N et al (2006a) Expression of heat-shock proteins Hsp10, Hsp27, Hsp60, Hsp70 and Hsp90 in urothelial carcinoma of urinary bladder. J Cancer Mol 2:7
Cappello F, Di Stefano A, David S et al (2006b) Hsp60 and Hsp10 down-regulation predicts bronchial epithelial carcinogenesis in smokers with chronic obstructive pulmonary disease. Cancer 107:2417–2424.3-77
Cappello F, David S, Peri G et al (2011) Hsp60: molecular anatomy and role in colorectal cancer diagnosis and treatment. Front Biosci S3:341–351
Caruso Bavisotto C, Nikolic D, Marino Gammazza A et al (2017) The dissociation of the Hsp60/pro-Caspase-3 complex by bis(pyridyl)oxadiazole copper complex (CubipyOXA) leads to cell death in NCI-H292 cancer cells. J Inorg Biochem 170:8–16
Castilla C, Congregado B, Conde JM et al (2010) Immunohistochemical expression of Hsp60 correlates with tumor progression and hormone resistance in prostate Cancer. Urology 76:1017.e1–1017.e6
Chandra D, Choy G, Tang DG (2007) Cytosolic accumulation of HSP60 during apoptosis with or without apparent mitochondrial release: evidence that its pro-apoptotic or pro-survival functions involve differential interactions with caspase-3. J Biol Chem 282:31289–31301
Chandrasekaran L, He CZ, Al-Barzai H, Krutzsch HC, Irulea-Arispe ML, Robets DD (2000) Cell contact-dependent activation of alpha 3 beta 1integrin modulates endothelial cell responses to thrombospondin-1. Mol Biol Cell 11:2885–2900
Chow MT, Möller A, Smyth MJ (2012) Inflammation and immune surveillance in cancer. Semin Cancer Biol 22:23–32
Chun JN, Choi B, Lee KW et al (2010) Cytosolic Hsp60 in involved in the NF-kB dependent survival of cancer cell via IKK regulation. PLoS One 5:e9422
Ciocca DR, Calderwood SK (2005) Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications. Cell Stress Chaperones 10:86–103
Cohen-Sfady M, Nussbaum G, Pevsner-Fischer M et al (2005) Control of B-cell responses by toll-like receptors. Nature 438:364–368
Corrao S, La Rocca G, Anzalone R et al (2008) Role of CD1a and Hsp60 in the antitumoral response of oesophageal cancer. Oncol Rev 1:225–232
Coventry BJ, Heinzel S (2004) CD1a in human cancers: a new role for an old molecule. Trends Immunol 25:242–248
Di Felice V, David S, Cappello F, Farina F, Zummo G (2005) Is chlamydial heat shock protein 60 a risk factor for oncogenesis? Cell Mol Life Sci 62:4–9
Fan GK, Chen F, Gen Y (2006) Immunohistochemical analysis of P57(kip2), p53 and Hsp60 expression in premalignant and malignant oral tissue. Oral Oncol 42:147–153
Flohé SB, Brüggermann J, Lendemans S et al (2003) Human heat shock protein 60 induces maturation of dendritic cells versus a Th1-promoting phenotype. J Immunol 170:2340–2348
Ghosh JC, Dohi T, Kang BH, Altieri DC (2008) Hsp60 regulation of tumor cell apoptosis. J Biol Chem 283:5188–5194
Gorska M, Marino Gammazza A, Zmijewski MA et al (2013) Geldanamycin-induced osteosarcoma cell death is associated with hyperacetylation and loss of mitochondrial pool of heat shock protein 60 (hsp60). PLoS One 8:e71135
Grivennikov SI, Greten FR, Karin M (2010) Immunity, inflammation, and cancer. Cell 140:883–899
Kao TY, Chiu YC, Fang WC et al (2015) Mitochondrial Lon regulates apoptosis through the association with Hsp60-mtHsp70 complex. Cell Death Dis 6:e1642
Kimura E, Enns RE, Thiebaut F, Howell SB (1993) Regulation of HSP60 mRNA expression in a human ovarian carcinoma cell line. Cancer Chemother Pharmacol 32:279–285
Lanneau D, Brunet M, Frisan E, Solary E, Fontenay M, Garrido C (2008) Heat shock proteins: essential proteins for apoptosis regulation. J Cell Mol Med 12:743–761
Lebret T, Watson RW, Molinie V (2003) Heat shock proteins HSP27, HSP60, HSP70, and HSP90: expression in bladder carcinoma. Cancer 98:970–977
Li X-s, Xu Q, Fu X-y, Luo W-s (2014) Heat shock protein 60 overexpression is associated with the progression and prognosis in gastric Cancer. PLoS One 9:e107507
Macario AJL, Conway de Macario E (2007) Chaperonopathies by defect, excess, or mistake. Ann N Y Acad Sci 1113:178–191
Merendino AM, Bucchieri F, Campanella C et al (2010) Hsp60 is actively secreted by human tumor cells. PLoS One 5:e9247
Osterloh A, Kalinke U, Weiss S, Fleisher B, Breloer M (2007) Synergistic and differential modulation of immune responses byHSP60 and LPS. J Biol Chem 282:4669–4680
Ostrand-Rosenberg S, Sinha P (2009) Myeloid-derived suppressor cells: linking inflammation and cancer. J Immunol 182:4499–4506
Pasare C, Medzhitov R (2005) Control of B-cell responses by Toll-like receptors. Nature 438:364–368
Rappa F, Farina F, Zummo G et al (2012) HSP-molecular chaperones in cancer biogenesis and tumor therapy: an overview. Anticancer Res 32:5139–5150
Rappa F, Unti E, Baiamonte P, Cappello F, Scibetta N (2013) Different immunohistochemical levels of Hsp60 and Hsp70 in a subset of brain tumors and putative role of Hsp60 in neuroepithelial tumorigenesis. Eur J Histochem 57:e20
Rappa F, Pitruzzella A, Marino Gammazza A et al (2016) Quantitative patterns of Hsps in tubular adenoma compared with normal and tumoral tissue, reveal the value of Hsp10 and Hsp60 in early diagnosis of large bowel cancer. Cell Stress Chaperones 21:927–933
Samali A, Cai J, Zhivotovsky B, Jones DP, Orrenius S (1999) Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of Jurkat cells. EMBO J 18:2040–2048
Schneider J, Jiménez E, Marenbach K, Romero H, Marx D, Meden H (1999) Immunohistochemical detection of HSP60 expression in human ovarian cancer. Correlation with survival in a series of 247 patients. Anticancer Res 19:2141–2146
Tsai YP, Yang MH, Huang CH et al (2009) Interaction between HSP60 and βcatenin promotes metastasis. Carcinogenesis 30:1049–1057
Xanthoudakis S, Roy S, Rasper D et al (1999) Hsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis. EMBO J 18:2049–2056
Zanin-Zhorov A, Nussbaum G, Franitza S, Cohen IR, Lider O (2003) T cells respond to heat shock protein 60 via TRL2: activation of adhesion and inhibition of chemokine receptors. FASEB J 17:1567–1569
Zanin-Zhorov A, Tal G, Shivtiel S et al (2005) Heat shock protein 60 activates cytokineassociated negative regulator suppressor of cytokine signaling 3 in T cells: effects on signaling, chemotaxis, and inflammation. J Immunol 175:276–285
Zhang D, Fei F, Li S et al (2017) The role of βcatenin in the initiation and metastasis of TA2 mice spontaneous breast cancer. J Cancer 8:2114–2123
Acknowledgements
F.C. and F.R. were partially supported by UniPA.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2019 Springer Nature Switzerland AG
About this chapter
Cite this chapter
Rappa, F., Carini, F., Schembri Wismayer, P. (2019). Hsp60 Involvement During Carcinogenesis. In: Asea, A., Kaur, P. (eds) Heat Shock Protein 60 in Human Diseases and Disorders. Heat Shock Proteins, vol 18. Springer, Cham. https://doi.org/10.1007/978-3-030-23154-5_10
Download citation
DOI: https://doi.org/10.1007/978-3-030-23154-5_10
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-030-23153-8
Online ISBN: 978-3-030-23154-5
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)