Hsp90 binds directly to fibronectin (FN) and inhibition reduces the extracellular fibronectin matrix in breast cancer cells

PLoS ONE

Volumn 9, Issue 1, 2014, Pages

  Hunter, Morgan C ^a   O'Hagan, Kyle L ^a   Kenyon, Amy ^a   Dhanani, Karim C H ^a   Prinsloo, Earl ^a   Edkins, Adrienne L ^a  

^a RHODES UNIVERSITY   (South Africa)

Author keywords

[No Author keywords available]

Indexed keywords

FIBRONECTIN; HEAT SHOCK PROTEIN 90; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1; NOVOBIOCIN;

ARTICLE; BINDING ASSAY; BREAST CANCER; BREAST CANCER CELL LINE; CONFOCAL MICROSCOPY; CONTROLLED STUDY; CROSS LINKING; EMBRYO DEVELOPMENT; EXTRACELLULAR MATRIX; GENE SILENCING; HS578T CELL LINE; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; IN VITRO STUDY; INHIBITION KINETICS; INTERNALIZATION; METASTASIS; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; SURFACE PLASMON RESONANCE; TANDEM MASS SPECTROMETRY; WOUND HEALING;

BACTERIAL PROTEINS; BREAST NEOPLASMS; CELL LINE, TUMOR; CHROMATOGRAPHY, AFFINITY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME-LINKED IMMUNOSORBENT ASSAY; EXTRACELLULAR MATRIX; FEMALE; FIBRONECTINS; FLUORESCENCE; HSP90 HEAT-SHOCK PROTEINS; HUMANS; MCF-7 CELLS; MICROSCOPY, CONFOCAL; RNA INTERFERENCE; SEPHAROSE; SURFACE PLASMON RESONANCE; TANDEM MASS SPECTROMETRY;

EID: 84899561595     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0086842     Document Type: Article

References (73)

1. Garnier C, Lafitte D, Tsvetkov PO, Barbier P, Leclerc-Devin J, et al. (2002) Binding of ATP to heat shock protein 90: evidence for an ATP-binding site in the C-terminal domain. The Journal of Biological Chemistry 277: 12208-12214. Available: http://www.ncbi.nlm.nih.gov/pubmed/11805114. Accessed 2013 March 22.
2. Cheng C, Li W (2008) Secretion of Heat Shock Protein-90 (Hsp90) by Normal Cells Under Stress or by Tumor Cells During Invasion: Why? 6: 765-772.
3. Taipale M, Krykbaeva I, Koeva M, Kayatekin C, Westover KD, et al. (2012) Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition. Cell 150: 987-1001. Available: http://www.ncbi.nlm.nih. gov/pubmed/22939624. Accessed 2013 Feb 28.
4. Citri A, Harari D, Shohat G, Ramakrishnan P, Gan J, et al. (2006) Hsp90 recognizes a common surface on client kinases. The Journal of Biological Chemistry 281: 14361-14369. Available: http://www.ncbi.nlm.nih.gov/pubmed/ 16551624. Accessed 2013 April 12.
5. Lee CC, Lin TW, Ko TP, Wang AHJ (2011) The hexameric structures of human heat shock protein 90. PloS one 6: e19961. Available: http://www.pubmedcentral. nih.gov/articlerender.fcgi?artid=3102065&tool=pmcentrez&rendertype= abstract. Accessed 2013 March 26.
6. Pearl LH, Prodromou C (2001) Structure, function and mechanism of the Hsp90 molecular chaperone. Advance Protein Chemistry 59: 157-186. Available: http://dx.doi.org/10.1016/S0065-3233(01)59005-1. Accessed 2013 April 16.
7. Donnelly A, Blagg BSJ (2008) Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket. Current medicinal chemistry 15: 2702-2717. Available:/pmc/articles/PMC2729083/?report=abstract. Accessed 2013 April 16.
8. Sánchez MC, Barcelona PF, Luna JD, Ortiz SG, Juarez PC, et al. (2006) Low-density lipoprotein receptor-related protein-1 (LRP-1) expression in a rat model of oxygen-induced retinal neovascularization. Experimental Eye Research 83: 1378-1385. Available: http://www.ncbi.nlm.nih.gov/pubmed/16979164. Accessed 2013 April 12.
9. Alfano L, Guida T, Provitera L, Vecchio G, Billaud M, et al. (2010) RET is a heat shock protein 90 (HSP90) client protein and is knocked down upon HSP90 pharmacological block. The Journal of clinical endocrinology and metabolism 95: 3552-3557. Available: http://www.ncbi.nlm.nih.gov/pubmed/20444924. Accessed 2013 April 16.
10. Lee CT, Graf C, Mayer FJ, Richter SM, Mayer MP (2012) Dynamics of the regulation of Hsp90 by the co-chaperone Sti1. The EMBO journal 31: 1518-1528. Available: http://www.ncbi.nlm.nih.gov/pubmed/22354036. Accessed 2013 March 1.
11. Eustace BK, Sakurai T, Stewart JK, Yimlamai D, Unger C, et al. (2004) Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasiveness. Nature Cell Biology 6: 507-514. Available: http://www.ncbi.nlm.nih.gov/pubmed/15146192. Accessed 2013 March 5.
12. Sidera K, Gaitanou M, Stellas D, Matsas R, Patsavoudi E (2008) A critical role for HSP90 in cancer cell invasion involves interaction with the extracellular domain of HER-2. The Journal of biological chemistry 283: 2031-2041. Available: http://www.ncbi.nlm.nih.gov/pubmed/18056992. Accessed 2013 April 16.
13. Chen Y, Erickson HP (2005) Rapid in Vitro assembly dynamics and subunit turnover of FtsZ demonstrated by fluorescence resonance energy transfer. The Journal of Biological Chemistry 280: 22549-22554. Available: http://www.ncbi.nlm.nih.gov/pubmed/15826938. Accessed 2013 April 12.
14. Sreedhar AS, Kalmár E, Csermely P, Shen Y-F (2004) Hsp90 isoforms: functions, expression and clinical importance. FEBS letters 562: 11-15. Available: http://www.ncbi.nlm.nih.gov/pubmed/15069952. Accessed 2013 March 3.
15. Grammatikakis N, Vultur A, Ramana C V, Siganou A, Schweinfest CW, et al. (2002) The role of Hsp90N, a new member of the Hsp90 family, in signal transduction and neoplastic transformation. The Journal of biological chemistry 277: 8312-8320. Available: http://www.ncbi.nlm.nih.gov/pubmed/11751906. Accessed 2013 March 5.
16. Whitesell L, Lindquist SL (2005) HSP90 and the chaperoning of cancer. Nature reviews Cancer 5: 761-772. Available: http://dx.doi.org/10.1038/nrc1716. Accessed 2013 March 3.
17. Becker B, Multhoff G, Farkas B, Wild PJ, Landthaler M, et al. (2004) Induction of Hsp90 protein expression in malignant melanomas and melanoma metastases. Experimental dermatology 13: 27-32. Available: http://www.ncbi.nlm. nih.gov/pubmed/15009113.
18. Eustace BK, Jay DG (2004) Extracellular Roles for the Molecular Chaperone, hsp90. Cell Cycle 3: 1098-1100. Available: http://www.ncbi.nlm.nih. gov/pubmed/15190213.
19. Tsutsumi S, Beebe K, Neckers L (2009) Impact of heat-shock protein 90 on cancer metastasis. Future Oncol 5: 679-688. doi:10.2217/fon.09.30.Impact.
20. McCready J, Sims JD, Chan D, Jay DG (2010) Secretion of extracellular hsp90α via exosomes increases cancer cell motility: a role for plasminogen activation. BMC Cancer 10: 294. Available: http://www.pubmedcentral.nih.gov/ articlerender.fcgi?artid=3087318&tool=pmcentrez&rendertype=abstract.
21. Li W, Li Y, Guan S, Fan J, Cheng C-F, et al. (2007) Extracellular heat shock protein-90alpha: linking hypoxia to skin cell motility and wound healing. The EMBO journal 26: 1221-1233. Available: http://www.pubmedcentral.nih.gov/ articlerender.fcgi?artid=1817627&tool=pmcentrez&rendertype=abstract. Accessed 2013 April 16.
22. Liao DF, Jin ZG, Baas a S, Daum G, Gygi SP, et al. (2000) Purification and identification of secreted oxidative stress-induced factors from vascular smooth muscle cells. The Journal of biological chemistry 275: 189-196. Available: http://www.ncbi.nlm.nih.gov/pubmed/10617604.
23. Wang X, Song X, Zhuo W, Fu Y, Shi H, et al. (2009) The regulatory mechanism of Hsp90alpha secretion and its function in tumor malignancy. Proceedings of the National Academy of Sciences of the United States of America 106: 21288-21293. Available: http://www.pubmedcentral.nih.gov/articlerender. fcgi?artid=2795546&tool=pmcentrez&rendertype=abstract.
24. Hegmans JPJJ, Bard MPL, Hemmes A, Luider TM, Kleijmeer MJ, et al. (2004) Proteomic analysis of exosomes secreted by human mesothelioma cells. The American journal of pathology 164: 1807-1815. Available: http://www. pubmedcentral.nih.gov/articlerender.fcgi?artid=1615654&tool= pmcentrez&rendertype=abstract.
25. Stellas D, El Hamidieh A, Patsavoudi E (2010) Monoclonal antibody 4C5 prevents activation of MMP2 and MMP9 by disrupting their interaction with extracellular HSP90 and inhibits formation of metastatic breast cancer cell deposits. BMC Cell Biology 11: 51. Available: http://www.pubmedcentral.nih.gov/ articlerender.fcgi?artid=2914660&tool=pmcentrez&rendertype=abstract.
26. Basu S, Binder RJ, Ramalingam T, Srivastava PK (2001) CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin. Immunity 14: 303-313. Available: http://www.ncbi.nlm.nih.gov/pubmed/11290339.
27. Tsutsumi S, Neckers L (2007) Extracellular heat shock protein 90: a role for a molecular chaperone in cell motility and cancer metastasis. Cancer Science 98: 1536-1539. Available: http://www.ncbi.nlm.nih.gov/pubmed/17645779. Accessed 2013 March 14.
28. Chen JS, Hsu YM, Chen CC, Chen LL, Lee CC, et al. (2010) Secreted Heat Shock Protein 90a Induces Colorectal Cancer Cell Invasion through CD91/LRP-1 and NF-κB-mediated Integrin αV Expression. The Journal of Biological Chemistry 285: 25458-25466. Available: http://www.pubmedcentral.nih.gov/ articlerender.fcgi?artid=2919109&tool=pmcentrez&rendertype=abstract. Accessed 2013 March 14.
29. Chen WS, Chen CC, Chen LL, Lee CC, Huang TS (2013) Secreted Heat Shock Protein 90κ Induces NF-κB-Mediated TCF12 Expression to Down-Regulate E-Cadherin and Enhance Cell Migration and Invasion in Colorectal Cancer Cells. The Journal of biological chemistry 288: 9001-9010. Available: http://www.ncbi.nlm.nih.gov/pubmed/23386606. Accessed 2013 March 10.
30. Mao Y, Schwarzbauer JE (2005) Fibronectin fibrillogenesis, a cell-mediated matrix assembly process. Matrix biology 24: 389-399. Available: http://www.ncbi.nlm.nih.gov/pubmed/16061370. Accessed 2013 March 1.
31. Schwarzbauer JE, Sechler JL (1999) Fibronectin fibrillogenesis: a paradigm for extracellular matrix assembly. Current Opinion in Cell Biology 11: 622-627. Available: http://www.ncbi.nlm.nih.gov/pubmed/10508649.
32. Crawford DC, Chobanian AV, Brecher P (1994) Angiotensin II induces fibronectin expression associated with cardiac fibrosis in the rat. Circulation Research 74: 727-739. Available: http://circres.ahajournals.org/content/74/4/ 727?related-urls=yes&legid=circresaha;74/4/727. Accessed 2013 April 18.
33. George EL, Georges-Labouesse EN, Patel-King RS, Rayburn H, Hynes RO (1993) Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin. Development (Cambridge, England) 119: 1079-1091. Available: http://www.ncbi.nlm.nih.gov/pubmed/8306876.
34. Prescott MF, Sawyer WK, Von Linden-Reed J, Jeune M, Chou M, et al. (1999) Effect of matrix metalloproteinase inhibition on progression of atherosclerosis and aneurysm in LDL receptor-deficient mice overexpressing MMP-3, MMP-12, and MMP-13 and on restenosis in rats after balloon injury. Annals of the New York Academy of Sciences 878: 179-190. Available: http://www.ncbi.nlm.nih.gov/pubmed/ 10415729.
35. Van der Westhuyzen DR, Coetzee GA, Demasius IP, Harley EH, Gevers W, et al. (1984) Low density lipoprotein receptor mutations in South African homozygous familial hypercholesterolemic patients. Arteriosclerosis, Thrombosis, and Vascular Biology 4: 238-247. Available: http://atvb.ahajournals.org/ content/4/3/238. Accessed 2013 April 11.
36. Laemmli UK (1970) Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4. Nature 227: 680-685. Available: http://www.nature.com/nature/journal/v227/n5259/pdf/227680a0.pdf. Accessed 2013 April 18.
37. Towbin H, Staehelin T, Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proceedings of the National Academy of Sciences of the United States of America 76: 4350-4354. Available: http://www.pubmedcentral.nih.gov/ articlerender.fcgi?artid=411572&tool=pmcentrez&rendertype=abstract. Accessed 2013 March 7.
38. Candiano G, Bruschi M, Musante L, Santucci L, Ghiggeri GM, et al. (2004) Blue silver: a very sensitive colloidal Coomassie G-250 staining for proteome analysis. Electrophoresis 25: 1327-1333. Available: http://www.ncbi.nlm.nih.gov/ pubmed/15174055. Accessed 2013 March 5.
39. Ngubo M, Kemp G, Patterton HG (2011) Nano-electrospray tandem mass spectrometric analysis of the acetylation state of histones H3 and H4 in stationary phase in Saccharomyces cerevisiae. BMC biochemistry 12: 34. Available: http://www.biomedcentral.com/1471-2091/12/34. Accessed 2013 April 18.
40. Brenner KA, Corbett SA, Schwarzbauer JE (2000) Regulation of fibronectin matrix assembly by activated Ras in transformed cells. Onco 19: 3156-3163. (Pubitemid 30455927)
41. Sottile J, Chandler J (2005) Fibronectin matrix turnover occurs through a caveolin-1-dependent process. Molecular biology of the cell 16: 757-768. Available: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid= 545909&tool=pmcentrez&rendertype=abstract. Accessed 2013 March 4.
42. Sidera K, Samiotaki M, Yfanti E, Panayotou G, Patsavoudi E (2004) Involvement of cell surface HSP90 in cell migration reveals a novel role in the developing nervous system. The Journal of biological chemistry 279: 45379-45388. Available: http://www.ncbi.nlm.nih.gov/pubmed/15302889. Accessed 2013 March 5.
43. Cid C, Alvarez-Cermeño JC, Camafeita E, Salinas M, Alcázar A (2004) Antibodies reactive to heat shock protein 90 induce oligodendrocyte precursor cell death in culture. Implications for demyelination in multiple sclerosis. FASEB journal: official publication of the Federation of American Societies for Experimental Biology 18: 409-411. Available: http://www.ncbi.nlm. nih.gov/pubmed/14688203.
44. Dihazi GH, Sinz A (2003) Mapping low-resolution three-dimensional protein structures using chemical cross-linking and Fourier transform ion-cyclotron resonance mass spectrometry. Rapid communications in mass spectrometry: RCM 17: 2005-2014. Available: http://www.ncbi.nlm.nih.gov/pubmed/12913864. Accessed 2013 April 17.
45. Cheng SK, Olale F, Brivanlou AH, Schier AF (2004) Lefty blocks a subset of TGFbeta signals by antagonizing EGF-CFC coreceptors. PLoS biology 2: E30. Available: http://dx.plos.org/10.1371/journal.pbio.0020030. Accessed 2013 April 18.
46. Redlak MJ, Miller TA (2011) Targeting PI3K/Akt/HSP90 signaling sensitizes gastric cancer cells to deoxycholate-induced apoptosis. Digestive Diseases and Sciences 56: 323-329. Available: http://www.ncbi.nlm.nih.gov/pubmed/20585984. Accessed 2013 April 12.
47. Perkins DN, Pappin DJ, Creasy DM, Cottrell JS (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20: 3551-3567. Available: http://www.ncbi.nlm.nih.gov/ pubmed/10612281. Accessed 2013 March 6.
48. Odunuga OO, Hornby JA, Bies C, Zimmermann R, Pugh DJ, et al. (2003) Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity. The Journal of biological chemistry 278: 6896-6904. Available: http://www.ncbi.nlm.nih.gov/pubmed/12482845. Accessed 2013 March 25.
49. Reitan NK, Sporsheim B, Bjørkøy A, Strand S, Davies C de L (2012) Quantitative 3-D colocalization analysis as a tool to study the intracellular trafficking and dissociation of pDNA-chitosan polyplexes. Journal of biomedical optics 17: 026015. Available: http://www.ncbi.nlm.nih.gov/pubmed/ 22463047. Accessed 2013 April 18.
50. Wierzbicka-Patynowski I, Schwarzbauer JE (2003) The ins and outs of fibronectin matrix assembly. Journal of cell science 116: 3269-3276. Available: http://www.ncbi.nlm.nih.gov/pubmed/12857786. Accessed 2013 March 5.
51. Verderio E a M, Telci D, Okoye A, Melino G, Griffin M (2003) A novel RGD-independent cel adhesion pathway mediated by fibronectin-bound tissue transglutaminase rescues cells from anoikis. The Journal of biological chemistry 278: 42604-42614. Available: http://www.ncbi.nlm.nih.gov/pubmed/12732629. Accessed 2013 Aug 28.
52. Hande KR (1998) Clinical Oncology Update Etoposide: Four Decades of Development of a Topoisomerase II Inhibitor. 34: 1514-1521.
53. Wang XQ, Duan XM, Liu LH, Fang YQ, Tan Y (2005) Carboxyfluorescein Diacetate Succinimidyl Ester Fluorescent Dye for Cell Labeling. Acta Biochimica et Biophysica Sinica 37: 379-385. Available: http://abbs.oxfordjournals.org/cgi/ doi/10.1111/j.1745-7270.2005.00051.x. Accessed 2013 Aug 28.
54. Zinchuk V, Zinchuk O, Okada T (2007) Quantitative colocalization analysis of multicolor confocal immunofluorescence microscopy images: pushing pixels to explore biological phenomena. Acta histochemica et cytochemica 40: 101-111. Available: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid= 1993886&tool=pmcentrez&rendertype=abstract. Accessed 2013 Aug 7.
55. Robinson EE, Foty RA, Corbett SA (2004) Fibronectin Matrix Assembly Regulates αa5β1-mediated Cell Cohesion. Molecular Biology of the cell 15: 973-981. doi:10.1091/mbc.E03. (Pubitemid 38316208)
56. Falsone SF, Kungl AJ, Rek A, Cappai R, Zangger K (2009) The molecular chaperone Hsp90 modulates intermediate steps of amyloid assembly of the Parkinson-related protein alpha-synuclein. The Journal of Biological Chemistry 284: 31190-31199. Available: http://www.pubmedcentral.nih.gov/articlerender. fcgi?artid=2781518&tool=pmcentrez&rendertype=abstract. Accessed 2013 April 12.
57. Cid C, Regidor I, Poveda PD, Alcazar A (2009) Expression of heat shock protein 90 at the cell surface in human neuroblastoma cells. Cell stress & chaperones 14: 321-327. Available: http://www.pubmedcentral.nih.gov/ articlerender.fcgi?artid=2728257&tool=pmcentrez&rendertype=abstract. Accessed 2013 April 18.
58. Bagatell R, Whitesell L (2004) Altered Hsp90 function in cancer: A unique therapeutic opportunity. Mol Cancer Ther 3: 1021-1030. (Pubitemid 39199597)
59. Csermely P, Prohászka Z, Schnaider T, Csaba S, Nardai G (1998) The 90-kDa Molecular Chaperone Family: Structure, Function, and Clinical Applications. A Comprehensive Review. Pharmacol Ther 79: 129-168. (Pubitemid 28380440)
60. Theodoraki M, Caplam A (2013) Quality Control and Fate Determination of Hsp90 Client Proteins. Biochimica et Biophysica Acta 1823: 683-688. doi:10.1016/j.bbamcr.2011.08.006.Quality.
61. Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, et al. (1997) Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90: 65-75. Available: http://www.ncbi.nlm. nih.gov/pubmed/9230303.
62. Allan RK, Mok D, Ward BK, Ratajczak T (2006) Modulation of chaperone function and cochaperone interaction by novobiocin in the C-terminal domain of Hsp90: evidence that coumarin antibiotics disrupt Hsp90 dimerization. The Journal of Biological Chemistry 281: 7161-7171. Available: http://www.ncbi.nlm. nih.gov/pubmed/16421106. Accessed 2013 March 29.
63. Blagg BSJ, Kerr TD (2006) Hsp90 inhibitors: small molecules that transform the Hsp90 protein folding machinery into a catalyst for protein degradation. Medicinal research reviews 26: 310-338. Available: http://www.ncbi.nlm.nih.gov/pubmed/16385472. Accessed 2013 Aug 22.
64. Olden K, Yamada KM (1977) Mechanism of the decrease in the major cell surface protein of chick embryo fibroblasts after transformation. Cell 11: 957-969. Available: http://dx.doi.org/10.1016/0092-8674(77)90307-5. Accessed 2013 April 22.
65. Sauk JJ, Nikitakis N, Siavash H (2005) Hsp47 a novel collagen binding serpin chaperone, autoantigen and therapeutic target. Frontiers in bioscience: a journal and virtual library 10: 107-118. Available: http://www.ncbi.nlm.nih. gov/pubmed/15574354. Accessed 2013 Aug 29.
66. Hebert C, Norris K, Della Coletta R, Reynolds M, Ordóñez J, et al. (1999) Cell surface colligin/Hsp47 associates with tetraspanin protein CD9 in epidermoid carcinoma cell lines. Journal of cellular biochemistry 73: 248-258. Available: http://www.ncbi.nlm.nih.gov/pubmed/10227388.
67. Ishida Y, Kubota H, Yamamoto A, Kitamura A, Ba HP, et al. (2006) Type I Collagen in Hsp47-null Cells Is Aggregated in Endoplasmic Reticulum and Deficient in N-Propeptide Processing and Fibrillogenesis. Molecular Biology of the cell 17: 2346-2355. doi:10.1091/mbc.E05. (Pubitemid 44011749)
68. Nagai N, Hosokawa M, Itohara S, Adachi E, Matsushita T, et al. (2000) Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis. The Journal of cell biology 150: 1499-1506. Available: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid= 2150697&tool=pmcentrez&rendertype=abstract.
69. Luo B, Lam BS, Lee SH, Wey S, Zhou H, et al. (2011) The endoplasmic reticulum chaperone protein GRP94 is required for maintaining hematopoietic stem cell interactions with the adult bone marrow niche. PloS one 6: e20364. Available: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid= 3101259&tool=pmcentrez&rendertype=abstract. Accessed 2013 Aug 29.
70. Liu X, Yan Z, Huang L, Guo M, Zhang Z, et al. (2011) Cell surface heat shock protein 90 modulates prostate cancer cell adhesion and invasion through the integrin-β1/focal adhesion kinase/c-Src signaling pathway. Oncology reports 25: 1343-1351. Available: http://www.ncbi.nlm.nih.gov/pubmed/21369706. Accessed 2013 Aug 29.
71. Labat-Robert J (2002) Fibronectin in malignancy Effect of aging. Cancer Biology 12: 187-195. doi:10.1016/S1044.
72. Akiyama SK, Olden K, Yamada KM (1995) Fibronectin and integrins in invasion and metastasis. Cancer metastasis reviews 14: 173-189. Available: http://www.ncbi.nlm.nih.gov/pubmed/8548867. Accessed 2013 April 22.
73. To WS, Midwood KS (2011) Plasma and cellular fibronectin: distinct and independent functions during tissue repair. Fibrogenesis & tissue repair 4: 21. Available: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid= 3182887&tool=pmcentrez&rendertype=abstract. Accessed 2013 April 22.