Contribution of the 37-kDa laminin receptor precursor in the anti-metastatic PSP94-derived peptide PCK3145 cell surface binding

Biochemical and Biophysical Research Communications

Volumn 346, Issue 1, 2006, Pages 358-366

  Annabi, Borhane ^a   Currie, Jean Christophe ^a   Bouzeghrane, Mounia ^b   Dulude, Hélène ^c   Daigneault, Luc ^c   Garde, Seema ^c   Rabbani, Shafaat A ^d   Panchal, Chandra ^c   Wu, Jinzi J ^c   Béliveau, Richard ^b  

^a UNIVERSITÉ DU QUÉBEC À MONTRÉAL   (Canada)

^b UNIVERSITY OF MONTREAL   (Canada)

^c INSTITUTE FOR RESEARCH IN IMMUNOLOGY AND CANCER   (Canada)

^d MCGILL UNIVERSITY HEALTH CENTRE   (Canada)

Author keywords

EGCg; Laminin receptor precursor; Metastasis; MMP 9; Prostate cancer

Indexed keywords

ANTIMETASTATIC AGENT; ARGINYLGLYCYLASPARTIC ACID; BETA MICROSEMINOPROTEIN; CARBON 14; COLLAGEN TYPE 1; HYALURONIC ACID; LAMININ; LAMININ RECEPTOR; PCK 3145; PROSTATIC SECRETORY PROTEIN; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG;

ARTICLE; BINDING ASSAY; CELL SURFACE; DRUG BINDING; DRUG EFFECT; FAR WESTERN BLOTTING; HUMAN; HUMAN CELL; INTERNALIZATION; LIGAND BINDING; PRIORITY JOURNAL; PROSTATE CANCER;

CATECHIN; CELL COMMUNICATION; CELL LINE, TUMOR; COLLAGEN TYPE I; DRUG SYNERGISM; HUMANS; KINETICS; MATRIX METALLOPROTEINASE 9; NEOPLASM METASTASIS; OLIGOPEPTIDES; PEPTIDE FRAGMENTS; PROSTATIC SECRETORY PROTEINS; PROTEIN PRECURSORS; RECEPTORS, CELL SURFACE; RECEPTORS, LAMININ;

EID: 33744982874     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.05.139     Document Type: Article

References (27)

1. Fidler I.J. Modulation of the organ microenvironment for the treatment of cancer metastasis. J. Natl. Cancer Inst. 87 (1995) 1588-1592
2. Goodin S., Rao K.V., and DiPaola R.S. State-of-the-art treatment of metastatic hormone-refractory prostate cancer. Oncologist 7 (2002) 360-370
3. Yang J.P., Finkelman M.A., and Clarke M.W. Detection of PSP94 and its specific binding sites in the prostate adenocarcinoma cell line LNCaP. J. Urol. 160 (1998) 2240-2244
4. Sakai H., Tsurusaki T., Kanda S., et al. Prognostic significance of β-microseminoprotein mRNA expression in prostate cancer. Prostate 38 (1999) 278-284
5. Shukeir N., Arakelian A., Kadhim S., et al. Prostate secretory protein PSP94 decreases tumor growth and hypercalcemia of malignancy in a syngenic in vivo model of prostate cancer. Cancer Res. 63 (2003) 2072-2078
6. Shukeir N., Arakelian A., Chen G., et al. A synthetic 15-mer peptide (PCK3145) derived from prostate secretory protein can reduce tumor growth, experimental skeletal metastases, and malignancy-associated hypercalcemia. Cancer Res. 64 (2004) 5370-5377
7. Hawkins R.E., Daigneault L., Cowan R., Griffiths R., Panchal C., Armstrong A., et al. Safety and tolerability of PCK3145, a synthetic peptide derived from prostate secretory protein 94 (PSP94) in metastatic hormone-refractory prostate cancer. Clin. Prostate Cancer. 4 (2005) 91-99
8. Gohji K., Fujimoto N., Hara I., Fujii A., Gotoh A., Okada H., et al. Serum matrix metalloproteinase-2 and its density in men with prostate cancer as a new predictor of disease extension. Int. J. Cancer. 79 (1998) 96-101
9. Moses M.A., Wiederschain D., Loughlin K.R., Zurakowski D., Lamb C.C., and Freeman M.R. Increased incidence of matrix metalloproteinases in urine of cancer patients. Cancer Res. 58 (1998) 1395-1399
10. Lokeshwar B.L. MMP inhibition in prostate cancer. Ann. N. Y. Acad. Sci. 878 (1999) 271-289
11. Nemeth J.A., Yousif R., Herzog M., Che M., Upadhyay J., Shekarriz B., et al. Matrix metalloproteinase activity, bone matrix turnover, and tumor cell proliferation in prostate cancer bone metastasis. J. Natl. Cancer Inst. 94 (2002) 17-25
12. Annabi B., Bouzeghrane M., Currie J.C., Ruiz M.T., Wisniewski J., Garde S., et al. A PSP94-derived peptide PCK3145 inhibits MMP-9 secretion and triggers CD44 cell surface shedding: implication in tumor metastasis. Clin. Exp. Metastasis 22 (2005) 429-439
13. Lamy S., Ruiz M.T., Wisniewski J., Garde S., Rabbani S.A., Panchal C., et al. A prostate secretory protein94-derived synthetic peptide PCK3145 antagonizes VEGF signaling in endothelial cells: implication in tumor angiogenesis. Int. J. Cancer 118 (2006) 2350-2358
14. Annabi B., Bouzeghrane M., Currie J.C., Dulude H., Daigneault L., Garde S., et al. The inhibition of MMP-9 secretion by the anti-metastatic PSP94-derived peptide PCK3145 requires cell surface laminin receptors signalling. Anticancer Drugs 17 (2006) 429-438
15. Givant-Horwitz V., Davidson B., and Reich R. Laminin-induced signaling in tumor cells: the role of the M(r) 67,000 laminin receptor. Cancer Res. 64 (2004) 3572-3579
16. Tachibana H., Koga K., Fujimura Y., and Yamada K. A receptor for green tea polyphenol EGCG. Nat. Struct. Mol. Biol. 11 (2004) 380-381
17. Yun J.H., Pang E.K., Kim C.S., Yoo Y.J., Cho K.S., Chai J.K., et al. Inhibitory effects of green tea polyphenol (-)-epigallocatechin gallate on the expression of matrix metalloproteinase-9 and on the formation of osteoclasts. J. Periodontal Res. 39 (2004) 300-307
18. Kim H.S., Kim M.H., Jeong M., Hwang Y.S., Lim S.H., Shin B.A., et al. EGCG blocks tumor promoter-induced MMP-9 expression via suppression of MAPK and AP-1 activation in human gastric AGS cells. Anticancer Res. 24 (2004) 747-753
19. Menard S., Tagliabue E., and Colnaghi M.I. The 67 kDa laminin receptor as a prognostic factor in human cancer. Breast Cancer Res. Treat. 52 (1998) 137-145
20. Carbone A., Gloghini A., Colombatti A., Castronovo V., and Menard S. Expression of the monomeric 67-kDa laminin-binding protein in human lymphomas as defined by MLuC5 monoclonal antibody and paraffin section immunohistochemistry. Hum. Pathol. 26 (1995) 541-546
21. Montuori N., Selleri C., Risitano A.M., Raiola A.M., Ragno P., DelVecchio L., Rotoli B., and Rossi G. Expression of the 67-kDa laminin receptor in acute myeloid leukemia cells mediates adhesion to laminin and is frequently associated with monocytic differentiation. Clin. Cancer Res. 5 (1999) 1465-1472
22. Kim K.J., Chung J.W., and Kim K.S. 67-kDa laminin receptor promotes internalization of cytotoxic necrotizing factor 1-expressing Escherichia coli K1 into human brain microvascular endothelial cells. J. Biol. Chem. 280 (2005) 1360-1368
23. Gauczynski S., Hundt C., Leucht C., and Weiss S. Interaction of prion proteins with cell surface receptors, molecular chaperones, and other molecules. Adv. Protein Chem. 57 (2001) 229-272
24. Gauczynski S., Peyrin J.M., Haik S., Leucht C., Hundt C., Rieger R., Krasemann S., Deslys J.P., Dormont D., Lasmezas C.I., and Weiss S. The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein. EMBO J. 20 (2001) 5863-5875
25. Iyer V., Pumiglia K., and DiPersio C.M. Alpha3beta1 integrin regulates MMP-9 mRNA stability in immortalized keratinocytes: a novel mechanism of integrin-mediated MMP gene expression. J. Cell Sci. 118 (2005) 1185-1195
26. St-Pierre Y., VanThemsche C., and Esteve P.O. Emerging features in the regulation of MMP-9 gene expression for the development of novel molecular targets and therapeutic strategies. Curr. Drug Targets Inflamm. Allergy 2 (2003) 206-215
27. Nair R.R., and Boyd D.D. Expression cloning of novel regulators of 92 kDa type IV collagenase expression. Biochem. Soc. Trans. 33 (2005) 1135-1136