Walker 256 Cancer Cells Secrete Tissue Inhibitor of Metalloproteinase-free Metalloproteinase-9

Overview

Journal Mol Cell Biochem

Publisher Springer

Specialty Biochemistry

Date 2009 Mar 31

PMID 19330523

Citations 1

Authors

Maria Pavlaki

Eleftheria Giannopoulou

Anna Niarakis

Panagiota Ravazoula

Alexios J Aletras

Affiliations

Soon will be listed here.

Abstract

Walker 256 (W256) cancer cells, developed as ascites in rats, in response to endogenous unidentified stimuli, secrete a gelatinase of apparent molecular mass of 94 kDa, immunologically homologous to the zymogen of matrix metalloproteinase-9 (proMMP-9). After treatment with the activating agent 4-aminophenylmercuric acetate (APMA), affinity-purified W256 gelatinase is converted to a final processed form of 66 kDa in a similar fashion to TIMP-free human proMMP-9. It is demonstrated that although being capable of binding TIMP-1, W256 proMMP-9 is secreted from W256 cells in TIMP-free forms (monomers or oligomers). Moreover, using biochemical and immunological methods, it is established that the W256 cells do not express or secrete TIMP-1 protein, although RT-PCR analysis indicated low-level TIMP-1 mRNA expression. W256 cancer cells displayed high metastatic ability in rats that may be attributed in part to secretion of TIMP-free proMMP-9.

Citing Articles

The Somatostatin Receptor-4 Agonist J-2156 Alleviates Mechanical Hypersensitivity in a Rat Model of Breast Cancer Induced Bone Pain.

Shenoy P, Kuo A, Khan N, Gorham L, Nicholson J, Corradini L Front Pharmacol. 2018; 9:495.

PMID: 29867498 PMC: 5962878. DOI: 10.3389/fphar.2018.00495.

References

Nagase H, Visse R, Murphy G . Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc Res. 2006; 69(3):562-73. DOI: 10.1016/j.cardiores.2005.12.002. View

Paterson A . The potential role of bisphosphonates as adjuvant therapy in the prevention of bone metastases. Cancer. 2000; 88(12 Suppl):3038-46. DOI: 10.1002/1097-0142(20000615)88:12+<3038::aid-cncr21>3.0.co;2-v. View

Opdenakker G, Masure S, Grillet B, Van Damme J . Cytokine-mediated regulation of human leukocyte gelatinases and role in arthritis. Lymphokine Cytokine Res. 1991; 10(4):317-24. View

Zucker S, Moll U, Lysik R, DiMassimo E, Stetler-Stevenson W, Liotta L . Extraction of type-IV collagenase/gelatinase from plasma membranes of human cancer cells. Int J Cancer. 1990; 45(6):1137-42. DOI: 10.1002/ijc.2910450625. View

Cha H, Kopetzki E, Huber R, Lanzendorfer M, Brandstetter H . Structural basis of the adaptive molecular recognition by MMP9. J Mol Biol. 2002; 320(5):1065-79. DOI: 10.1016/s0022-2836(02)00558-2. View

Sang Q, Birkedal-Hansen H, Van Wart H . Proteolytic and non-proteolytic activation of human neutrophil progelatinase B. Biochim Biophys Acta. 1995; 1251(2):99-108. DOI: 10.1016/0167-4838(95)00086-a. View

Homem De Bittencourt Jr P, Curi R . Antiproliferative prostaglandins and the MRP/GS-X pump role in cancer immunosuppression and insight into new strategies in cancer gene therapy. Biochem Pharmacol. 2001; 62(7):811-9. DOI: 10.1016/s0006-2952(01)00738-9. View

Goldberg G, Marmer B, Grant G, Eisen A, Wilhelm S, He C . Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2. Proc Natl Acad Sci U S A. 1989; 86(21):8207-11. PMC: 298249. DOI: 10.1073/pnas.86.21.8207. View

Moll U, Youngleib G, Rosinski K, Quigley J . Tumor promoter-stimulated Mr 92,000 gelatinase secreted by normal and malignant human cells: isolation and characterization of the enzyme from HT1080 tumor cells. Cancer Res. 1990; 50(19):6162-70. View

10.

Sternlicht M, Werb Z . How matrix metalloproteinases regulate cell behavior. Annu Rev Cell Dev Biol. 2001; 17:463-516. PMC: 2792593. DOI: 10.1146/annurev.cellbio.17.1.463. View

11.

Wilhelm S, Collier I, Marmer B, Eisen A, Grant G, Goldberg G . SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages. J Biol Chem. 1989; 264(29):17213-21. View

12.

Bastaki M, Missirlis E, Klouras N, Karakiulakis G, Maragoudakis M . Suppression of angiogenesis by the antitumor agent titanocene dichloride. Eur J Pharmacol. 1994; 251(2-3):263-9. DOI: 10.1016/0014-2999(94)90408-1. View

13.

Olson M, Bernardo M, Pietila M, Gervasi D, Toth M, Kotra L . Characterization of the monomeric and dimeric forms of latent and active matrix metalloproteinase-9. Differential rates for activation by stromelysin 1. J Biol Chem. 2000; 275(4):2661-8. DOI: 10.1074/jbc.275.4.2661. View

14.

Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View

15.

Simpkins H, Lehman J, Mazurkiewicz J, Davis B . A morphological and phenotypic analysis of Walker 256 cells. Cancer Res. 1991; 51(4):1334-8. View

16.

Birkedal-Hansen H, Moore W, Bodden M, Windsor L, DeCarlo A, Engler J . Matrix metalloproteinases: a review. Crit Rev Oral Biol Med. 1993; 4(2):197-250. DOI: 10.1177/10454411930040020401. View

17.

Tschesche H . Human neutrophil collagenase. Methods Enzymol. 1995; 248:431-49. DOI: 10.1016/0076-6879(95)48028-5. View

18.

Kim M, Albertsson P, Xue Y, Kitson R, Nannmark U, Goldfarb R . Expression of matrix metalloproteinases and their inhibitors by rat NK cells: inhibition of their expression by genistein. In Vivo. 2000; 14(5):557-64. View

19.

Ogata Y, Itoh Y, Nagase H . Steps involved in activation of the pro-matrix metalloproteinase 9 (progelatinase B)-tissue inhibitor of metalloproteinases-1 complex by 4-aminophenylmercuric acetate and proteinases. J Biol Chem. 1995; 270(31):18506-11. DOI: 10.1074/jbc.270.31.18506. View

20.

Deryugina E, Quigley J . Matrix metalloproteinases and tumor metastasis. Cancer Metastasis Rev. 2006; 25(1):9-34. DOI: 10.1007/s10555-006-7886-9. View