Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts

Li H, Bauzon DE, Xu XY, Tschesche H, Cao J, Sang QXA (1998)
MOLECULAR CARCINOGENESIS 22(2): 84-94.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Autor*in
Li, H; Bauzon, DE; Xu, XY; Tschesche, HaraldUniBi; Cao, J; Sang, QXA
Abstract / Bemerkung
Membrane type (MT) 1 matrix metalloproteinase (MMP) activates progelatinase A (pro-MMP-2), a type IV collagenase, on the cell surface of tumors; however, its function in breast cancer progression and metastasis is not fully understood. To examine the expression of MT1-MMP in breast cancer cells and fibroblasts, a specific rabbit antibody (Ab) directed against a unique synthetic peptide derived from the human MT1-MMP catalytic domain was produced, purified, and characterized. This Ab is not likely to cross-react with MT2-, MT3-, or MT4-MMP or any other MMPs. MT1-MMP expression and pro-M M P-2 activation were stimulated by concanavalin A in two human breast carcinoma cell lines (BT549 and MDA-MB-231) and in normal human fetal-lung fibroblasts (HFL-1) and were slightly upregulated by breast cancer cell-fibroblast interactions. Both pro-MT1-MMP in plasma membrane (63.4 kDa) and the soluble forms of the enzyme in culture medium (57.6 and 25-30 kDa) were detected by immunoblot analysis, suggesting that cell-surface MT1-MMP exhibits an active conformation without the removal of its propeptide domain and that the mature enzyme is shed into the medium. In breast cancer cells, MT1-MMP and a recombinant catalytic domain of MT1-MMP were unable to activate pro-matrilysin, indicating that MT1-MMP is not a universal activator of all MMPs. MT1-MMP may play an important role in the invasive growth and spread of breast cancer cells by specifically activating pro-MMP-2 to cleave the connective-tissue barrier. Furthermore, use of the specific Ab may aid in the investigation of the role of MT1-MMP in human tumors. Mel. Carcinog. 22:84-94, 1998. (C) 1998 Wiley-Liss, Inc.
Stichworte
antibody production; matrilysin; proteinase processing; invasion and metastasis; gelatinase A
Erscheinungsjahr
1998
Zeitschriftentitel
MOLECULAR CARCINOGENESIS
Band
22
Ausgabe
2
Seite(n)
84-94
ISSN
0899-1987
eISSN
1098-2744
Page URI
https://pub.uni-bielefeld.de/record/1625271

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Li H, Bauzon DE, Xu XY, Tschesche H, Cao J, Sang QXA. Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts. MOLECULAR CARCINOGENESIS. 1998;22(2):84-94.
Li, H., Bauzon, D. E., Xu, X. Y., Tschesche, H., Cao, J., & Sang, Q. X. A. (1998). Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts. MOLECULAR CARCINOGENESIS, 22(2), 84-94. doi:10.1002/(SICI)1098-2744(199806)22:2<84::AID-MC3>3.0.CO;2-K
Li, H., Bauzon, D. E., Xu, X. Y., Tschesche, H., Cao, J., and Sang, Q. X. A. (1998). Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts. MOLECULAR CARCINOGENESIS 22, 84-94.
Li, H., et al., 1998. Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts. MOLECULAR CARCINOGENESIS, 22(2), p 84-94.
H. Li, et al., “Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts”, MOLECULAR CARCINOGENESIS, vol. 22, 1998, pp. 84-94.
Li, H., Bauzon, D.E., Xu, X.Y., Tschesche, H., Cao, J., Sang, Q.X.A.: Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts. MOLECULAR CARCINOGENESIS. 22, 84-94 (1998).
Li, H, Bauzon, DE, Xu, XY, Tschesche, Harald, Cao, J, and Sang, QXA. “Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts”. MOLECULAR CARCINOGENESIS 22.2 (1998): 84-94.

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