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An elastinolytic enzyme detected in the culture medium of human arterial smooth muscle cells
Author(s) -
Okada Yoshikatsu,
Katsuda Shogo,
Okada Yasunori,
Nakanishi Isao
Publication year - 1993
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1006/cbir.1993.1149
Subject(s) - matrix metalloproteinase , elastin , enzyme , biochemistry , cytoplasm , serine , chemistry , microbiology and biotechnology , biology , genetics
The culture medium of human arterial smooth muscle cells exhibits an elastinolytic activity with 68 and 64 kDa on elastin substrate gels. The enzymatic activities are inhibited by ethylenediamine tetraacetic acid, a metalloproteinase inhibitor, but not by other inhibitors of serine, cysteine and aspartic proteinases. The proteinase in the culture medium is activatable by 4‐aminophenylmercuric acetate and degrades insoluble elastin. Compared to other matrix metalloproteinases (MMP), the activity shows the similar elastinolytic pattern to that by MMP‐2 purified from human rheumatoid synovium, while MMP‐3 and MMP‐9 have different lytic patterns and MMP‐1 possesses no elastinolytic activity. An immunoblot analysis demonstrated that the 68‐kDa enzyme is MMP‐2. An immunofluorescence study illustrates that MMP‐2 is localized within the cytoplasm of the smooth muscle cells. These findings suggest that the elastinolytic enzyme secreted by human arterial smooth muscle cells is MMP‐2.