An elastinolytic enzyme detected in the culture medium of human arterial smooth muscle cells

Yoshikatsu Okada, Shogo Katsuda, Yasunori Okada, Isao Nakanishi

研究成果: Article査読

26 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)863-869
ページ数7
ジャーナルCell Biology International
17
9
DOI
出版ステータスPublished - 1993 9

ASJC Scopus subject areas

  • Cell Biology

フィンガープリント 「An elastinolytic enzyme detected in the culture medium of human arterial smooth muscle cells」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル