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

Yoshikatsu Okada, Shogo Katsuda, Yasunori Okada, Isao Nakanishi

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)863-870
Number of pages8
JournalCell Biology International
Volume17
Issue number9
DOIs
Publication statusPublished - 1993 Sep

Fingerprint

Matrix Metalloproteinase 2
Smooth Muscle Myocytes
Culture Media
ethylenediamine
Elastin
Enzymes
Aspartic Acid Proteases
Matrix Metalloproteinase 3
Matrix Metalloproteinase 1
Cysteine Proteases
Synovial Membrane
Matrix Metalloproteinase 9
Metalloproteases
Serine Proteases
Matrix Metalloproteinases
Fluorescent Antibody Technique
Cytoplasm
Peptide Hydrolases
Gels
Acids

ASJC Scopus subject areas

  • Cell Biology

Cite this

An elastinolytic enzyme detected in the culture medium of human arterial smooth muscle cells. / Okada, Yoshikatsu; Katsuda, Shogo; Okada, Yasunori; Nakanishi, Isao.

In: Cell Biology International, Vol. 17, No. 9, 09.1993, p. 863-870.

Research output: Contribution to journalArticle

Okada, Yoshikatsu ; Katsuda, Shogo ; Okada, Yasunori ; Nakanishi, Isao. / An elastinolytic enzyme detected in the culture medium of human arterial smooth muscle cells. In: Cell Biology International. 1993 ; Vol. 17, No. 9. pp. 863-870.
@article{66498ea1df09417abe1ede844fbb8376,
title = "An elastinolytic enzyme detected in the culture medium of human arterial smooth muscle cells",
abstract = "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.",
author = "Yoshikatsu Okada and Shogo Katsuda and Yasunori Okada and Isao Nakanishi",
year = "1993",
month = "9",
doi = "10.1006/cbir.1993.1149",
language = "English",
volume = "17",
pages = "863--870",
journal = "Cell Biology International",
issn = "1065-6995",
publisher = "Portland Press Ltd.",
number = "9",

}

TY - JOUR

T1 - An elastinolytic enzyme detected in the culture medium of human arterial smooth muscle cells

AU - Okada, Yoshikatsu

AU - Katsuda, Shogo

AU - Okada, Yasunori

AU - Nakanishi, Isao

PY - 1993/9

Y1 - 1993/9

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0027371723&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027371723&partnerID=8YFLogxK

U2 - 10.1006/cbir.1993.1149

DO - 10.1006/cbir.1993.1149

M3 - Article

VL - 17

SP - 863

EP - 870

JO - Cell Biology International

JF - Cell Biology International

SN - 1065-6995

IS - 9

ER -