Relaxed specificity of matrix metalloproteinases (MMPS) and TIMP insensitivity of tumor necrosis factor-α (TNF-α) production suggest the major TNF-α converting enzyme is not an MMP

Roy A. Black, Fiona H. Durie, Carol Otten-Evans, Robert Miller, Jennifer L. Slack, David H. Lynch, Beverly Castner, Kendall M. Mohler, Mary Gerhart, Richard S. Johnson, Yoshifumi Itoh, Yasunori Okada, Hideaki Nagase

研究成果: Article査読

68 被引用数 (Scopus)

抄録

Tumor necrosis factor-α is released from cells by a proteolytic cleavage. Previous work suggested that a specific, non-matrix metalloproteinase carries out this cleavage, but matrix metalloproteinases have also been implicated. In this paper, we report that none of the matrix metalloproteinases tested cleaved peptide substrates as specifically as the non-matrix metalloproteinase. A matrix metalloproteinase did process tumor necrosis factor-α extracted from COS cells, but neither tissue inhibitor of metalloproteinases-1 nor -2 blocked tumor necrosis factor-α processing by human monocytes. Moreover, tissue inhibitor of metalloproteinases-1 had at most a partial effect on the in vivo release of the cytokine in mice. We conclude. that a non-matrix metalloproteinase is the major physiological tumor necrosis factor-α convertase.

本文言語English
ページ(範囲)400-405
ページ数6
ジャーナルBiochemical and Biophysical Research Communications
225
2
DOI
出版ステータスPublished - 1996 8月 14
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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