Degradation of T-kininogen by cathepsin D and matrix metalloproteinases

Wataru Sakamoto, Katsutoshi Fujie, Masayuki Kaga, Hiroshi Handa, Katsuhiro Gotoh, Jun Nishihira, Jun Ichi Kishi, Taro Hayakawa, Yasunori Okada

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Cathepsin D, matrix metalloproteinase (MMP)-2, MMP-3 (stromelysin), and MMP-9 were isolated from rat granulomatous tissues, HT1080 human fibrosarcoma cells and rheumatoid synovial cell CM. At acidic conditions, cathepsin D cleaved T-kininogen into small peptides and released Met-T-kinin-Leu (kinin precursor), but failed to release kinin. MMP-3 cleaved T-kininogen into a 57 kDa fragment as measured by SDS-PAGE and Western blot analysis using anti-T-kininogen antiserum. On the other hand, no degradation of T-kininogen occurred during incubation with MMP-2 or MMP-9100/1) at pH 7.5 for 7 h.

Original languageEnglish
Pages (from-to)73-75
Number of pages3
JournalImmunopharmacology
Volume32
Issue number1-3
DOIs
Publication statusPublished - 1996 May

Keywords

  • Cathepsin D
  • Kinin
  • Matrix metalloproteinase
  • T-kininogen

ASJC Scopus subject areas

  • Pharmacology

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  • Cite this

    Sakamoto, W., Fujie, K., Kaga, M., Handa, H., Gotoh, K., Nishihira, J., Kishi, J. I., Hayakawa, T., & Okada, Y. (1996). Degradation of T-kininogen by cathepsin D and matrix metalloproteinases. Immunopharmacology, 32(1-3), 73-75. https://doi.org/10.1016/0162-3109(95)00054-2