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 language | English |
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Pages (from-to) | 73-75 |
Number of pages | 3 |
Journal | Immunopharmacology |
Volume | 32 |
Issue number | 1-3 |
DOIs | |
Publication status | Published - 1996 May |
Keywords
- Cathepsin D
- Kinin
- Matrix metalloproteinase
- T-kininogen
ASJC Scopus subject areas
- Pharmacology