Degradation of T-kininogen by cathepsin D and matrix metalloproteinases.
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.
Sakamoto
W
W
Department of Biochemistry, School of Dentistry, Hokkaido University, Sapporo, Japan.
Fujie
K
K
Kaga
M
M
Handa
H
H
Gotoh
K
K
Nishihira
J
J
Kishi
J
J
Hayakawa
T
T
Okada
Y
Y
D002402:Cathepsin D / Q000302:isolation & purification / Q000494:pharmacology*; D017364:Collagenases / Q000302:isolation & purification / Q000494:pharmacology; D018093:Gelatinases / Q000302:isolation & purification / Q000494:pharmacology; D007704:Kininogens / Q000187:drug effects* / Q000378:metabolism*; D020778:Matrix Metalloproteinase 2; D019278:Matrix Metalloproteinase 3 / Q000302:isolation & purification / Q000494:pharmacology; D020780:Matrix Metalloproteinase 9; D008666:Metalloendopeptidases / Q000302:isolation & purification / Q000494:pharmacology*; D014407:Tumor Cells, Cultured
D007704:Kininogens; D002402:Cathepsin D; D017364:Collagenases; D018093:Gelatinases; D008666:Metalloendopeptidases; D019278:Matrix Metalloproteinase 3; D020778:Matrix Metalloproteinase 2; D020780:Matrix Metalloproteinase 9