PMID- 2553780
OWN - NLM
STAT- MEDLINE
DCOM- 19891204
LR  - 20220317
IS  - 0021-9738 (Print)
IS  - 0021-9738 (Linking)
VI  - 84
IP  - 5
DP  - 1989 Nov
TI  - Synovial procollagenase activation by human mast cell tryptase dependence upon 
      matrix metalloproteinase 3 activation.
PG  - 1657-62
AB  - Mast cells have been implicated in the pathogenesis of the matrix degradation 
      observed in the cartilaginous and osseous structures of the rheumatoid joint. We 
      previously reported that human mast cell tryptase, a 134-kD granule-associated 
      neutral protease, is present in rheumatoid synovium and can activate collagenase 
      in crude culture medium in vitro. the present study attempts to depict the 
      precise mechanism of this activation. To express full activation of latent 
      collagenase, matrix metalloproteinase 3 (MMP-3) or stromelysin, can be activated 
      by tryptase in a time and dose-dependent manner. Tryptase was not capable of 
      generating active collagenase in the crude media from cultured rheumatoid 
      synoviocytes depleted of proMMP-3 by immunoadsorption. In addition, the function 
      of the tissue inhibitor of metalloproteinases (TIMP) was not altered by tryptase, 
      and SDS-PAGE analysis revealed no degradation of TIMP by tryptase. The tryptase 
      dependent activation of synoviocyte procollagenase thereby appears to be entirely 
      dependent upon its ability to activate proMMP-3.
FAU - Gruber, B L
AU  - Gruber BL
AD  - Division of Allergy, Rheumatology and Clinical Immunology, Veterans 
      Administration, Northport, New York 11768.
FAU - Marchese, M J
AU  - Marchese MJ
FAU - Suzuki, K
AU  - Suzuki K
FAU - Schwartz, L B
AU  - Schwartz LB
FAU - Okada, Y
AU  - Okada Y
FAU - Nagase, H
AU  - Nagase H
FAU - Ramamurthy, N S
AU  - Ramamurthy NS
LA  - eng
GR  - AI-20487/AI/NIAID NIH HHS/United States
GR  - AR-39189/AR/NIAMS NIH HHS/United States
GR  - DEO3987/DE/NIDCR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Clin Invest
JT  - The Journal of clinical investigation
JID - 7802877
RN  - 0 (Enzyme Precursors)
RN  - 0 (Glycoproteins)
RN  - 0 (Tissue Inhibitor of Metalloproteinases)
RN  - 9007-34-5 (Collagen)
RN  - EC 3.4.- (Peptide Hydrolases)
RN  - EC 3.4.- (tosylarginine methyl ester hydrolase)
RN  - EC 3.4.24.- (Collagenases)
RN  - EC 3.4.24.- (Metalloendopeptidases)
RN  - EC 3.4.24.- (procollagenase)
RN  - EC 3.4.24.17 (Matrix Metalloproteinase 3)
RN  - EC 3.4.24.3 (Microbial Collagenase)
SB  - IM
MH  - Blotting, Western
MH  - Collagen/metabolism
MH  - *Collagenases
MH  - Enzyme Activation/drug effects
MH  - Enzyme Precursors/*metabolism
MH  - Glycoproteins/pharmacology
MH  - Humans
MH  - Mast Cells/*enzymology
MH  - Matrix Metalloproteinase 3
MH  - Metalloendopeptidases/*metabolism
MH  - Microbial Collagenase/*metabolism
MH  - Peptide Hydrolases/*pharmacology
MH  - Synovial Membrane/*enzymology
MH  - Tissue Inhibitor of Metalloproteinases
PMC - PMC304033
EDAT- 1989/11/01 00:00
MHDA- 1989/11/01 00:01
PMCR- 1989/11/01
CRDT- 1989/11/01 00:00
PHST- 1989/11/01 00:00 [pubmed]
PHST- 1989/11/01 00:01 [medline]
PHST- 1989/11/01 00:00 [entrez]
PHST- 1989/11/01 00:00 [pmc-release]
AID - 10.1172/JCI114344 [doi]
PST - ppublish
SO  - J Clin Invest. 1989 Nov;84(5):1657-62. doi: 10.1172/JCI114344.