Section 8
Chapter 7,327

Evidence that human rheumatoid synovial matrix metalloproteinase 3 is an endogenous activator of procollagenase

Ito, A.; Nagase, H.

Archives of Biochemistry and Biophysics 267(1): 211-216


ISSN/ISBN: 0003-9861
PMID: 2848449
DOI: 10.1016/0003-9861(88)90025-2
Accession: 007326511

Download citation:  

The treatment of crude culture medium from human rheumatoid synovial cells with 4-aminophenylmercuric acetate (APMA) or trypsin results in the activation of procollagenase. This process was shown to be dependent on the presence of matrix metalloproteinase 3 (MMP-3). MMP-3 can directly activate procollagenase without changing the apparent molecular weight of procollagenase. This activity was accelerated in the presence of APMA. We propose that MMP-3 plays an important role in connective tissue destruction through the activation of procollagenase in addition to its direct action on components of the extracellular matrix.

PDF emailed within 0-6 h: $19.90