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Matrix metalloproteinases (MMP) are Zn2+- and Ca2+- dependent endopeptidases [1]. Main subfamilies of MMP are collagenases, gelatinases, stromelysins and membrane-type matrix metalloproteinases [2]. Three homologous collagenases have been identified in human tissues: interstitial collagenase, neutrophil collagenase and collagenase-3. The three enzymes cleave fibrillar collagens at a single site, generating fragments of approximately ¾ and ¼ the size of the original molecules. Procollagenase-3 consists of 452 amino acids with a calculated Mr of 51.680 Da [3]. Due to N-linked glycosylation the apparent Mr is about 60.000 Da [4]. Within the protein the following domains and sequence regions can be distinguished [3, 4]: an N-terminal propeptide, which confers latency to the proenzyme, a Ca2+- and Zn2+-ions binding catalytic domain, a hinge region, and a C-terminal hemopexin-like domain.

Procollagenase-3 can be activated by proteases as stromelysin [4], gelatinase A, membrane-type 1 matrix metalloproteinase and plasmin [5] or by incubation with organomercurials (e.g. APMA) [4]. Active collagenase-3 begins with the N-terminal sequence YNVFPRTL [4]. Collagenase-3 hydrolyzes type II collagen 5- to 6-times faster than type I and type III collagens. The enzyme exhibits also high activity towards gelatin and it degrades SERPINS as ?1-antichymotrypsin and plaminogen activator inhibitor-2 [4]. Collagenase-3 is inhibited in a 1:1 stoichiometric fashion by TIMP-1, TIMP-2 and TIMP-3. Collagenase-3 is expressed during fetal bone development [6]. In adult human tissues collagenase-3 has been detected only in pathological conditions: in malignant tumors [3], in chronic ulcers [7], in arthritic cartilage [8] and synovium [9].