Go Back MMP 13 (Collagenase 3) catalytic domain

Product Detail

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 51 686 Da [3]. Due to N-linked glycosylation the actual 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. Latent procollagenase-3 can be activated by proteases as stromelysin [4], gelatinase A, membrane-type 1 matrix metalloproteinase and plasmin [5] or by incubation with APMA [4]. The Mr of active full-length collagenase-3 is 48 000 Da [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].