Degradation of the COL1 domain of type XIV collagen by 92-kDa gelatinase
| Autor: | Howard G. Welgus, Bernard Dublet, Ulrike I. Sires, Elisabeth Aubert-Foucher, Michel van der Rest |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Matrix metalloproteinase
Biochemistry Catalysis Gelatinase Animals Humans Collagenases Matrilysin Molecular Biology Glycoproteins chemistry.chemical_classification Chemistry Hydrolysis Substrate (chemistry) Metalloendopeptidases Tissue Inhibitor of Metalloproteinases Cell Biology Rats Enzyme Gelatinases Matrix Metalloproteinase 7 Interstitial collagenase Cattle Matrix Metalloproteinase 3 Collagen Type I collagen Triple helix |
| Zdroj: | The Journal of biological chemistry. 270(3) |
| ISSN: | 0021-9258 |
| Popis: | Type XIV collagen is a newly described member of the fibril-associated collagens with interrupted triple helices (FACITs). Expression of this collagen has been localized to various embryonic tissues, suggesting that it has a functional role in development. All FACITs thus far described (types IX, XII, XIV, and XVI) contain a highly homologous carboxyl-terminal triple helical domain designated COL1. We have studied the capacity of various matrix metalloproteinases (interstitial collagenase, stromelysin, matrilysin, and 92-kDa gelatinase) to degrade the COL1 domain of collagen XIV. We found that only 92-kDa gelatinase cleaves COL1. Furthermore, digestion of whole native collagen XIV by the 92-kDa gelatinase indicates that this enzyme specifically attacks the carboxyl-terminal triple helix-containing region of the molecule. COL1 is cleaved by 92-kDa gelatinase at 30 degrees C, a full 5-6 degrees C below the melting temperature (Tm) of this domain; native collagen XIV is also degraded at 30 degrees C. In comparison to interstitial collagenase degradation of its physiologic native type I collagen substrate, the 92-kDa enzyme cleaved COL1 (XIV) with comparable catalytic efficacy. Interestingly, following thermal denaturation of the COL1 fragment, its susceptibility to 92-kDa gelatinase increases, but only to a degree that leaves it several orders of magnitude less sensitive to degradation than denatured collagens I and III. These data indicate that native COL1 and collagen XIV are readily and specifically cleaved by 92-kDa gelatinase. They also suggest a role for 92-kDa gelatinase activity in the structural tissue remodeling of the developing embryo. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|