Degradation of the COL1 Domain of Type XIV Collagen by 92-kDa Gelatinase (∗)

• Published in: The Journal of biological chemistry Vol. 270; no. 3; pp. 1062 - 1067
• Main Authors: Sires, Ulrike I., Dublet, Bernard, Aubert-Foucher, Elisabeth, van der Rest, Michel, Welgus, Howard G.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 20.01.1995; American Society for Biochemistry and Molecular Biology
• Subjects: Animals; Biochemistry, Molecular Biology; Catalysis; Cattle; Collagen - chemistry; Collagen - metabolism; Collagenases - metabolism; Gelatinases - antagonists & inhibitors; Gelatinases - metabolism; Glycoproteins - pharmacology; Humans; Hydrolysis; Life Sciences; Matrix Metalloproteinase 3; Matrix Metalloproteinase 7; Metalloendopeptidases - metabolism; Rats; Tissue Inhibitor of Metalloproteinases
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.270.3.1062

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°C, a full 5-6°C below the melting temperature (Tm) of this domain; native collagen XIV is also degraded at 30°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.