Abstract
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.
Highlights
AR07284, and HL29594 from the National Institutes of Health and by a grant from the CNRS
While cysteine residues and helix imperfections have been found in other collagen types (e.g. type IV collagen [17]; type VI collagen [18], and type XIII collagen
Th e COLI dom ain a ppears as a doubl et in t hese den a turing elect rophore tic gels because two differen t a mi no-terminal seque nces of COLI, VRTIQ GPP and IQGPP, are pr odu ced during the pu rifi ca tion of this domain
Summary
AR07284, and HL29594 from the National Institutes of Health and by a grant from the CNRS. The homology between types IX and XII collagens is highest in the short carboxyl-terminal triple helical domain designated COLI [15]. This triple helical domain has been used as a "signature" to define FACIT molecules [16]. Aside from a role in linking together fibrils of a tissue, collagen XIV has been shown to interact with heparin sulfate proteoglycan, collagen VI and the dermatan sulfate side chain of decorin and may be important in cell-matrix interactions [23, 24]. Stromelysins-1 and -2 are highly related metalloproteinases with the capacity to attack a broad range of matrix substrates including laminin, fibronectin, proteoglycans, and types IV and IX collagens in their nonhelical domains [28, 37, 39]. Matrilysin is the smallest metalloproteinase, but it exhibits potent catalytic activity against noncollagenous matrix components including proteoglycans, fibronectin, laminin, entactin, and elastin [37, 40, 41]
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