Collagen XIV degradation

Stable Identifier
Reaction [transition]
Bos taurus
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Collagen XIV degradation

Collagen type XIV is a member of the fibril-associated collagens with interrupted triple helices (FACIT) family, expressed in most mesenchymal tissues. The non-collagenous domain at the N-terminus of collagen XIV is extremely large, nearly 80% of the entire polypeptide. This domain is composed of eight fibronectin type III repeats, two von Willebrand factor A-like (vWFA) domains and one non-collagenous domain 4 (NC4 domain) related to collagen type IX. Collagen XIV is expressed in most mesenchymal tissues where it appears to interact with collagen type VI, glycosaminoglycans, proteoglycans and matrix receptors (Brown et al. 1993, Imhof & Trueb 1998). Collagen XIV has been implicated as a regulator of fibrillogenesis. Collagen type XIV deficient mice have a grossly normal phenotype but their skin has altered mechanical properties. Tendons were seen to be enlarged at postnatal day 4 though mature tendons appeared normal. Tendons from postnatal day 7 KO mice had reduced strength but by 60 days were comparable with wild-type (Ansorge et al. 2009). Adult Col14a1 mice have defects in ventricular morphogenesis (Tao et al. 2012).

Collagen type XIV is degraded by MMP9 (Sires et al. 1995) and MMP13 (Knauper et al. 1997).

Literature References
PubMed ID Title Journal Year
9065415 The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction

Knäuper, V, Cowell, S, Smith, B, López-Otin, C, O'Shea, M, Morris, H, Zardi, L, Murphy, G

J Biol Chem 1997
7836360 Degradation of the COL1 domain of type XIV collagen by 92-kDa gelatinase

Sires, UI, Dublet, B, Aubert-Foucher, E, van der Rest, M, Welgus, HG

J. Biol. Chem. 1995
Catalyst Activity

metalloendopeptidase activity of MMP9,13 [extracellular region]

Orthologous Events
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