Abstract
Type XIV collagen is a fibril-associated collagen with interrupted triple helices (FACIT) found mainly in the skin, tendon, cornea, and articular cartilage. It adheres to fibrillar collagens to regulate fibrillogenesis by limiting the collagen fibril diameter and preventing the lateral fusion of adjacent fibrils. Type XIV collagen expression is highest during development but is also co-distributed with type I collagen in adult tissues. Type XIV collagen consists of three α1(XIV) chains. Each α1(XIV) chain is composed of two collagenous domains (COL1 and COL2) that adhere to fibrillar collagen and three noncollagenous (NC1–NC3) domains. Type XIV collagen is usually present in tissue areas with high mechanical stress, indicating that it provides important mechanical properties to tissues. Collagen XIV null mice are viable, but the formation of an interstitial collagen network is defective in tendons and skin, leading to reduced biomechanical function. A COL14A1 missense mutation (p.Pro1502Leu) is causal for punctuated palmoplantar keratoderma. The transcriptional silencing of COL14A1 by promoter methylation has been reported in multiple types of carcinomas. Increased type XIV collagen expression has been implicated in the progression of lung fibrosis and metastatic colon cancer. No biomarkers are available for type XIV collagen.
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