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It has at least three different molecular isoforms\u2014\u03b11(V)<jats:sub>2<\/jats:sub>\u03b12(V), \u03b11(V)<jats:sub>3,<\/jats:sub> and \u03b11(V)\u03b12(V)\u03b13(V)\u2014formed by combinations of three different polypeptide \u03b1 chains\u2014\u03b11(V), \u03b12(V), and \u03b13(V). COL V is a relatively minor collagen of the extracellular matrix (ECM). Morphologically, COLV occurs as heterotypic fibrils with type I collagen (COLI), microfilaments, or 12\u2010nm\u2010thick fibrils. COLV is synthesized in various mesenchymal cells and its gene expression is modulated by TGF\u2010\u03b2 and growth factors. While resistant to digestion by interstitial collagenases, native and denatured COLV are degraded by metalloproteinases and gelatinases, thereby promoting ECM remodeling. COLV interacts with matrix collagens and structural proteins, conferring structural integrity to tissue scaffolds. It binds matrix macromolecules, modulating cellular behavior, and functions. COLV co\u2010assembles with COLI into heterotypic fibrils in the cornea and skin dermis, acting as a dominant regulator of collagen fibrillogenesis. COLV deficiency is associated with loss of corneal transparency and classic Ehlers\u2013Danlos syndrome, while COLV overexpression is found in cancer, granulation tissue, inflammation, atherosclerosis, and fibrosis of lungs, skin, kidneys, adipose tissue, and liver. COLV isoform containing the \u03b13(V) chain is involved in mediating pancreatic islet cell functions. In the liver, COLV is a minor but regular component of the ECM. Increases in COLV are associated with both early and advanced hepatic fibrosis. The neoepitopes of COLV have been shown to be a useful noninvasive serum biomarker for assessing fibrotic progression and resolution in experimental hepatic fibrosis. COLV is multifunctional in health, disease, and fibrosis. 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