Type XVI collagen is a member of the FACIT collagen family (fibril-associated collagens with interrupted helices). During early mouse development, it occurs in many tissues and is co-distributed with the major fibrillar collagens (Lai & Chu 1996). In skin, collagen XVI preferentially occurs in narrow zones near basement membranes at the dermo-epidermal junction (DEJ) of blood vessels (Grässel et al., 1999). In papillary dermis, the protein unexpectedly does not occur in banded collagen fibrils, but is a component of specialized fibrillin-1-containing microfibrils. However, in cartilage matrix it does not aggregate with fibrillin-1, rather it exists as a discrete population of thin, weakly banded collagen fibrils in association with collagens II and XI (Kassner et al. 2003, 2004). Collagen XVI induces the recruitment of integrins alpha1 beta1 and alpha1 beta 2 into focal adhesion plaques, a principal step in integrin signaling (Eble et al. 2006), allowing cells to affect the architecture of the ECM networks by binding and moving ECM proteins.
Collagen type XVI is cleaved by MMP9 (Sires et al. 1995).