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Collagen fibrillogenesis: fibronectin, integrins, and minor collagens as organizers and nucleators Kadler KE; Hill A; Canty-Laird EGCurr Opin Cell Biol 2008[Oct]; 20 (5): 495-501Collagens are triple helical proteins that occur in the extracellular matrix (ECM) and at the cell-ECM interface. There are more than 30 collagens and collagen-related proteins but the most abundant are collagens I and II that exist as D-periodic (where D = 67 nm) fibrils. The fibrils are of broad biomedical importance and have central roles in embryogenesis, arthritis, tissue repair, fibrosis, tumor invasion, and cardiovascular disease. Collagens I and II spontaneously form fibrils in vitro, which shows that collagen fibrillogenesis is a selfassembly process. However, the situation in vivo is not that simple; collagen I-containing fibrils do not form in the absence of fibronectin, fibronectin-binding and collagen-binding integrins, and collagen V. Likewise, the thin collagen II-containing fibrils in cartilage do not form in the absence of collagen XI. Thus, in vivo, cellular mechanisms are in place to control what is otherwise a protein self-assembly process. This review puts forward a working hypothesis for how fibronectin and integrins (the organizers) determine the site of fibril assembly, and collagens V and XI (the nucleators) initiate collagen fibrillogenesis.|Animals[MESH]|Cell Membrane/metabolism[MESH]|Collagen/chemistry/*metabolism[MESH]|Extracellular Matrix/chemistry/metabolism[MESH]|Fibronectins/*metabolism[MESH]|Humans[MESH]|Integrins/*metabolism[MESH]|Models, Molecular[MESH]|Protein Isoforms/chemistry/*metabolism[MESH] |
