Collagen fibrillogenesis in tissues, in a solution and from modeling: a synthesis.
Collagen fibril formation has been studied in tissues by light and electron microscopy; in solution by light scattering and microscopy; and from modeling based on the amino acid sequence of type I collagen. Taken together these studies indicate that collagen fibril assembly involves a stepwise formation of intermediate aggregates in which each intermediate is formed from earlier aggregates. In this sequence, monomeric collagen contributes only to the formation of early aggregates; and fibrils grow in length by the addition of intermediate aggregates to the end of a subfibril and in width by lateral wrapping of subfibrils. Modeling based on amino acid sequence data of possible intermolecular charge-charge interactions indicate 2 different kinds, one which promotes linear aggregation and the other which promotes linear aggregation. The effects of different collagens and coprecipitants such as glycoproteins and proteoglycans can begin to be explained by their influence on the character of intermediate subassemblies. Ultrastructural data from 2 tissues, embryonic cornea and tendon, indicate that the site of fibril growth and assembly is at the cell surface.
D000818:Animals; D002642:Chick Embryo; D003094:Collagen / Q000378:metabolism / Q000502:physiology*; D003315:Cornea / Q000378:metabolism / Q000648:ultrastructure*; D004848:Epithelium / Q000378:metabolism; D008954:Models, Biological; D008961:Models, Structural; D013710:Tendons / Q000648:ultrastructure*
D003094:Collagen