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Fibrillogenesis is the development of fine fibrils normally present in collagen fibers of connective tissue. It is derived from the New Latin fibrilla (meaning fibrils, or pertaining to fibrils) and Greek genesis (to create, the process by which something is created).
The assembly of collagen fibrils, fibrillogenesis appears to be a self-assembly process although there is much speculation about the specifics of the mechanism through which the body produces collagen fibrils.[1] In the body, collagen fibrils are composed of several types of collagen as well as macromolecules. Type I collagen is the most abundant structural macromolecule within the vertebrate body and also represents the most abundant collagen found within various collagen fibrils[2] There are immense differences in the types of collagen fibrils that exist within the body. For instance, fibrils within the tendon vary in width and are banded into aggregates that form fibril bundles that resist forces of tension within one dimension. Similarly, fibrils that form the translucent corneal stromal matrix form orthogonal sheets and withstand the force of traction in two dimensions. These two structurally different collagen fibrils are speculated to be formed from the same molecules with type I collagen being the primary collagen found within both structures.[2]
- ^ Kader, Karl (2008). "Collagen fibrillogenesis: fibronectin, integrins, and minor collagens as organizers and nucleators". Current Opinion in Cell Biology. 20 (5–24): 495–501. doi:10.1016/j.ceb.2008.06.008. PMC 2577133. PMID 18640274.
- ^ a b Hansen, Uwe; Peter Bruckner (July 2003). "Macromolecular Specificity of Collagen Fibrillogenesis". Journal of Biological Chemistry. 278 (39): 37352–37359. doi:10.1074/jbc.M304325200. PMID 12869566.