title: Collagen fibril biosynthesis in tendon: a review and recent insights.
abstract: The development and evolution of multicellular animals relies on the ability of certain cell types to synthesise an extracellular matrix (ECM) comprising very long collagen fibrils that are arranged in very ordered 3-dimensional scaffolds. Tendon is a good example of a highly ordered ECM, in which tens of millions of collagen fibrils, each hundreds of microns long, are synthesised parallel to the tendon long axis. This review highlights recent discoveries showing that the assembly of collagen fibrils in tendon is hierarchical, and involves the formation of fairly short "collagen early fibrils" that are the fusion precursors of the very long fibrils that occur in mature tendon.
authors.affiliation: Wellcome Trust Centre for Cell-Matrix Research, School of Biological Sciences, University of Manchester, Stopford Building 2.205, Oxford Road, M13 9PT, Manchester, United Kingdom.
authors.forename: E G
authors.initials: EG
authors.lastname: Canty
authors.forename: K E
authors.initials: KE
authors.lastname: Kadler
mesh_terms: D000818:Animals; D005109:Extracellular Matrix / Q000737:chemistry / Q000378:metabolism; D024022:Fibrillar Collagens / Q000096:biosynthesis* / Q000378:metabolism; D011347:Procollagen / Q000378:metabolism; D013710:Tendons / Q000737:chemistry / Q000378:metabolism*
chemical_list: D024022:Fibrillar Collagens; D011347:Procollagen