title: The thrombospondins.
abstract: Thrombospondins are evolutionarily conserved, calcium-binding glycoproteins that undergo transient or longer-term interactions with other extracellular matrix components. They share properties with other matrix molecules, cytokines, adaptor proteins, and chaperones, modulate the organization of collagen fibrils, and bind and localize an array of growth factors or proteases. At cell surfaces, interactions with an array of receptors activate cell-dependent signaling and phenotypic outcomes. Through these dynamic, pleiotropic, and context-dependent pathways, mammalian thrombospondins contribute to wound healing and angiogenesis, vessel wall biology, connective tissue organization, and synaptogenesis. We overview the domain organization and structure of thrombospondins, key features of their evolution, and their cell biology. We discuss their roles in vivo, associations with human disease, and ongoing translational applications. In many respects, we are only beginning to appreciate the important roles of these proteins in physiology and pathology.
authors.affiliation: School of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom. jo.adams@bristol.ac.uk
authors.forename: Josephine C
authors.initials: JC
authors.lastname: Adams
authors.forename: Jack
authors.initials: J
authors.lastname: Lawler
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002465:Cell Movement; D049109:Cell Proliferation; D004330:Drosophila / Q000378:metabolism; D019143:Evolution, Molecular; D020022:Genetic Predisposition to Disease; D006801:Humans; D051379:Mice; D018345:Mice, Knockout; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D015398:Signal Transduction; D019699:Thrombospondins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000502:physiology*
chemical_list: D019699:Thrombospondins