The interaction of Thrombospondins with extracellular matrix proteins
Open Access
- 16 October 2009
- journal article
- research article
- Published by Wiley in Journal of Cell Communication and Signaling
- Vol. 3 (3-4), 177-187
- https://doi.org/10.1007/s12079-009-0074-2
Abstract
The thrombospondins (TSPs) are a family of five matricellular proteins that appear to function as adapter molecules to guide extracellular matrix synthesis and tissue remodeling in a variety of normal and disease settings. Various TSPs have been shown to bind to fibronectin, laminin, matrilins, collagens and other extracellular matrix (ECM) proteins. The importance of TSP-1 in this context is underscored by the fact that it is rapidly deposited at the sites of tissue damage by platelets. An association of TSPs with collagens has been known for over 25 years. The observation that the disruption of the TSP-2 gene in mice leads to collagen fibril abnormalities provided important in vivo evidence that these interactions are physiologically important. Recent biochemical studies have shown that TSP-5 promotes collagen fibril assembly and structural studies suggest that TSPs may interact with collagens through a highly conserved potential metal ion dependent adhesion site (MIDAS). These interactions are critical for normal tissue homeostasis, tumor progression and the etiology of skeletal dysplasias.Keywords
This publication has 101 references indexed in Scilit:
- Structural Insights into the Interactions between Platelet Receptors and Fibrillar CollagenOnline Journal of Public Health Informatics, 2009
- The crystal structure of the signature domain of cartilage oligomeric matrix protein: implications for collagen, glycosaminoglycan and integrin bindingThe FASEB Journal, 2009
- Distinct Roles of β1 Metal Ion-dependent Adhesion Site (MIDAS), Adjacent to MIDAS (ADMIDAS), and Ligand-associated Metal-binding Site (LIMBS) Cation-binding Sites in Ligand Recognition by Integrin α2β1Online Journal of Public Health Informatics, 2008
- Collagen fibril architecture, domain organization, and triple-helical conformation govern its proteolysisProceedings of the National Academy of Sciences of the United States of America, 2008
- Heparin-induced cis- and trans-Dimerization Modes of the Thrombospondin-1 N-terminal DomainOnline Journal of Public Health Informatics, 2008
- Blockade of Thrombospondin-1-CD47 Interactions Prevents Necrosis of Full Thickness Skin GraftsAnnals of Surgery, 2008
- Cellular and molecular mechanisms of fibrosisThe Journal of Pathology, 2007
- Interaction of Cartilage Oligomeric Matrix Protein/Thrombospondin 5 with AggrecanOnline Journal of Public Health Informatics, 2007
- Structural Basis of Integrin Regulation and SignalingAnnual Review of Immunology, 2007
- Thrombospondin‐1 inhibits VEGF levels in the ovary directly by binding and internalization via the low density lipoprotein receptor‐related protein‐1 (LRP‐1)Journal of Cellular Physiology, 2006