The interaction of Thrombospondins with extracellular matrix proteins.
The interaction of Thrombospondins with extracellular matrix proteins.
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DOI：
10.1007/s12079-009-0074-2
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发表时间：
2009-12
影响因子：
4.1
通讯作者：
Lawler, Jack
中科院分区：
文献类型：
--
作者：
Tan, Kemin;Lawler, Jack
血小板反应蛋白（TSP）是一个家族的五个基质细胞蛋白，似乎作为衔接分子，以指导细胞外基质的合成和组织重塑在各种正常和疾病的设置。各种TSP已显示与纤连蛋白、层粘连蛋白、基质蛋白、胶原蛋白和其他细胞外基质（ECM）蛋白结合。TSP-1在这种情况下的重要性是由血小板在组织损伤部位快速沉积的事实所强调的。已知TSP与胶原蛋白的关联超过25年。小鼠TSP-2基因的破坏导致胶原纤维异常的观察结果提供了重要的体内证据，表明这些相互作用在生理上是重要的。最近的生物化学研究表明，TSP-5促进胶原原纤维组装和结构研究表明，TSP可能通过高度保守的潜在金属离子依赖性粘附位点（MIDAS）与胶原相互作用。这些相互作用对于正常组织稳态、肿瘤进展和骨骼发育不良的病因学至关重要。
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.
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影响因子：
5.3
作者：
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通讯作者：
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影响因子：
3.3
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