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Thrombospondin-1 (TSP1) was first characterized in 1971 by Baenziger et al. as a glycoprotein released from the α-granules of platelets in response to treatment with thrombin (Roberts and Lau 2011). This large protein consists of three 150 kDa disulfide-linked subunits and is highly conserved among vertebrate species (Carlson et al. 2008). Multi-sequence analysis has generated a phylogenetic tree for the evolution of modern TSPs (Bentley and Adams 2010). Duplication of the gene encoding a primordial TSP that is currently found in insects initiated the evolution of two subfamilies containing five members in modern vertebrates (Bentley and Adams 2010). The central feature of all TSPs is the presence of a carboxy-terminal signature domain containing EGF-like modules and seven TSP-type Ca-binding repeats, which wrap around the C-terminal lectin-like globular domain. This domain is about 650 amino acids long and is...
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