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• W1965598077 abstract "Thrombospondins-1 and -2 (TSP-1, TSP-2) are matricellular glycoproteins with potent antiangiogenic activity. We have previously shown that the antiangiogenic activity of TSP-1 is mediated by the interaction of the type I repeats (TSR) with the receptor CD36, although other domains of TSP-1 have also been implicated. We now show that the antiangiogenic activity of TSP-2, which contains three TSRs but, unlike TSP-1, lacks the capacity to activate TGF-β, is similarly dependent on CD36. Using the corneal pocket assay we found that TSP-2 did not inhibit bFGF-induced angiogenesis in CD36 null mice. We then demonstrated that 125[I]-TSP-2 bound to murine macrophages and that binding was diminished by 70% by anti-CD36 antibody or by using cells from CD36 null animals. Solid-phase binding studies revealed that 125[I]-TSP-2 bound to CD36/glutathione-S-transferase (GST) fusion proteins encoding the region spanning amino acids 93-120, but not amino acids 298–439. This 93–120 amino acid region, previously identified as the TSP-1 binding site, is homologous to domains on other TSP binding proteins, such as LIMP-2 and histidine-rich glycoprotein (HRGP). Finally, we showed with an immunoabsorbent binding assay that TSP-2 bound HRGP with high affinity and that HRGP blocked the antiangiogenic activity of TSP-2, acting like a “decoy” receptor. These data suggest that modulation of the TSR/CD36 system may play an important role in the regulation of the angiogenic “switch,” and may provide a target for therapeutic interventions." @default.
• W1965598077 created "2016-06-24" @default.
• W1965598077 creator A5065729262 @default.
• W1965598077 creator A5066788721 @default.
• W1965598077 creator A5071903899 @default.
• W1965598077 date "2005-02-01" @default.
• W1965598077 modified "2023-10-11" @default.
• W1965598077 title "The antiangiogenic effect of thrombospondin-2 is mediated by CD36 and modulated by histidine-rich glycoprotein" @default.
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• W1965598077 doi "https://doi.org/10.1016/j.matbio.2004.11.005" @default.
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