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The term “Thrombospondin receptor” is not a precise canonical molecular target name; it refers to cell-surface receptors that bind thrombospondin family proteins, most notably thrombospondin-1. The best-characterized thrombospondin-1 receptor is CD47 (integrin-associated protein), which binds to the C-terminal domain of thrombospondin-1 and mediates key vascular, immune, and cancer-related functions. CD47 is a widely expressed cell-surface protein in the immunoglobulin superfamily. CD47-thrombospondin-1 interaction inhibits nitric oxide-stimulated vascular signaling and plays major roles in cell survival, immune evasion (as a “don’t eat me” signal to macrophages), angiogenesis, and tissue responses to injury. Additional thrombospondin-1 receptors include CD36, integrins, and LRP1 (low density lipoprotein receptor-related protein 1), which mediate diverse cell-adhesion and matrix signaling effects. CD47 is a clinically validated immuno-oncology target, especially for drugs that block CD47-SIRPα interaction to promote macrophage-mediated phagocytosis of tumor cells. “Thrombospondin receptor” is a functional term; the most established thrombospondin-1 binding receptor and true clinical target is CD47. Alternative “thrombospondin receptors” (CD36, LRP1, integrins) are context-dependent and not typically called “the thrombospondin receptor.” The term as stated is ambiguous and thus is_incorrect: true; the canonical target is CD47 (integrin-associated protein).
Blockade of CD47-macrophage SIRPα interaction to promote phagocytosis, Modulation of nitric oxide/cGMP signaling, Inhibition of angiogenesis
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