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Thy-1 cell surface antigen (CD90) is a small, heavily glycosylated GPI-anchored membrane glycoprotein (25–37 kDa), comprising a single V-like immunoglobulin domain[1][4]. It is broadly expressed among vertebrates, including humans, in diverse tissues (nervous system, immune system, vascular endothelium, fibroblasts)[2]. Thy-1/CD90 lacks an intracellular domain but is found within lipid rafts and mediates cell signaling through *cis* and *trans* interactions with G inhibitory proteins, SRC family kinases, and cytoskeletal molecules. It plays context-dependent roles in cell adhesion, migration, immune modulation, and cancer progression—including serving as a biomarker for tumor-initiating cells and a functional factor in metastasis and epithelial-to-mesenchymal transition[1][4]. Experimental evidence shows that CD90’s signaling can be pharmacologically targeted (e.g., dasatinib for SRC inhibition) to modulate tumor invasion and dissemination, though its broad physiological roles pose therapeutic challenges[1].
Tyrosine kinase inhibition, targeting SRC family kinases linked with CD90 signaling
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