Phosphomimetic Thrombospondin-1 Modulates Integrin β1-FAK Signaling and Vascular Cell Functions.

ABSTRACT: Thrombospondin-1 (TSP1) is a multifunctional glycoprotein that plays a crucial role in angiogenesis and vascular remodeling. Ser93 of TSP1 has recently been identified as a novel phosphorylation site, influencing angiogenic properties; however, the underlying signaling mechanism remains unclear. Here, we investigated the functional impact of Ser93 phosphorylation using phosphomimetic (TSP1^S93D) and phosphonull (TSP1^S93A) mutants. Endothelial cell (EC) migration was analyzed using scratch assay and electric cell-substrate impedance sensing. Activation of key pathways (Akt, p38, ERK, and FAK) was analyzed by immunoblotting. TSP1 secretion was quantified by ELISA. Downstream effects on smooth muscle cells were examined by Western blot using conditioned media of endotheli

SUBMITTER: Raya A 

PROVIDER: S-EPMC12839108 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature