Vasohibin-1 (VASH1)

Vasohibin-1 (VASH1) is a metallocarboxypeptidase enzyme primarily known for its dual role in the regulation of angiogenesis and in the post-translational modification of α-tubulin. VASH1 is initially identified as an endothelium-derived feedback inhibitor of angiogenesis, inhibiting migration and proliferation of endothelial cells and suppressing new blood vessel formation. It forms a complex with the small vasohibin-binding protein (SVBP) to efficiently catalyze the detyrosination of polymerized microtubule α-tubulin—a process critical for cytoskeletal regulation in cell division, neural function, and cardiac contraction[1][2]. VASH1 is expressed in vascular endothelium as well as other tissues and has been implicated in multiple physiological and pathological processes, such as vascular stress defense, tumor angiogenesis, diabetes complications, liver cirrhosis, and retinal vascular disease[2][3][4]. While it acts as an anti-angiogenic factor in most normal and pathological settings, in the tumor microenvironment VASH1 may paradoxically correlate with enhanced angiogenesis. VASH1’s anti-angiogenic function differs from classical inhibitors by supporting endothelial cell survival and stress resistance, in part through upregulating SOD2 and SIRT1. VASH1 has at least two isoforms (VASH1A and VASH1B) with distinct or complementary roles, and its secretion is controlled by unconventional mechanisms requiring association with SVBP[2]. VASH1 is also emerging as a biomarker in liver cirrhosis and a modulator of endothelial senescence and vascular integrity[3][4].

Other names

Tubulinyl-Tyr carboxypeptidase 1KIAA1036VASHTTCP 1Tubulin carboxypeptidase 1Tyrosine carboxypeptidase 1Vasohibin-1tubulinyl-Tyr carboxypeptidase 1tubulin carboxypeptidase 1tyrosine carboxypeptidase 1

Inhibition of angiogenesis through negative regulation of endothelial cell migration and proliferation; maintains endothelial cell barrier and stress resistance; catalyzes detyrosination of α-tubulin in microtubules[1][2][3][4]