Disease relevance of VASH1

• The expression of KIAA1036 was selective to ECs, and hypoxia or TNF-alpha abrogated its inducible expression [1].
• As this molecule is preferentially expressed in ECs, we designated it "vasohibin." Transfection of Lewis lung carcinoma cells with the vasohibin gene did not affect the proliferation of cancer cells in vitro, but did inhibit tumor growth and tumor angiogenesis in vivo [1].

High impact information on VASH1

• Specific elimination of the expression of KIAA1036 in ECs restored their responsiveness to a higher concentration of VEGF [1].
• Vasohibin is selectively induced in endothelial cells by proangiogenic stimulatory growth factors such as VEGF; it appears to operate as an intrinsic and highly specific feedback inhibitor of activated endothelial cells engaged in the process of angiogenesis [2].
• In order to identify the proteolysis sites, vasohibin cDNA mutants were generated to substitute some basic amino acids with alanine and then were transfected into endothelial cells [3].
• Vasohibin is a VEGF-inducible angiogenesis inhibitor in vascular endothelium [4].
• Here we examined the presence of vasohibin in human arterial wall, and found it in endothelium of adventitial microvessels in atherosclerotic lesion [4].

Biological context of VASH1

• Actinomycin D did not alter the kinetics of vasohibin mRNA induction upon TNFalpha treatment [5].
• Our aim is to find DNA sequences homologous to vasohibin and determine their expression profile [6].
• After that time point, vasohibin-1 and -2 became faint, but persisted to a certain extent in arterial endothelial cells from late gestation to neonate [6].
• Overall amino acid sequence homology between the prototype vasohibin (vasohibin-1) and vasohibin-2 was >50% [6].

Anatomical context of VASH1

• Gene regulation of a novel angiogenesis inhibitor, vasohibin, in endothelial cells [5].
• Vasohibin exhibited no direct effect on migration and proliferation of smooth muscle cells [4].

Associations of VASH1 with chemical compounds

• Actinomycin D did not alter the kinetics of vasohibin mRNA induction upon VEGF treatment, whereas cycloheximide completely abolished its induction [5].

Regulatory relationships of VASH1

• VEGF induced the expression of vasohibin, and this induction was abrogated by anti-VEGFR2 mAb but not by anti-VEGFR1 mAb [5].

Other interactions of VASH1

• TNFalpha, IL1 and IFNgamma decreased VEGF-stimulated vasohibin expression [5].

Analytical, diagnostic and therapeutic context of VASH1

• Western blots with anti-vasohibin monoclonal antibody following the transfection showed that there were at least two cleaving sites in the amino terminal region [3].

References