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Multiple processing forms and their biological activities of a novel angiogenesis inhibitor vasohibin.

Abstract：

:Vasohibin is a newly identified negative feedback regulator for angiogenesis. When expressed in cultured human endothelial cells, vasohibin polypeptides were detected in multiple distinct molecular weight forms, suggesting that some proteolytic events may occur within cells or the pericellular milieu. 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. Western blots with anti-vasohibin monoclonal antibody following the transfection showed that there were at least two cleaving sites in the amino terminal region. Purified recombinant protein of the amino terminal truncated forms not only retained its inhibitory activity on angiogenesis in mouse corneal assay but also showed strong affinity to heparin. Moreover, deletion of some basic residues at the carboxyl terminal resulted in abrogation of both antiangiogenic and heparin-binding activities. Processing patterns and biological activities of the processed forms of this novel antiangiogenic factor are discussed.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Sonoda H,Ohta H,Watanabe K,Yamashita H,Kimura H,Sato Y

doi

10.1016/j.bbrc.2006.01.185

subject

Has Abstract

pub_date

2006-04-07 00:00:00

pages

640-6

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(06)00167-7

journal_volume

342

pub_type

杂志文章

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