Vascular Anticoagulant Beta: a Novel Human Ca2+/phospholipid Binding Protein That Inhibits Coagulation and Phospholipase A2 Activity. Its Molecular Cloning, Expression and Comparison with VAC-alpha

Overview

Journal Eur J Biochem

Specialty Biochemistry

Date 1989 Oct 20

PMID 2530088

Citations 27

Authors

R Hauptmann

E Krystek

G Bodo

H Andree

C P Reutelingsperger

Affiliations

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Abstract

A cDNA was cloned coding for a new member of the human Ca2+-modulated phospholipid-binding protein family termed annexins. Due to its 56% identity to the human vascular anticoagulant (VAC) the new protein is named VAC-beta, renaming the previous VAC as VAC-alpha. Northern analysis detects one hybridizing mRNA species of 2.2 kb in human placenta. Genomic Southern blot analysis shows a VAC-beta gene of comparable complexity to the VAC-alpha gene. The cDNA was expressed in Escherichia coli and the recombinant protein purified to homogeneity. Antiserum raised against VAC-beta weakly cross-reacts with VAC-alpha. The properties of VAC-beta as an anticoagulant and as an inhibitor of phospholipase A2 activity were analyzed and compared to those of VAC-alpha.

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