Heparin Inhibits the Reconstituted Plasma Membrane Ca(2+)-ATPase from Porcine Brain Synaptosome

Overview

Journal Glycoconj J

Publisher Springer

Specialties Biochemistry
Endocrinology

Date 2004 Jan 7

PMID 14707483

Authors

Yongfang Zhao

Xujia Zhang

Affiliations

Soon will be listed here.

Abstract

Heparin has been shown to be involved in the regulation of cellular Ca(2+) by binding to many proteins with high affinity. Here we examined the effects of heparin on the plasma membrane Ca(2+)-ATPase from porcine brain synaptosome. Our results showed that heparin dramatically inhibited the ATP hydrolysis and Ca(2+) uptake in the presence and absence of calmodulin. Together with controlled proteolysis by trypsin, we concluded that the calmodulin-binding domain of the plasma membrane Ca(2+)-ATPase was less important for the heparin inhibition. Excess phosphatidylserine was able to eliminate the heparin inhibition. We observed that Ca(2+) affinity kept no obvious changes, but the ATP affinity of plasma membrane Ca(2+)-ATPase was apparently decreased in the presence of heparin. Our results indicated that heparin had little effects on ATP or Ca(2+) binding sites of the enzyme.

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