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PMID: 2528347 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

AIF4-induced inhibition of the ATPase activity, the Ca2+-transport activity and the phosphoprotein-intermediate formation of plasma-membrane and endo(sarco)plasmic-reticulum Ca2+-transport ATPases in different tissues. Evidence for a tissue-dependent functional difference.

The Biochemical journal ·Vol. 261 ·No. 2 ·1989-07-15 ·Pages 655-60

Missiaen L, Wuytack F, De Smedt H, Amant F, Casteels R

Abstract

AIF4- inhibits the (Ca2+ + Mg2+)-ATPase activity of the plasma-membrane and the sarcoplasmic-reticulum Ca2+-transport ATPase [Missiaen, Wuytack, De Smedt, Vrolix & Casteels (1988) Biochem. J. 253, 827-833]. The aim of the present work was to investigate this inhibition further. We now report that AIF4- inhibits not only the (Ca2+ + Mg2+)-ATPase activity, but also the ATP-dependent 45Ca2+ transport, and the formation of the phosphoprotein intermediate by these pumps. Mg2+ potentiated the effect of AIF4-, whereas K+ had no such effect. The plasma-membrane Ca2+-transport ATPase from erythrocytes was 20 times less sensitive to inhibition by AIF4- as compared with the Ca2+-transport ATPase from smooth muscle. The endoplasmic-reticulum Ca2+-transport ATPase from smooth muscle was inhibited to a greater extent than the sarcoplasmic-reticulum Ca2+-transport ATPase of slow and fast skeletal muscle.

MeSH Terms
Adenosine Triphosphatases/antagonists & inhibitors Aluminum/pharmacology Aluminum Compounds Animals Biological Transport, Active/drug effects Calcium/pharmacokinetics Cell Membrane/enzymology Endoplasmic Reticulum/enzymology Erythrocyte Membrane/enzymology Erythrocytes/enzymology Fluorides/pharmacology Muscle, Smooth/enzymology,ultrastructure Phosphoproteins/metabolism Sarcoplasmic Reticulum/enzymology Swine
Chemicals
Aluminum Compounds Phosphoproteins Aluminum Adenosine Triphosphatases Fluorides Calcium aluminum fluoride
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Missiaen L
Department of Physiology, Catholic University of Leuven, Belgium.
Wuytack F
De Smedt H
Amant F
Casteels R
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2610655
Published
1989-07-15
Pages
655-60
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1138873
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2610655 PMC Full Text View journal details
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