Transmembrane Ca2+ gradient-mediated modulation of sarcoplasmic reticumul Ca2+-ATPase

Yaping Tu, F. Y. Yang

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Ca2+-ATPase from skeletal muscle sarcoplasmic reticulum was reconstituted into liposomes with (100-1000 fold) or without transmembrane Ca2+ gradient. The highest enzyme activity and Ca2+ uptake were observed in the vesicles without transmembrane Ca2+ gradient. If there existed transmembrane Ca2+ gradient, no matter what the direction was, a lower activity would appear. Dissipation of transmembrane Ca2+ gradient by A23187 could lead to a change in enzyme activity of incorporated Ca2+-ATPase. A concomitant change of lipid fluidity of proteoliposomes with that of enzyme activity and Ca2+ uptake was observed. The inhibition of Ca2+-ATPase by the transmembrane Ca2+ gradient could be observed in the PC-PE vesicles, but not in the PS-PE or PG-PE proteoliposomes.

Original languageEnglish
Pages (from-to)561-568
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume196
Issue number2
DOIs
StatePublished - 1993
Externally publishedYes

Fingerprint

Calcium-Transporting ATPases
Enzyme activity
Modulation
Enzymes
Fluidity
Calcimycin
Sarcoplasmic Reticulum
Liposomes
Muscle
Skeletal Muscle
Lipids
proteoliposomes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Transmembrane Ca2+ gradient-mediated modulation of sarcoplasmic reticumul Ca2+-ATPase. / Tu, Yaping; Yang, F. Y.

In: Biochemical and Biophysical Research Communications, Vol. 196, No. 2, 1993, p. 561-568.

Research output: Contribution to journalArticle

@article{10ed5a07d8254e7f9d9e31a77b88713c,
title = "Transmembrane Ca2+ gradient-mediated modulation of sarcoplasmic reticumul Ca2+-ATPase",
abstract = "Ca2+-ATPase from skeletal muscle sarcoplasmic reticulum was reconstituted into liposomes with (100-1000 fold) or without transmembrane Ca2+ gradient. The highest enzyme activity and Ca2+ uptake were observed in the vesicles without transmembrane Ca2+ gradient. If there existed transmembrane Ca2+ gradient, no matter what the direction was, a lower activity would appear. Dissipation of transmembrane Ca2+ gradient by A23187 could lead to a change in enzyme activity of incorporated Ca2+-ATPase. A concomitant change of lipid fluidity of proteoliposomes with that of enzyme activity and Ca2+ uptake was observed. The inhibition of Ca2+-ATPase by the transmembrane Ca2+ gradient could be observed in the PC-PE vesicles, but not in the PS-PE or PG-PE proteoliposomes.",
author = "Yaping Tu and Yang, {F. Y.}",
year = "1993",
doi = "10.1006/bbrc.1993.2286",
language = "English",
volume = "196",
pages = "561--568",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Transmembrane Ca2+ gradient-mediated modulation of sarcoplasmic reticumul Ca2+-ATPase

AU - Tu, Yaping

AU - Yang, F. Y.

PY - 1993

Y1 - 1993

N2 - Ca2+-ATPase from skeletal muscle sarcoplasmic reticulum was reconstituted into liposomes with (100-1000 fold) or without transmembrane Ca2+ gradient. The highest enzyme activity and Ca2+ uptake were observed in the vesicles without transmembrane Ca2+ gradient. If there existed transmembrane Ca2+ gradient, no matter what the direction was, a lower activity would appear. Dissipation of transmembrane Ca2+ gradient by A23187 could lead to a change in enzyme activity of incorporated Ca2+-ATPase. A concomitant change of lipid fluidity of proteoliposomes with that of enzyme activity and Ca2+ uptake was observed. The inhibition of Ca2+-ATPase by the transmembrane Ca2+ gradient could be observed in the PC-PE vesicles, but not in the PS-PE or PG-PE proteoliposomes.

AB - Ca2+-ATPase from skeletal muscle sarcoplasmic reticulum was reconstituted into liposomes with (100-1000 fold) or without transmembrane Ca2+ gradient. The highest enzyme activity and Ca2+ uptake were observed in the vesicles without transmembrane Ca2+ gradient. If there existed transmembrane Ca2+ gradient, no matter what the direction was, a lower activity would appear. Dissipation of transmembrane Ca2+ gradient by A23187 could lead to a change in enzyme activity of incorporated Ca2+-ATPase. A concomitant change of lipid fluidity of proteoliposomes with that of enzyme activity and Ca2+ uptake was observed. The inhibition of Ca2+-ATPase by the transmembrane Ca2+ gradient could be observed in the PC-PE vesicles, but not in the PS-PE or PG-PE proteoliposomes.

UR - http://www.scopus.com/inward/record.url?scp=0027339949&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027339949&partnerID=8YFLogxK

U2 - 10.1006/bbrc.1993.2286

DO - 10.1006/bbrc.1993.2286

M3 - Article

C2 - 8240328

AN - SCOPUS:0027339949

VL - 196

SP - 561

EP - 568

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -