Sodium-calcium exchange and sidedness of isolated cardiac sarcolemmal vesicles

Donald M Bers, Kenneth D. Philipson, Ann Y. Nishimoto

Research output: Contribution to journalArticle

99 Citations (Scopus)

Abstract

The sidedness of isolated rabbit cardiac sarcolemmal vesicles was studied by observing the effects of several permeability-increasing agents on measurements of the amount of sialic acid released by neuraminidase, specific ouabain binding, and K+-phosphatase and (Na+ + K+)-ATPase activities. The results suggest that the vesicles are sealed and are about 80% right-side-out. Na+-Ca2+ exchange exhibited by these vesicles could be attributed to the sarcolemma rather than to some contaminating organelle. Ca2+ uptake was stimulated by preloading the vesicles with NaCl (and not KCl). Increasing the external [Na+] induced a rapid Ca2+ loss, which could not be mimicked by K+, Li+, Rb+ or choline+. The Nai +-dependent Ca2+ uptake was inhibited by certain cations: Cd2+ > La3+ > Y3+ > Mn2+ > Co2+ > Mg2+. The Nai+-dependent Ca2+ influx was enhanced by an inside positive membrane potential and inhibited by an inside negative membrane potential. Potentials were induced by a K+-valinomycin system.

Original languageEnglish (US)
Pages (from-to)358-371
Number of pages14
JournalBBA - Biomembranes
Volume601
Issue numberC
DOIs
StatePublished - 1980

Fingerprint

Membrane Potentials
Sodium
Calcium
Membranes
Valinomycin
Sarcolemma
Neuraminidase
N-Acetylneuraminic Acid
Ouabain
Choline
Phosphoric Monoester Hydrolases
Organelles
Adenosine Triphosphatases
Cations
Permeability
Rabbits
sodium-translocating ATPase

Keywords

  • (Sarcolemmal vesicle)
  • Na-Ca exchange
  • Ouabain binding
  • Permeability
  • Sialic acid
  • Sidedness

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Medicine(all)

Cite this

Sodium-calcium exchange and sidedness of isolated cardiac sarcolemmal vesicles. / Bers, Donald M; Philipson, Kenneth D.; Nishimoto, Ann Y.

In: BBA - Biomembranes, Vol. 601, No. C, 1980, p. 358-371.

Research output: Contribution to journalArticle

Bers, Donald M ; Philipson, Kenneth D. ; Nishimoto, Ann Y. / Sodium-calcium exchange and sidedness of isolated cardiac sarcolemmal vesicles. In: BBA - Biomembranes. 1980 ; Vol. 601, No. C. pp. 358-371.
@article{a54b3ab073d8416582ecc7578bffe9c3,
title = "Sodium-calcium exchange and sidedness of isolated cardiac sarcolemmal vesicles",
abstract = "The sidedness of isolated rabbit cardiac sarcolemmal vesicles was studied by observing the effects of several permeability-increasing agents on measurements of the amount of sialic acid released by neuraminidase, specific ouabain binding, and K+-phosphatase and (Na+ + K+)-ATPase activities. The results suggest that the vesicles are sealed and are about 80{\%} right-side-out. Na+-Ca2+ exchange exhibited by these vesicles could be attributed to the sarcolemma rather than to some contaminating organelle. Ca2+ uptake was stimulated by preloading the vesicles with NaCl (and not KCl). Increasing the external [Na+] induced a rapid Ca2+ loss, which could not be mimicked by K+, Li+, Rb+ or choline+. The Nai +-dependent Ca2+ uptake was inhibited by certain cations: Cd2+ > La3+ > Y3+ > Mn2+ > Co2+ > Mg2+. The Nai+-dependent Ca2+ influx was enhanced by an inside positive membrane potential and inhibited by an inside negative membrane potential. Potentials were induced by a K+-valinomycin system.",
keywords = "(Sarcolemmal vesicle), Na-Ca exchange, Ouabain binding, Permeability, Sialic acid, Sidedness",
author = "Bers, {Donald M} and Philipson, {Kenneth D.} and Nishimoto, {Ann Y.}",
year = "1980",
doi = "10.1016/0005-2736(80)90540-4",
language = "English (US)",
volume = "601",
pages = "358--371",
journal = "Biochimica et Biophysica Acta - Biomembranes",
issn = "0005-2736",
publisher = "Elsevier",
number = "C",

}

TY - JOUR

T1 - Sodium-calcium exchange and sidedness of isolated cardiac sarcolemmal vesicles

AU - Bers, Donald M

AU - Philipson, Kenneth D.

AU - Nishimoto, Ann Y.

PY - 1980

Y1 - 1980

N2 - The sidedness of isolated rabbit cardiac sarcolemmal vesicles was studied by observing the effects of several permeability-increasing agents on measurements of the amount of sialic acid released by neuraminidase, specific ouabain binding, and K+-phosphatase and (Na+ + K+)-ATPase activities. The results suggest that the vesicles are sealed and are about 80% right-side-out. Na+-Ca2+ exchange exhibited by these vesicles could be attributed to the sarcolemma rather than to some contaminating organelle. Ca2+ uptake was stimulated by preloading the vesicles with NaCl (and not KCl). Increasing the external [Na+] induced a rapid Ca2+ loss, which could not be mimicked by K+, Li+, Rb+ or choline+. The Nai +-dependent Ca2+ uptake was inhibited by certain cations: Cd2+ > La3+ > Y3+ > Mn2+ > Co2+ > Mg2+. The Nai+-dependent Ca2+ influx was enhanced by an inside positive membrane potential and inhibited by an inside negative membrane potential. Potentials were induced by a K+-valinomycin system.

AB - The sidedness of isolated rabbit cardiac sarcolemmal vesicles was studied by observing the effects of several permeability-increasing agents on measurements of the amount of sialic acid released by neuraminidase, specific ouabain binding, and K+-phosphatase and (Na+ + K+)-ATPase activities. The results suggest that the vesicles are sealed and are about 80% right-side-out. Na+-Ca2+ exchange exhibited by these vesicles could be attributed to the sarcolemma rather than to some contaminating organelle. Ca2+ uptake was stimulated by preloading the vesicles with NaCl (and not KCl). Increasing the external [Na+] induced a rapid Ca2+ loss, which could not be mimicked by K+, Li+, Rb+ or choline+. The Nai +-dependent Ca2+ uptake was inhibited by certain cations: Cd2+ > La3+ > Y3+ > Mn2+ > Co2+ > Mg2+. The Nai+-dependent Ca2+ influx was enhanced by an inside positive membrane potential and inhibited by an inside negative membrane potential. Potentials were induced by a K+-valinomycin system.

KW - (Sarcolemmal vesicle)

KW - Na-Ca exchange

KW - Ouabain binding

KW - Permeability

KW - Sialic acid

KW - Sidedness

UR - http://www.scopus.com/inward/record.url?scp=0019328117&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0019328117&partnerID=8YFLogxK

U2 - 10.1016/0005-2736(80)90540-4

DO - 10.1016/0005-2736(80)90540-4

M3 - Article

VL - 601

SP - 358

EP - 371

JO - Biochimica et Biophysica Acta - Biomembranes

JF - Biochimica et Biophysica Acta - Biomembranes

SN - 0005-2736

IS - C

ER -