Part II. Phospholamban and cardiac sarcoplasmic reticulum. Phospholamban ablation and compensatory responses in the mammalian heart

G. Chu, D. G. Ferguson, I. Édes, E. Kiss, Y. Sato, E. G. Kranias

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Phospholamban is a low molecular weight phosphoprotein in cardiac sarcoplasmic reticulum. The regulatory role of phospholamban in vivo has recently been elucidated by targeting the gene of this protein in embryonic stem cells and generating phospholamban-deficient mice. The phospholamban knockout hearts exhibited significantly enhanced contractile parameters and attenuated responses to β-agonists. The hyperdynamic cardiac function of the phospholamban knockout mice was not accompanied by any cytoarchitectural abnormalities or alterations in the expression levels of the cardiac sarcoplasmic reticulum Ca2+-ATPase, calsequestrin, Na+-Ca2+ exchanger, or the contractile proteins. Furthermore, the attenuation of the cardiac responses to β-agonists was not due to alterations in the phosphorylation levels of the other key cardiac phosphoproteins in the phospholamban knockout hearts. However, ablation of phospholamban was associated with down-regulation of the ryanodine receptor, which suggests that a cross-talk between cardiac sarcoplasmic reticulum Ca2+ uptake and Ca2+ release occurred in an attempt to maintain Ca2+ homeostasis in these hyperdynamic phospholamban knockout hearts.

Original languageEnglish
Pages (from-to)49-62
Number of pages14
JournalAnnals of the New York Academy of Sciences
Volume853
Publication statusPublished - 1998

Fingerprint

Sarcoplasmic Reticulum
Ablation
Phosphoproteins
Calsequestrin
Contractile Proteins
Ryanodine Receptor Calcium Release Channel
Phosphorylation
Calcium-Transporting ATPases
phospholamban
Embryonic Stem Cells
Stem cells
Knockout Mice
Homeostasis
Down-Regulation
Protein
Mouse
Alteration
Molecular Weight
Molecular weight

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Part II. Phospholamban and cardiac sarcoplasmic reticulum. Phospholamban ablation and compensatory responses in the mammalian heart. / Chu, G.; Ferguson, D. G.; Édes, I.; Kiss, E.; Sato, Y.; Kranias, E. G.

In: Annals of the New York Academy of Sciences, Vol. 853, 1998, p. 49-62.

Research output: Contribution to journalArticle

@article{660f5056e8fb41cdb2e814d669478fbe,
title = "Part II. Phospholamban and cardiac sarcoplasmic reticulum. Phospholamban ablation and compensatory responses in the mammalian heart",
abstract = "Phospholamban is a low molecular weight phosphoprotein in cardiac sarcoplasmic reticulum. The regulatory role of phospholamban in vivo has recently been elucidated by targeting the gene of this protein in embryonic stem cells and generating phospholamban-deficient mice. The phospholamban knockout hearts exhibited significantly enhanced contractile parameters and attenuated responses to β-agonists. The hyperdynamic cardiac function of the phospholamban knockout mice was not accompanied by any cytoarchitectural abnormalities or alterations in the expression levels of the cardiac sarcoplasmic reticulum Ca2+-ATPase, calsequestrin, Na+-Ca2+ exchanger, or the contractile proteins. Furthermore, the attenuation of the cardiac responses to β-agonists was not due to alterations in the phosphorylation levels of the other key cardiac phosphoproteins in the phospholamban knockout hearts. However, ablation of phospholamban was associated with down-regulation of the ryanodine receptor, which suggests that a cross-talk between cardiac sarcoplasmic reticulum Ca2+ uptake and Ca2+ release occurred in an attempt to maintain Ca2+ homeostasis in these hyperdynamic phospholamban knockout hearts.",
author = "G. Chu and Ferguson, {D. G.} and I. {\'E}des and E. Kiss and Y. Sato and Kranias, {E. G.}",
year = "1998",
language = "English",
volume = "853",
pages = "49--62",
journal = "Annals of the New York Academy of Sciences",
issn = "0077-8923",
publisher = "Wiley-Blackwell",

}

TY - JOUR

T1 - Part II. Phospholamban and cardiac sarcoplasmic reticulum. Phospholamban ablation and compensatory responses in the mammalian heart

AU - Chu, G.

AU - Ferguson, D. G.

AU - Édes, I.

AU - Kiss, E.

AU - Sato, Y.

AU - Kranias, E. G.

PY - 1998

Y1 - 1998

N2 - Phospholamban is a low molecular weight phosphoprotein in cardiac sarcoplasmic reticulum. The regulatory role of phospholamban in vivo has recently been elucidated by targeting the gene of this protein in embryonic stem cells and generating phospholamban-deficient mice. The phospholamban knockout hearts exhibited significantly enhanced contractile parameters and attenuated responses to β-agonists. The hyperdynamic cardiac function of the phospholamban knockout mice was not accompanied by any cytoarchitectural abnormalities or alterations in the expression levels of the cardiac sarcoplasmic reticulum Ca2+-ATPase, calsequestrin, Na+-Ca2+ exchanger, or the contractile proteins. Furthermore, the attenuation of the cardiac responses to β-agonists was not due to alterations in the phosphorylation levels of the other key cardiac phosphoproteins in the phospholamban knockout hearts. However, ablation of phospholamban was associated with down-regulation of the ryanodine receptor, which suggests that a cross-talk between cardiac sarcoplasmic reticulum Ca2+ uptake and Ca2+ release occurred in an attempt to maintain Ca2+ homeostasis in these hyperdynamic phospholamban knockout hearts.

AB - Phospholamban is a low molecular weight phosphoprotein in cardiac sarcoplasmic reticulum. The regulatory role of phospholamban in vivo has recently been elucidated by targeting the gene of this protein in embryonic stem cells and generating phospholamban-deficient mice. The phospholamban knockout hearts exhibited significantly enhanced contractile parameters and attenuated responses to β-agonists. The hyperdynamic cardiac function of the phospholamban knockout mice was not accompanied by any cytoarchitectural abnormalities or alterations in the expression levels of the cardiac sarcoplasmic reticulum Ca2+-ATPase, calsequestrin, Na+-Ca2+ exchanger, or the contractile proteins. Furthermore, the attenuation of the cardiac responses to β-agonists was not due to alterations in the phosphorylation levels of the other key cardiac phosphoproteins in the phospholamban knockout hearts. However, ablation of phospholamban was associated with down-regulation of the ryanodine receptor, which suggests that a cross-talk between cardiac sarcoplasmic reticulum Ca2+ uptake and Ca2+ release occurred in an attempt to maintain Ca2+ homeostasis in these hyperdynamic phospholamban knockout hearts.

UR - http://www.scopus.com/inward/record.url?scp=0032537891&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032537891&partnerID=8YFLogxK

M3 - Article

VL - 853

SP - 49

EP - 62

JO - Annals of the New York Academy of Sciences

JF - Annals of the New York Academy of Sciences

SN - 0077-8923

ER -