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Cited by 263Cardiac electrophysiology and arrhythmiasThyroid Disorders and TreatmentsCardiovascular Function and Risk Factors

Thyroid hormone-induced alterations in phospholamban protein expression. Regulatory effects on sarcoplasmic reticulum Ca2+ transport and myocardial relaxation

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Kiss, E, Jakab, G, Kranias, E G, Edes, I·1994·Circulation Research
DOI 10.1161/01.res.75.2.245
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Abstract

The aim of the present study was to determine the changes in phospholamban protein levels and their regulatory effect on sarcoplasmic reticulum (SR) Ca2+ uptake and left ventricular function in hypothyroid and hyperthyroid rat hearts. Hypothyroidism was associated with decreases in basal left ventricular function (+dP/dt and -dP/dt), whereas in hyperthyroidism these parameters were elevated compared with values for euthyroid hearts. The maximal SR Ca2+ uptake rates were 12.8 +/- 1.1, 15.5 +/- 1.2, and 21.4 +/- 1.4 nmol Ca2+ per milligram per minute, and the EC50 values for Ca2+ were 0.76 +/- 0.09, 0.41 +/- 0.07, and 0.30 +/- 0.05 mumol/L assayed in homogenates from hypothyroid, euthyroid, and hyperthyroid hearts, respectively. The relative tissue level of phospholamban was increased (135%) in hypothyroidism and decreased (75%) in hyperthyroidism compared with euthyroidism (100%). An opposite trend was observed for the SR Ca(2+)-ATPase, which was depressed (74%) in hypothyroid hearts but increased (134%) in hyperthyroid hearts. Consequently, the relative ratio of phospholamban to Ca(2+)-ATPase was highest in hypothyroid and lowest in hyperthyroid hearts, and these changes correlated with changes in the EC50 of the SR Ca2+ uptake for Ca2+. Stimulation of hearts with 0.1 mumol/L isoproterenol revealed that the relaxant effects were lower in hyperthyroid hearts and higher in hypothyroid hearts compared with euthyroid hearts, consistent with the alterations in the phospholamban levels. The maximal increases in the speed of relaxation, elicited by isoproterenol stimulation, correlated with the changes in the relative ratio of phospholamban to Ca(2+)-ATPase in these hearts.(ABSTRACT TRUNCATED AT 250 WORDS)

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Research works printed but not linked: 30

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Authors
Kiss, E., Jakab, G., Kranias, E. G., & Edes, I.
Affiliations
  • Department of Pharmacology and Cell Biophysics, University of Cincinnati College of Medicine, OH 45267-0575.
  • University of Cincinnati (US)
ORCID
Kranias, E G
Venue
Circulation Research
Publisher
Ovid Technologies (Wolters Kluwer Health)
Published
1994-08
Volume
75
Issue
2
Pages
245-251
ISSN
  • 0009-7330 (ISSN-L)
  • 1524-4571
DOI
10.1161/01.res.75.2.245
OpenAlex
W2105417752
Cited by
263
References
2
Citations by year
2026: 1 · 2025: 4 · 2024: 4 · 2023: 2 · 2022: 3 · 2021: 11 · 2020: 13 · 2019: 9 · 2018: 7 · 2017: 6 · 2016: 7 · 2015: 7 · 2014: 13 · 2013: 11 · 2012: 8
FWCI
5.68
Type
journal article
Language
en
Open access
Locations
  • Circulation Research (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • U.S. Department of Health and Human Services
  • Hungarian Scientific Research Fund
  • Magyar Tudományos Akadémia
  • National Institutes of Health
  • National Heart, Lung, and Blood Institute (HL26057)
  • Fogarty International Center (F05 TWO, F05 TWO H-888-01)
Topics
  • Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac electrophysiology and arrhythmias
  • Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Thyroid Disorders and Treatments
  • Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiovascular Function and Risk Factors
Keywords
phospholamban, thyroid hormones, hypothyroidism, hyperthyroidism, sarcoplasmic reticulum Ca2+-ATPase, myocardial relaxation, left ventricular function, isoproterenol, cardiac contractility, protein expression
MeSH terms
Phospholamban, Adenosine Triphosphatases, Calcium-Transporting ATPases, Animals, Biological Transport, Calcium, Calcium-Binding Proteins, Kinetics, Male, Myocardial Contraction, Rats, Inbred Strains, Sarcoplasmic Reticulum, Thyroid Diseases, Thyroid Hormones, Ventricular Function, Left, Rats

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