Phospholamban overexpression in rabbit ventricular myocytes does not alter sarcoplasmic reticulum Ca transport
| العنوان: | Phospholamban overexpression in rabbit ventricular myocytes does not alter sarcoplasmic reticulum Ca transport |
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| المؤلفون: | Jason R. Waggoner, Evangelia G. Kranias, Jeffrey Robbins, Kobra Haghighi, Kenneth S. Ginsburg, Bryan Mitton, Donald M. Bers |
| المصدر: | American Journal of Physiology-Heart and Circulatory Physiology. 296:H698-H703 |
| بيانات النشر: | American Physiological Society, 2009. |
| سنة النشر: | 2009 |
| مصطلحات موضوعية: | medicine.medical_specialty, SERCA, Physiology, Heart Ventricles, Genetic Vectors, Biology, Sodium-Calcium Exchanger, Adenoviridae, Sarcoplasmic Reticulum Calcium-Transporting ATPases, Contractility, Mice, Transduction, Genetic, Caffeine, Physiology (medical), Calcium-binding protein, Internal medicine, medicine, Animals, Myocyte, Myocytes, Cardiac, Calcium Signaling, Phosphorylation, Cells, Cultured, Calcium signaling, Sodium-calcium exchanger, Endoplasmic reticulum, Calcium-Binding Proteins, Isoproterenol, Biological Transport, Articles, Adrenergic beta-Agonists, musculoskeletal system, Myocardial Contraction, Up-Regulation, Phospholamban, Sarcoplasmic Reticulum, Endocrinology, cardiovascular system, Calcium, Rabbits, Cardiology and Cardiovascular Medicine, tissues, circulatory and respiratory physiology |
| الوصف: | Phospholamban has been suggested to be a key regulator of cardiac sarcoplasmic reticulum (SR) Ca cycling and contractility and a potential therapeutic target in restoring the depressed Ca cycling in failing hearts. Our understanding of the function of phospholamban stems primarily from studies in genetically altered mouse models. To evaluate the significance of this protein in larger mammalian species, which exhibit Ca cycling properties similar to humans, we overexpressed phospholamban in adult rabbit cardiomyocytes. Adenoviral-mediated gene transfer, at high multiplicities of infection, resulted in an insignificant 1.22-fold overexpression of phospholamban. There were no effects on twitch Ca-transient amplitude or decay under basal or isoproterenol-stimulated conditions. Furthermore, the SR Ca load and Na/Ca exchanger function were not altered. These apparent differences between phospholamban overexpression in rabbit compared with previous findings in the mouse may be due to a significantly higher (1.5-fold) endogenous phospholamban-to-sarco(endo)plasmic reticulum Ca-ATPase (SERCA) 2a ratio and potential functional saturation of SERCA2a by phospholamban in rabbit cardiomyocytes. The findings suggest that important species-dependent differences in phospholamban regulation of SERCA2a occur. In larger mammals, a higher fraction of SERCA2a pumps are regulated by phospholamban, and this may influence therapeutic strategies to enhance cardiac contractility and functional cardiac reserve. |
| تدمد: | 1522-1539 0363-6135 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9664d304d561cf3f4954b779da8dd89Test https://doi.org/10.1152/ajpheart.00272.2008Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....d9664d304d561cf3f4954b779da8dd89 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 15221539 03636135 |
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