Role of phospholamban phosphorylation on Thr17 in cardiac physiological and pathological conditions

dc.creatorMattiazzi, Alicia Ramona
dc.creatorMundiña-Weilenmann, Cecilia
dc.creatorGuoxiang, Chu
dc.creatorVittone, Leticia
dc.creatorKranias, Evangelia
dc.date2005-10-13
dc.date2019-10-17T15:53:23Z
dc.identifierhttp://sedici.unlp.edu.ar/handle/10915/83507
dc.identifierissn:0008-6363
dc.descriptionThe sarcoplasmic reticulum (SR) Ca2+-ATPase (SERCA2a) is under the control of a closely associated SR protein named phospholamban (PLN). Dephosphorylated PLN inhibits the SR Ca2+ pump, whereas phosphorylation of PLN, at either Ser16 by PKA or Thr17 by calmodulin-dependent protein kinase II (CaMKII), reverses this inhibition, thus increasing SERCA2a activity and the rate of Ca2+ uptake by the SR. This would in turn lead to an increase in the velocity of relaxation, SR Ca 2+ load, and myocardial contractility. Thus, PLN is a major determinant of cardiac contractility and relaxation. Although in the intact heart, β-adrenoceptor stimulation results in phosphorylation of PLN at both Ser16 and Thr17 residues, the role of Thr17 site has long remained equivocal. In this review, we attempt to highlight the signaling cascade and the physiological relevance of the phosphorylation of this residue in the heart under both physiological and pathological situations.
dc.descriptionFacultad de Ciencias Médicas
dc.formatapplication/pdf
dc.languageen
dc.rightshttp://creativecommons.org/licenses/by-nc-sa/4.0/
dc.rightsCreative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.subjectCiencias Médicas
dc.subjectβ-adrenergic stimulation
dc.subjectAcidosis
dc.subjectPhospholamban
dc.subjectThr17 site phosphorylation
dc.subjectInsuficiencia Cardíaca
dc.subjectIsquemia
dc.titleRole of phospholamban phosphorylation on Thr17 in cardiac physiological and pathological conditions
dc.typeArticulo
dc.typeArticulo


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