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dc.date.accessioned 2021-08-23T15:33:05Z
dc.date.available 2021-08-23T15:33:05Z
dc.date.issued 1996-12-27
dc.identifier.uri http://sedici.unlp.edu.ar/handle/10915/123153
dc.description.abstract Phosphorylation site-specific antibodies, quantification of 32P incorporation into phospholamban, and simultaneous measurements of mechanical activity were used in Langendorff-perfused rat hearts to provide further insights into the underlying mechanisms of phospholamban phosphorylation. Immunological detection of phospholamban phosphorylation sites showed that the isoproterenol concentration-dependent increase in phospholamban phosphorylation was due to increases in phosphorylation of both Ser16 and Thr17 residues. When isoproterenol concentration was increased at extremely low Ca²⁺ supply to the myocardium, phosphorylation of Thr17 was virtually absent. Under these conditions, 32P incorporation into phospholamban, due to Ser16, decreased by 50%. Changes in Ca²⁺ supply to the myocardium either at constant β-adrenergic stimulation or in the presence of okadaic acid, a phosphatase inhibitor, exclusively modified Thr17 phosphorylation. Changes in phospholamban phosphorylation due to either Ser16 and/or Thr17 were paralleled by changes in myocardial relaxation. The results indicate that cAMP- (Ser16) and Ca²⁺-calmodulin (Thr17)-dependent pathways of phospholamban phosphorylation can occur independently of each other. However, in the absence of β-adrenergic stimulation, phosphorylation of Thr17 could only be detected after simultaneous activation of Ca²⁺-calmodulin-dependent protein kinase and inactivation of phosphatase. It is suggested that under physiological conditions, this requisite is only filled by cAMP-dependent mechanisms. en
dc.format.extent 33561-33567 es
dc.language en es
dc.subject Rats es
dc.subject Phosphorylation es
dc.subject Heart es
dc.subject Phospholamban es
dc.subject Isoproterenol es
dc.title Immunodetection of phosphorylation sites gives new insights into the mechanisms underlying phospholamban phosphorylation in the intact heart en
dc.type Articulo es
sedici.identifier.other pmid:8969222 es
sedici.identifier.other doi:10.1074/jbc.271.52.33561 es
sedici.identifier.issn 0021-9258 es
sedici.creator.person Mundiña-Weilenmann, Cecilia es
sedici.creator.person Vittone, Leticia Beatriz es
sedici.creator.person Ortale, Manuel es
sedici.creator.person Chiappe de Cingolani, Gladys Ethel es
sedici.creator.person Mattiazzi, Alicia Ramona es
sedici.subject.materias Medicina es
sedici.subject.materias Biología es
sedici.description.fulltext true es
mods.originInfo.place Facultad de Ciencias Médicas es
mods.originInfo.place Centro de Investigaciones Cardiovasculares es
sedici.subtype Articulo es
sedici.rights.license Creative Commons Attribution 4.0 International (CC BY 4.0)
sedici.rights.uri http://creativecommons.org/licenses/by/4.0/
sedici.description.peerReview peer-review es
sedici.relation.journalTitle The Journal of Biological Chemistry es
sedici.relation.journalVolumeAndIssue vol. 271, no. 52 es


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Creative Commons Attribution 4.0 International (CC BY 4.0) Excepto donde se diga explícitamente, este item se publica bajo la siguiente licencia Creative Commons Attribution 4.0 International (CC BY 4.0)