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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 |