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Melatonin stimulates calmodulin phosphorylation by protein kinase C.

dc.creatorSoto-Vega, Elena
dc.creatorMeza, Isaura
dc.creatorRamírez-Rodríguez, Gerardo
dc.creatorBenítez-King, Gloria
dc.date.accessioned2017-06-29T04:33:12Z
dc.date.available2017-06-29T04:33:12Z
dc.date.issued2004es_ES
dc.identifier430es_ES
dc.identifier.issn0742-3098es_ES
dc.identifier.urihttp://repositorio.inprf.gob.mx/handle/123456789/5119
dc.identifier.urihttps://doi.org/10.1111/j.1600-079X.2004.00141.xes_ES
dc.language.isoenges_ES
dc.relation37 (2) 98-106 p.es_ES
dc.relationversión del editores_ES
dc.rightsacceso cerradoes_ES
dc.titleMelatonin stimulates calmodulin phosphorylation by protein kinase C.es_ES
dc.typearticlees_ES
dc.contributor.affiliationDepto. Neurofarmacología, Subdirección de Investigaciones Clínicas, Instituto Nacional de Psiquiatría, México.es_ES
dc.relation.jnabreviadoJ PINEAL RESes_ES
dc.relation.journalJournal of pineal researches_ES
dc.date.published2004es_ES
dc.identifier.organizacionInstituto Nacional de Psiquiatría Ramón de la Fuente Muñizes_ES
dc.identifier.doi10.1111/j.1600-079X.2004.00141.xes_ES
dc.description.monthSepes_ES
dc.description.abstractotrodiomaCalmodulin (CaM)-dependent processes can be modulated by the availability of Ca(+2), the subcellular distribution of both CaM and its target proteins, CaM antagonism, and post-translational modifications such as CaM phosphorylation. Melatonin, the pineal secretory product synthesized during the dark phase of the photoperiod is an endogenous CaM antagonist. This indolamine causes CaM subcellular redistribution in epithelial MDCK and MCF-7 cells, and selectively activates protein kinase C alpha (PKC alpha) in neuronal N1E-115 cells. In the present work we have characterized the phosphorylation of CaM mediated by PKC alpha and its stimulation by melatonin in an in vitro reconstituted enzyme system. Additionally, the participation of MAPK and ERKs, downstream kinases of the PKC signaling pathway, was explored utilizing MDCK cell extracts as source of these kinases. Phosphorylation of CaM was characterized in the whole cells by MDCK cell metabolic labeling with [(32)P]-orthoposhospate, and CaM separation by sodium dodecyl sulphate-polyacrylamide gel electrophoresis, as well as by immunocolocalization of phosphorylated threonine/serine residues and CaM in cultured cells incubated with melatonin. Our results show that melatonin increased CaM phosphorylation by PKC alpha with an EC(50) of 10(-8) m in the presence of the phorbol ester, phorbol-12-myristate-13-acetate (PMA) in the in vitro reconstituted enzyme system. An increase in phosphorylated CaM was also observed in cells cultured with melatonin, or PMA for 2 hr, while, PKC, MAPK, or ERK inhibitors abolished CaM phosphorylation elicited by melatonin in MDCK cell extracts. Our data show that melatonin can stimulate phosphorylation of CaM by PKC alpha in the in vitro reconstituted system and suggest that in MDCK cells this phosphorylation is accomplished by PKC. Modification of CaM by melatonin can be another route to inhibit CaM interaction with its target enzymeses_ES
dc.subject.meshmCell Extractses_ES
dc.subject.meshmCell Linees_ES
dc.subject.meshmTumores_ES
dc.subject.meshmDogses_ES
dc.subject.meshmDose-Response Relationshipes_ES
dc.subject.meshmDruges_ES
dc.subject.meshmEnzyme Activation-Physiologyes_ES
dc.subject.meshmEnzyme Inhibitors-Pharmacologyes_ES
dc.subject.meshmHumanses_ES
dc.subject.meshmMelatonines_ES
dc.subject.meshmMicroscopyes_ES
dc.subject.meshmFluorescencees_ES
dc.subject.meshmMitogen-Activated Protein Kinase Kinases-Metabolismes_ES
dc.subject.meshmPhosphorylation-Drug effectses_ES
dc.subject.meshmProtein Kinase Ces_ES
dc.subject.meshmSignal Transduction-Drug effectses_ES
dc.subject.meshmTetradecanoylphorbol Acetate-Analogs & derivativeses_ES
dc.subject.kwCalmodulinaes_ES
dc.subject.kwMelatoninaes_ES
dc.subject.kwFosforilaciónes_ES
dc.subject.kwProteína quinasa Ces_ES
dc.subject.koCalmodulines_ES
dc.subject.koMelatonines_ES
dc.subject.koPhosphorylationes_ES
dc.subject.koProtein kinase Ces_ES


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