Mostrar el registro sencillo del ítem

PKC activation by melatonin modulates vimentin intermediate filament organization in N1E-115 cells

dc.creatorBenítez-King, G.
dc.date.accessioned2017-06-29T04:23:58Z
dc.date.available2017-06-29T04:23:58Z
dc.date.issued2000es_ES
dc.identifier308es_ES
dc.identifier.issn0742-3098es_ES
dc.identifier.urihttp://repositorio.inprf.gob.mx/handle/123456789/5001
dc.identifier.urihttps://doi.org/10.1034/j.1600-079X.2000.290102.xes_ES
dc.language.isoenges_ES
dc.relation29 (1) 8-14 p.es_ES
dc.relationversión del editores_ES
dc.rightsacceso cerradoes_ES
dc.titlePKC activation by melatonin modulates vimentin intermediate filament organization in N1E-115 cellses_ES
dc.typearticlees_ES
dc.contributor.affiliationInst Mexicano Psiquiatria, Dept Neurofarmacol, DIC, Mexico City 14370, DF, Mexico.es_ES
dc.relation.jnabreviadoJ PINEAL RESes_ES
dc.relation.journalJournal Of Pineal Researches_ES
dc.identifier.placeCopenhaguees_ES
dc.date.published2000es_ES
dc.identifier.organizacionInstituto Nacional de Psiquiatría Ramón de la Fuente Muñizes_ES
dc.identifier.doi10.1034/j.1600-079X.2000.290102.xes_ES
dc.description.monthAgoes_ES
dc.description.abstractotrodiomaMelatonin enters cells and causes cytoskeletal rearrangements in unicellular organisms, plants and vertebrates. This pineal secretory product causes microtubule enlargement and neurite outgrowth by a calmodulin antagonism in N1E-115 cells. Recently, direct in vitro activation of protein kinase C by melatonin was described. Vimentin intermediate filaments are attached to microtubules and their organization depends on both microtubule distribution and phosphorylation of specific proteins. Protein kinase C is a serine threonine kinase which phosphorylates vimentin and through this mechanism causes intermediate filament disassembly. In this work the effects of melatonin on protein kinase C activation, content, and subcellular distribution were studied in N1E-115 cells. Also, melatonin effects on vimentin phosphorylation and subcellular distribution were explored. The results show that melatonin both activates and increases protein kinase C content in the membrane-cytoskeletal fraction. Melatonin protein kinase C activation was followed by an increase in both vimentin phosphorylation and by vimentin subcellular redistribution. Moreover, staurosporine, a serine threonine kinase inhibitor, prevented increased vimentin phosphorylation elicited by melatonin. Similar effects to those caused by melatonin were obtained with the protein kinase C activator phorbol 12-myristate 13-acetate. Data support the idea that melatonin modulates vimentin organization through protein kinase C activation.es_ES
dc.subject.koProtein-Kinase-Ces_ES
dc.subject.koStress Fiberses_ES
dc.subject.koIn-Vitroes_ES
dc.subject.koCalmodulines_ES
dc.subject.koInhibitiones_ES
dc.subject.koMdckes_ES
dc.subject.koPhosphorylationes_ES
dc.subject.koCoexpressiones_ES
dc.subject.koAssociationes_ES
dc.subject.koBindinges_ES


Ficheros en el ítem

FicherosTamañoFormatoVer

No hay ficheros asociados a este ítem.

Este ítem aparece en la(s) siguiente(s) colección(ones)

Mostrar el registro sencillo del ítem