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dc.creatorBenítez-King, G.
dc.creatorAntón-Tay, F.
dc.date.accessioned2017-06-29T04:16:33Z
dc.date.available2017-06-29T04:16:33Z
dc.date.issued1993es_ES
dc.identifier158es_ES
dc.identifier.issn0014-4754es_ES
dc.identifier.urihttp://repositorio.inprf.gob.mx/handle/123456789/4852
dc.identifier.urihttps://doi.org/10.1007/BF01923944es_ES
dc.language.isoenges_ES
dc.relation49 (8) 635-641 p.es_ES
dc.relationversión del editores_ES
dc.rightsacceso cerradoes_ES
dc.titleCalmodulin mediates melatonin cytoskeletal effectses_ES
dc.typearticlees_ES
dc.contributor.affiliationInstituto Mexicano de Psiquiatría, Departamento de Neurofarmacologia, Col. San Lorenzo Huipulco, México.es_ES
dc.relation.jnabreviadoEXPERIENTIAes_ES
dc.relation.journalExperientiaes_ES
dc.identifier.placeSwitzerlandes_ES
dc.date.published1993es_ES
dc.identifier.organizacionInstituto Mexicano de Psiquiatríaes_ES
dc.identifier.doi10.1007/BF01923944es_ES
dc.description.monthAgoes_ES
dc.description.abstractotrodiomaIn this article, we review the data concerning melatonin interactions with calmodulin. The kinetics of melatonin-calmodulin binding suggest that the hormone modulates cell activity through intracellular binding to the protein at physiological concentration ranges. Melatonin interaction with calmodulin may allow the hormone to modulate rhythmically many cellular functions. Melatonin's effect on tubulin polymerization, and cytoskeletal changes in MDCK and N1E-115 cells cultured with melatonin, suggest that at low concentrations (10(-9) M) cytoskeletal effects are mediated by its antagonism to Ca2+-calmodulin. At higher concentrations (10(-5)M) non-specific binding of melatonin to tubulin occurs thus overcoming the specific melatonin antagonism to Ca2+-calmodulin. Since the structures of melatonin and calmodulin are phylogenetically well preserved, calmodulin-melatonin interaction probably represents a major mechanism for regulation and synchronization of cell physiology.es_ES


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