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dc.contributor.author Galigniana, Mario Daniel
dc.contributor.author Piwien Pilipuk, Graciela
dc.date.available 2017-11-26T16:17:28Z
dc.date.issued 2004
dc.identifier.citation Galigniana, Mario Daniel; Piwien Pilipuk, Graciela; Activation of the ligand-mineralocorticoid receptor functional unit by ancient, classical, and novel ligands: structure-activity relationship; Elsevier Inc; Vitamins And Hormones Series; 69; -1-2004; 31-68
dc.identifier.issn 0083-6729
dc.identifier.uri http://hdl.handle.net/11336/29122
dc.description.abstract The mineralocorticoid effect on epithelial cells is the resultant of an intricate net of biochemical regulations that ultimately leads to the maintenance of electrolyte homeostasis. Two key protagonists in this plot are the ligand, which broadcasts the information, and the receptor, which functions as a receiver and transducer. Therefore, the responsibility for the final biological effect is not limited to each individual component but to both of them, so they constitute a functional unit. In addition, several prereceptor regulatory mechanisms are also determinant factors for the final biological response. Because steroids are present in both animals and plants and are derived from common precursors, it is intriguing how these simple molecules have acquired specialization to shape biological development and differentiation. This is particularly true for the function of aldosterone in mammals, which is mimicked by glucocorticoids or progesterone in some particular cases. Inasmuch as the most potent mineralocorticoid in nature, aldosterone, shows a poorly angled steroid nucleus at the A?B-ring junction, and because steroids that possess identical functional groups and different steroidal frames elicit different mineralocorticoid effects, we postulate that a planar conformation of the ligand is a key requirement to acquire potent sodium retention properties. The model takes into consideration all the mechanisms involved in the regulation of the final biological effect, although it does not provide a definitive answer to the original question. It is also discussed how the use of novel mineralocorticoid ligands may shed light on the still obscure mechanism of action of the mineralocorticoid receptor.
dc.format application/pdf
dc.language.iso eng
dc.publisher Elsevier Inc
dc.rights info:eu-repo/semantics/restrictedAccess
dc.rights.uri https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject ALDOSTERONE
dc.subject NATRIURESIS
dc.subject MINERALCORTICOIDS
dc.subject MOLECULAR CONFORMATION
dc.subject.classification Bioquímica y Biología Molecular
dc.subject.classification Medicina Básica
dc.subject.classification CIENCIAS MÉDICAS Y DE LA SALUD
dc.title Activation of the ligand-mineralocorticoid receptor functional unit by ancient, classical, and novel ligands: structure-activity relationship
dc.type info:eu-repo/semantics/article
dc.type info:ar-repo/semantics/artículo
dc.type info:eu-repo/semantics/publishedVersion
dc.date.updated 2017-11-16T15:13:32Z
dc.identifier.eissn 0083-6729
dc.journal.volume 69
dc.journal.pagination 31-68
dc.journal.pais Países Bajos
dc.journal.ciudad Amsterdam
dc.description.fil Fil: Galigniana, Mario Daniel. University of Michigan; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil Fil: Piwien Pilipuk, Graciela. University of Michigan; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.journal.title Vitamins And Hormones Series
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0083672904690029?via%3Dihub
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/S0083-6729(04)69002-9
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/pmid/15196878


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    Articulos de INST.DE BIOLOGIA Y MEDICINA EXPERIMENTAL (I)

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info:eu-repo/semantics/restrictedAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Atribución-NoComercial-SinDerivadas 2.5 Argentina (CC BY-NC-ND 2.5 AR)