Identificador persistente para citar o vincular este elemento: http://hdl.handle.net/10553/48423
Campo DC Valoridioma
dc.contributor.authorLuzardo, Octavio P.en_US
dc.contributor.authorMachín, Rubén P.en_US
dc.contributor.authorDíaz-Chico, Bonifacio N.en_US
dc.contributor.authorFernández, Leandroen_US
dc.date.accessioned2018-11-23T21:39:42Z-
dc.date.available2018-11-23T21:39:42Z-
dc.date.issued2000en_US
dc.identifier.issn0013-7227en_US
dc.identifier.urihttp://hdl.handle.net/10553/48423-
dc.description.abstractWe have demonstrated previously that both rat and human liver microsomes contain a highly specific binding protein for the anabolic steroids stanozolol(ST) and danazol (DA). In this study we solubilized the male rat liver ST-binding protein (STBP) and investigated the following parameters: 1) pharmacological properties, 2) hydrodynamic properties, 3) peptidic composition, 4) the effects of age and hypophysectomy, and 5) inducibility by 17 alpha-ethinyl estradiol. We found that STEP is an integral protein bound to the endoplasmic reticulum. 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS) provided its optimal solubilization without changes in its pharmacological properties, i.e, high specificity for ST and danazol, between natural steroids and ligands of low affinity glucocorticoid-binding sites or of progesterone-binding sites. Hydrodynamic properties of the STEP showed that it has a molecular mass of at least 118 kDa. SDS-PAGE of covalently labeled STEP under nonreducing conditions showed that [H-3]ST binds to a 110-kDa protein. The STEP was resolved under reducing conditions into three peptides of 55, 31, and 22 bDa, respectively. STEP increased from immature to adult rats, and it dramatically decreased after hypophysectomy. Unlike the 22-kDa peptide, both the 55- and 31-kDa peptides drastically decreased in both immature and hypophysectomized rats. 17 alpha-Ethinyl estradiol administration to immature or hypophysectomized rats induced the 55- and 31-kDa [H-3]STBP to a greater extent than the 22-kDa peptide. Thus, STEP appears as an oligomeric protein composed of hormone-regulated peptides. The availability of solubilized STEP and the fact that it can be induced in vivo represent major steps toward the purification and functional significance of this unique steroid-binding protein.en_US
dc.languageengen_US
dc.relation.ispartofEndocrinology (Philadelphia)en_US
dc.sourceEndocrinology[ISSN 0013-7227],v. 141, p. 3377-3387en_US
dc.subject32 Ciencias médicasen_US
dc.subject320502 Endocrinologíaen_US
dc.subject.otherMale-Rat Liveren_US
dc.subject.otherGrowth-Hormoneen_US
dc.subject.otherDexamethasone Bindingen_US
dc.subject.otherEstrogen-Receptoren_US
dc.subject.otherMembrane-Proteinsen_US
dc.subject.otherPlasma-Membraneen_US
dc.subject.otherSitesen_US
dc.subject.otherMicrosomesen_US
dc.subject.otherPurificationen_US
dc.subject.otherInductionen_US
dc.titlePhotoaffinity labeling identification of a specific binding protein for the anabolic steroids stanozolol and danazol: An oligomeric protein regulated by age, pituitary hormones, and ethinyl estradiolen_US
dc.typeinfo:eu-repo/semantics/Articleen_US
dc.typeArticleen_US
dc.identifier.doi10.1210/endo.141.9.7667en_US
dc.identifier.scopus0034457846-
dc.identifier.isi000088872200040-
dc.contributor.authorscopusid6507534124-
dc.contributor.authorscopusid57189610970-
dc.contributor.authorscopusid7003603506-
dc.contributor.authorscopusid7202848203-
dc.description.lastpage3387en_US
dc.description.firstpage3377en_US
dc.relation.volume141en_US
dc.investigacionCiencias de la Saluden_US
dc.type2Artículoen_US
dc.contributor.daisngid418704-
dc.contributor.daisngid2333393-
dc.contributor.daisngid1724161-
dc.contributor.daisngid795544-
dc.description.numberofpages11en_US
dc.utils.revisionen_US
dc.contributor.wosstandardWOS:Luzardo, OP-
dc.contributor.wosstandardWOS:Machin, RP-
dc.contributor.wosstandardWOS:Diaz-Chico, BN-
dc.contributor.wosstandardWOS:Fernandez, L-
dc.date.coverdateEnero 2000en_US
dc.identifier.ulpgcen_US
dc.contributor.buulpgcBU-MEDen_US
dc.description.jcr4,79-
dc.description.jcrqQ1-
dc.description.scieSCIE-
item.grantfulltextnone-
item.fulltextSin texto completo-
crisitem.author.deptGIR IUIBS: Medio Ambiente y Salud-
crisitem.author.deptIU de Investigaciones Biomédicas y Sanitarias-
crisitem.author.deptDepartamento de Ciencias Clínicas-
crisitem.author.deptGIR IUIBS: Bioquímica-
crisitem.author.deptIU de Investigaciones Biomédicas y Sanitarias-
crisitem.author.deptDepartamento de Bioquímica y Biología Molecular, Fisiología, Genética e Inmunología-
crisitem.author.deptGIR IUIBS: Farmacología Molecular y Traslacional-
crisitem.author.deptIU de Investigaciones Biomédicas y Sanitarias-
crisitem.author.deptDepartamento de Ciencias Clínicas-
crisitem.author.orcid0000-0002-4153-3028-
crisitem.author.orcid0000-0002-0944-990X-
crisitem.author.orcid0000-0001-7802-465X-
crisitem.author.parentorgIU de Investigaciones Biomédicas y Sanitarias-
crisitem.author.parentorgIU de Investigaciones Biomédicas y Sanitarias-
crisitem.author.parentorgIU de Investigaciones Biomédicas y Sanitarias-
crisitem.author.fullNamePérez Luzardo, Octavio Luis-
crisitem.author.fullNameDíaz Chico, Juan Carlos-
crisitem.author.fullNameFernández Pérez, Leandro Francisco-
Colección:Artículos
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