Please use this identifier to cite or link to this item: http://hdl.handle.net/10553/43072
Title: Solubilization and photoaffinity labeling identification of glucocorticoid binding peptides in endoplasmic reticulum from rat liver
Authors: Pérez-Machín, Rubén
Henríquez-Hernández, Luis 
Pérez-Luzardo, Octavio 
Betancor-Hernández, Eva 
Tabares-Domínguez, Ezequiel
Mateos-Díaz, Carlos
Novoa-Mogollón, Javier
Díaz-Chico, B. N. 
Fernández, Leandro 
Keywords: Membrane-Proteins
Steroid-Hormones
Microsomes
Sites
Androgens
Purification
Expression
Stanozolol
Danazol
Issue Date: 2003
Publisher: 0960-0760
Journal: Journal of Steroid Biochemistry and Molecular Biology 
Conference: 15th International Symposium of the Journal-of-Steroid-Biochemistry-and-Molecular-Biology 
Abstract: Steroid-binding proteins unrelated to the classical nuclear receptors have been proposed to play a role in non-genomic effects of steroid hormones. We have previously described that the low-affinity glucocorticoid binding protein (LAGS), present in the endoplasmic reticulum of the mate rat liver, has pharmacological and biochemical properties different from those of nuclear receptors. The LAGS is under multihormonal regulation and binds glucocorticoids, progestins, and synthetic steroids but is unable to bind either estradiol, testosterone, or triamcinolone acetonide. In this study, we have solubilized the LAGS and investigated their pharmacological and hydrodynamic properties and their peptide composition. We found that LAGS is an integral protein bound to the endoplasmic reticulum. CHAPS provided its optimal solubilization without changes in its pharmacological properties. Hydrodynamic properties of LAGS showed that it has a molecular mass of at least 135 kDa. SDS-PAGE of covalently-labeled LAGS showed that [H-3]dexamethasone binds two peptides of 53 and 37 kDa, respectively. Thus, the LAGS appears as an oligomeric protein under multihormonal regulation. The availability of solubilized LAGS and the fact that it can be induced in vivo represent major steps toward purification and understanding the functional significance of this unique steroid-binding protein. (C) 2003 Elsevier Science Ltd. All rights reserved.
URI: http://hdl.handle.net/10553/43072
ISSN: 0960-0760
DOI: 10.1016/S0960-0760(03)00038-4
Source: Journal of Steroid Biochemistry and Molecular Biology[ISSN 0960-0760],v. 84, p. 245-253
Appears in Collections:Actas de congresos
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