Evidence for the presence of specific binding sites for corticoids in mouse liver plasma membranes
Autor: | M. J. Sancho, Iñaki Ibarrola, Jose M. Macarulla, Ana Isabel Vallejo, Miguel Trueba, Aida Marino, Isabel Rodriguez |
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Rok vydání: | 1989 |
Předmět: |
Male
medicine.medical_specialty Hydrocortisone Physiology Biophysics Mice Inbred Strains Buffers Cell Fractionation Ouabain Mice chemistry.chemical_compound Adrenal Cortex Hormones Corticosterone Cations Internal medicine medicine Animals Binding site Receptor Binding Sites Chemistry Cell Membrane Osmolar Concentration Temperature Cell Biology Endocrinology Membrane Liver Cortisone hormones hormone substitutes and hormone antagonists Glucocorticoid medicine.drug |
Zdroj: | The Journal of Membrane Biology. 108:115-124 |
ISSN: | 1432-1424 0022-2631 |
DOI: | 10.1007/bf01871023 |
Popis: | The specific binding of [3H]cortisol to plasma membranes purified from mouse liver, studied by the ultrafiltration method, shows the existence of specific binding sites for cortisol. The kinetic parameters of this binding are KD = 4.4 nM and Bmax = 685 fmol/mg protein in presence of 1 microM of corticosterone. With respect to the binding of 4 nM [3H]cortisol to the membrane, the affinities of the steroids decreased in the following order: deoxycorticosterone greater than corticosterone greater than progesterone greater than cortisol greater than prednisolone greater than testosterone greater than 20 beta-hydroxyprogesterone greater than cortisone. Estradiol, dexamethasone, ouabain and triamcinolone acetonide do not have affinity for this binding site. Neither Ca2+ nor Mg2+ affected the binding of [3H]cortisol to the plasma membranes. Likewise, the presence of agonists and antagonists of alpha and beta-adrenergic receptors did not modify the binding of [3H]cortisol. The results suggest that the plasma membrane binding site characterized is more specific for corticoids and is different from nuclear glucocorticoid and progesterone receptors. |
Databáze: | OpenAIRE |
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