An early effect of estradiol at hepatic level, previous to its protein synthesis activation

Sanchez-Bueno, A; Sancho, María J.; Trueba, Miguel; Macarulla, J. M.

doi:10.1016/0020-711x(87)90129-7

Cited by 13 publications

(14 citation statements)

References 23 publications

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“…In our case, we believe that the molecular process by which cortisol binds to plasma membrane sites probably originated the early glycogenolytic effect previously cited (Diez et al, 1984;Vallejo et al, 1986;Sanchez-Bueno et al, 1987). This glycogenolytic effect could be affected by the interaction between the membrane binding site and the steroid.…”

Section: Discussionmentioning

confidence: 65%

“…Previous studies in our laboratory have shown that cortisol, estradiol and testosterone have a glycogenolytic effect on chicken liver (Egafia, Sancho & Macarulla, 1981;Dfez et al, 1984;Sancho et al, 1986;Sanchez-Bueno et al, 1987). This effect is previous to and independent of protein synthesis activation, and it is accompanied by a decrease in the cAMP levels and by an increase in cGMP.…”

Section: Introductionmentioning

confidence: 73%

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Evidence for the presence of specific binding sites for corticoids in mouse liver plasma membranes

et al. 1989

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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.

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Section: Discussionmentioning

confidence: 65%

Section: Introductionmentioning

confidence: 73%

Evidence for the presence of specific binding sites for corticoids in mouse liver plasma membranes

et al. 1989

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“…Some of these steroid effects are: anaesthetics (Holzbauer, 1976) and changes on cell excitability (Batra, 1980;Van Wilgenburg, 1982), on cyclic nucleotide levels (Sadler & Maller, 1982;, on extraneuronal uptake (Rascher et at., 1980), on ion (Wehling, Kasmayr & Theisen, 1989), glucose (Livingston & Lockwood, 1975) and nucleoside (Gagne, Homo & Duval, 1980) transport, on lysosomes (Szego & Pietras, 1984) and as regulators of enzyme activities (Ackerman et al, 1981). In our laboratory we have found a short-time glycogenolytic effect in liver after steroid injection that is protein synthesis independent, and it provokes a decrease of cAMP levels with several steroid hormones (Diez et al, 1984;Sancho et al, 1986Sancho et al, , 1988Vallejo et al, 1986;Sanchez-Bueno et al, 1987).…”

Section: Introductionmentioning

confidence: 69%

Specific binding sites for corticosterone in isolated cells and plasma membrane from rat liver

et al. 1991

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The specific binding of [3H]corticosterone to hepatocytes is a nonsaturable, reversible and temperature-dependent process. The binding to liver purified plasma membrane fraction is also specific, reversible and temperature dependent but it is saturable. Two types of independent and equivalent binding sites have been determined from hepatocytes. One of them has high affinity and low binding capacity (KD = 8.8 nM and Bmax = 1477 fmol/mg protein) and the other one has low affinity and high binding capacity (KD = 91 nM and Bmax = 9015 fmol/mg). In plasma membrane only one type of binding site has been characterized (KD = 11.2 nM and Bmax = 1982 fmol/mg). As it can be deduced from displacement data obtained in hepatocytes and plasma membrane the high affinity binding sites are different from the glucocorticoid, progesterone nuclear receptors and the Na+,K(+)-ATPase digitalis receptor. Probably it is of the same nature that the one determinate of [3H]cortisol and [3H]corticosterone in mouse liver plasma membrane. Beta- and alpha-adrenergic antagonists as propranolol and phentolamine did not affect [3H]corticosterone binding to hepatocytes and plasma membranes; therefore, these binding sites are independent of adrenergic receptors. The binding sites in hepatocytes and plasma membranes are not exclusive for corticosterone but other steroids are also bound with very different affinities.

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“…Our results show (Fig. 4) that progesterone, not only did not increase the cellular cAMP levels in liver, but it even caused a depletion in those levels 7.5 h after injection, So, as in the case of estradiol (Sanchez-Bueno et al, 1987), cAMP depletion occurs a little after glycogen phosphorylase activation.…”

Section: Resultsmentioning

confidence: 47%

“…Studies from this laboratory have demonstrated that several steroid hormones display a glycogenolytic action, independent of their protein synthesis activation effects. Cortisol (Egafla et aL, 1981;Sancho et al, 1986;Vallejo et al, 1986), testosterone (Diez et al, 1984) and estradiol (Sanchez-Bueno et al, 1987) are able to activate liver glycogen phosphorylase without enhancing cAMP levels. However, cGMP levels are increased concomitantly or little after phosphorylase activation, cAMP levels are, on the other hand, significantly depleted.…”

Section: Introductionmentioning

confidence: 99%

Glycogen Phosphorylase Activation by Progesterone in Liver

Gómez-Muñoz²,

Sanchez-Bueno³

et al. 2009

Exp Clin Endocrinol Diabetes

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Glycogen phosphorylase activity is increased before protein synthesis activation by progesterone. This effect is not blocked by antibiotics (actinomycin D and cycloheximide) that are known to inhibit mRNA or protein synthesis. At times similar to those of phosphorylase activation, cAMP are not enhanced, as would be expected considering the classical glycogenolytic cascade, but depleted with respect to control values. A little earlier, cGMP levels are significantly increased.

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An early effect of estradiol at hepatic level, previous to its protein synthesis activation

Cited by 13 publications

References 23 publications

Evidence for the presence of specific binding sites for corticoids in mouse liver plasma membranes

Evidence for the presence of specific binding sites for corticoids in mouse liver plasma membranes

Specific binding sites for corticosterone in isolated cells and plasma membrane from rat liver

Glycogen Phosphorylase Activation by Progesterone in Liver

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