An Early Effect of Cortisol, Previous to its Glycogenogenic Action

M, Egaña; Mj, Sancho; Jm, Macarulla

doi:10.1055/s-2007-1019351

Cited by 15 publications

(10 citation statements)

References 6 publications

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“…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%

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: 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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“…While we did not measure gluconeogenesis earlier than 3 h, the observed increase in blood glucose may have been due to a combination of effects, including an increase in gluconeogenesis, an increase in glycogen breakdown and\or a decrease in glucose utilization. Earlier work in chickens demonstrated that cortisol increases glycogen breakdown as early as 45 min [21], so that some of the observed increase in blood glucose may have been due to liver glycogen mobilization [19,21]. Unfortunately, blood samples were not obtained at 1 or 2 h to determine the early effects of cortisol on glycogenolysis or gluconeogenesis.…”

Section: Discussionmentioning

confidence: 98%

Cortisol increases gluconeogenesis in humans: its role in the metabolic syndrome

2001

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Android obesity is associated with increased cortisol secretion. Direct effects of cortisol on gluconeogenesis and other parameters of insulin resistance were determined in normal subjects. Gluconeogenesis was determined using the reciprocal pool model of Haymond and Sunehag (HS method), and by the Cori cycle/lactate dilution method of Tayek and Katz (TK method). Glucose production (GP) and gluconeogenesis were measured after a 3 h baseline infusion and after a 4-8 h pituitary-pancreatic infusion of somatostatin, replacement insulin, growth hormone (GH), glucagon and a high dose of cortisol (hydrocortisone). The pituitary-pancreatic infusion maintains insulin, GH and glucagon concentrations within the fasting range, while increasing the concentration of only one hormone, cortisol. Two groups of five subjects were each given high-dose cortisol administration, and results were compared with those from a group of six 'fasting alone' subjects (no infusion) at 16 and 20 h of fasting. Fasting GP (12 h fasting) was similar in all groups, averaging 12.5+/-0.2 micromol x min(-1) x kg(-1). Gluconeogenesis, as a percentage of GP, was 35+/-2% using the HS method and 40+/-2% using the TK method. After 16 h of fasting, GP had fallen (11.5+/-0.6 micromol x min(-1) x kg(-1)) and gluconeogenesis had increased (55+/-5% and 57+/-5% of GP by the HS and TK methods respectively; P<0.05). High-dose cortisol infusion for 4 h increased serum cortisol (660+/-30 nmol/l; P<0.05), blood glucose (7.9+/-0.5 mmol/l; P<0.05) and GP (14.8+/-0.8 micromol x min(-1) x kg(-1); P<0.05). The increase in GP was due entirely to an increase in gluconeogenesis, determined by either the HS or the TK method (66+/-6% and 65+/-5% of GP respectively; P<0.05). Thus cortisol administration in humans increases GP by stimulating gluconeogenesis. Smaller increases in serum cortisol may contribute to the abnormal glucose metabolism known to occur in the metabolic syndrome.

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“…This nuclear effect of glucocorticoids on the enzymes of glycogen metabolism has been recently documented by Hers (1985). However, in contrast with it, an early glycogenolytic effect, independent of protein synthesis enhancement, has been accounted (Egaña et al, 1981;Vallejo et al, 1986;Sancho et al, 1986), in animals treated with cortisol or other steroid hormones (Diez et al, 1984;Sánchez-Bueno et al, 1987). Dexamethasone, a synthetic analogue of cortisol, also elicits phosphorylase activation (Fig.…”

Section: Discussionmentioning

confidence: 86%

“…It has been shown by in vivo experimentation in liver that cortisol causes a glyoogenolytic effect 45 min after hormone administration. This effect is previous to the protein synthesis enhancement shown by the glucocorticoid between 2-3 h after hormone injection (Egaña et al, 1981;Vallejo et al, 1986). The event is due to an increase in glycogen mobilization associated to an activation of glycogen phosphorylase a; in addition, the liver cAMP levels falls and the cGMP levels increase (Sancho et al, 1986;Sánchez-Bueno et al, 1987).…”

Section: Introthictionmentioning

confidence: 85%

Increased Phospholipid Methylation and Glycogen Phosphorylase Activation after a Single Dose of Dexamethasone in Mouse Liver

Marino

Bartolomé²,

Trueba³

et al. 2009

Exp Clin Endocrinol Diabetes

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Two different effects on phospholipid methylation and glycogen phosphorylase a activation were accomplished by treating mice livers with dexamethasone. A biphasic effect on the glycogen phosphorylase a was determined in the homogenated liver of dexamethasone-treated animals: The enzymatic activity increased between 45 to 90 min and decreased about 3 h. Moreover, the increased activity of glycogen phosphorylase a was also found in adrenalectomized mice. Also, the incorporation of ethanolamine into PE1) and PC1) after 15 min of hormone-administration was 77% and 270%, respectively, over the control values. The increase in phospholipid methylation was maintained during the first hour. After 4 h the hormone-treated animals also showed significant differences compared to the controls. Finally, studies of total lipid phosphorus content in the liver fail to show any differences between control and hormone-treated mice.

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An Early Effect of Cortisol, Previous to its Glycogenogenic Action

Cited by 15 publications

References 6 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

Cortisol increases gluconeogenesis in humans: its role in the metabolic syndrome

Increased Phospholipid Methylation and Glycogen Phosphorylase Activation after a Single Dose of Dexamethasone in Mouse Liver

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