Potentiation of Epinephrine-Induced Lipolysis by Catechol Estrogens and Their Methoxy Derivatives*

Ackerman, Gary E.; MacDonald, Paul C.; Gudelsky, Gary A.; Mendelson, Carole R.; Simpson, Evan R.

doi:10.1210/endo-109-6-2084

Cited by 25 publications

(9 citation statements)

References 18 publications

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“…These are direct steroid actions, not mediated through nuclear receptor occupancy (Baulieu et al, 1978). 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: 92%

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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Section: Introductionmentioning

confidence: 92%

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

et al. 1991

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“…Ovariectomy increases lipoprotein lipase and lipid deposition in adipocytes and 17beta-estradiol reverses this increase [177]. On the other hand, 17beta-estradiol can indirectly affect lipolysis by inducing the lipolytic enzyme hormone-sensitive lipase [178] or by increasing the lipolytic effects of adrenaline [179]. Moreover fatty acid oxidation might also be increased, which might contribute to the decrease in AT mass induced by 17beta-estradiol.…”

Section: Estrogen Signaling In Metabolic Inflammationmentioning

confidence: 99%

Estrogen Signaling in Metabolic Inflammation

Monteiro

Teixeira

Calhau

2014

Mediators of Inflammation

160

122

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There is extensive evidence supporting the interference of inflammatory activation with metabolism. Obesity, mainly visceral obesity, is associated with a low-grade inflammatory state, triggered by metabolic surplus where specialized metabolic cells such as adipocytes activate cellular stress initiating and sustaining the inflammatory program. The increasing prevalence of obesity, resulting in increased cardiometabolic risk and precipitating illness such as cardiovascular disease, type 2 diabetes, fatty liver, cirrhosis, and certain types of cancer, constitutes a good example of this association. The metabolic actions of estrogens have been studied extensively and there is also accumulating evidence that estrogens influence immune processes. However, the connection between these two fields of estrogen actions has been underacknowledged since little attention has been drawn towards the possible action of estrogens on the modulation of metabolism through their anti-inflammatory properties. In the present paper, we summarize knowledge on the modification inflammatory processes by estrogens with impact on metabolism and highlight major research questions on the field. Understanding the regulation of metabolic inflammation by estrogens may provide the basis for the development of therapeutic strategies to the management of metabolic dysfunctions.

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“…E2 can indirectly affect lipolysis by inducing the lipolytic enzyme hormone-sensitive lipase (31) or by increasing the lipolytic effects of epinephrine (32). Fatty acid-b oxidation might also be increased, which might contribute to the decrease in adipose tissue deposition induced by E2 (33).…”

Section: Direct Effects Of Estrogen On Adipocytesmentioning

confidence: 99%

Loss of cyclin‐dependent kinase inhibitors produces adipocyte hyperplasia and obesity

et al. 2004

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Adipocyte hyperplasia is characteristic of some forms of human obesity, but the role of adipocyte number in obesity and how normal adipocyte number is established are unclear. Preadipocytes proliferate and then differentiate to become mitotically quiescent adipocytes. This involves exit from the cell cycle, a process regulated by cell cycle inhibitors such as the cyclin-dependent kinase inhibitors (CDKIs) p27 and p21. 3T3-L1 preadipocytes show marked changes in p27 and p21 during differentiation, suggesting CDKIs may regulate establishment of adipocyte number in vivo. To study the role of these CDKIs in adipogenesis, we analyzed adult p27 knockout (p27KO), p21 knockout (p21KO), p27/p21 double knockout (DBKO), and wild-type (WT) mice. Adult DBKO mice weighed 100% more and had fourfold increases in body fat percentage compared with WT. Fat pad weights were increased 80, 90, and 500% in p27KO, p21KO, and DBKO mice, respectively, compared with WT. Adipocyte numbers of p27KO, p21KO, and DBKO mice were 1.9-, 1.7-, and 6.1-fold, respectively, that of WT; adipocyte size was not increased. DBKO mice showed glucose intolerance, insulin insensitivity, hepatic steatosis and dyslipidemia; gradations of these effects occurred in p27KO and p21KO mice. In conclusion, p27KO and p21KO mice are obese because of adipocyte hyperplasia, and DBKO mice have further increases in obesity and adipocyte hyperplasia, indicating that their functions in establishing adipocyte number are not redundant. p27 and p21 are major regulators of adipocyte number in vivo, and knockouts lacking one or both of these proteins provide models for producing adipocyte hyperplasia and understanding its metabolic consequences.

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Potentiation of Epinephrine-Induced Lipolysis by Catechol Estrogens and Their Methoxy Derivatives*

Cited by 25 publications

References 18 publications

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

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

Estrogen Signaling in Metabolic Inflammation

Loss of cyclin‐dependent kinase inhibitors produces adipocyte hyperplasia and obesity

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