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      Adiponectin: A New Regulator of Female Reproductive System

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          Abstract

          Adiponectin is the hormone that belongs to the group of adipokines, chemical agents mainly derived from the white adipose tissue. The hormone plays pleiotropic roles in the organism, but the most important function of adiponectin is the control of energy metabolism. The presence of adiponectin and its receptors in the structures responsible for the regulation of female reproductive functions, such as hypothalamic-pituitary-gonadal (HPG) axis, indicates that adiponectin may be involved in the female fertility regulation. The growing body of evidence suggests also that adiponectin action is dependent on the actual and hormonal status of the animal. Present study presents the current knowledge about the presence and role of adiponectin system (adiponectin and its receptors: AdipoR1 and AdipoR2) in the ovaries, oviduct, and uterus, as well as in the hypothalamus and pituitary, the higher branches of HPG axis, involved in the female fertility regulation.

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          Most cited references96

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          Cloning of adiponectin receptors that mediate antidiabetic metabolic effects.

          Adiponectin (also known as 30-kDa adipocyte complement-related protein; Acrp30) is a hormone secreted by adipocytes that acts as an antidiabetic and anti-atherogenic adipokine. Levels of adiponectin in the blood are decreased under conditions of obesity, insulin resistance and type 2 diabetes. Administration of adiponectin causes glucose-lowering effects and ameliorates insulin resistance in mice. Conversely, adiponectin-deficient mice exhibit insulin resistance and diabetes. This insulin-sensitizing effect of adiponectin seems to be mediated by an increase in fatty-acid oxidation through activation of AMP kinase and PPAR-alpha. Here we report the cloning of complementary DNAs encoding adiponectin receptors 1 and 2 (AdipoR1 and AdipoR2) by expression cloning. AdipoR1 is abundantly expressed in skeletal muscle, whereas AdipoR2 is predominantly expressed in the liver. These two adiponectin receptors are predicted to contain seven transmembrane domains, but to be structurally and functionally distinct from G-protein-coupled receptors. Expression of AdipoR1/R2 or suppression of AdipoR1/R2 expression by small-interfering RNA supports our conclusion that they serve as receptors for globular and full-length adiponectin, and that they mediate increased AMP kinase and PPAR-alpha ligand activities, as well as fatty-acid oxidation and glucose uptake by adiponectin.
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            A novel serum protein similar to C1q, produced exclusively in adipocytes.

            We describe a novel 30-kDa secretory protein, Acrp30 (adipocyte complement-related protein of 30 kDa), that is made exclusively in adipocytes and whose mRNA is induced over 100-fold during adipocyte differentiation. Acrp30 is structurally similar to complement factor C1q and to a hibernation-specific protein isolated from the plasma of Siberian chipmunks; it forms large homo-oligomers that undergo a series of post-translational modifications. Like adipsin, secretion of Acrp30 is enhanced by insulin, and Acrp30 is an abundant serum protein. Acrp30 may be a factor that participates in the delicately balanced system of energy homeostasis involving food intake and carbohydrate and lipid catabolism. Our experiments also further corroborate the existence of an insulin-regulated secretory pathway in adipocytes.
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              cDNA cloning and expression of a novel adipose specific collagen-like factor, apM1 (AdiPose Most abundant Gene transcript 1).

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                Author and article information

                Contributors
                Journal
                Int J Endocrinol
                Int J Endocrinol
                IJE
                International Journal of Endocrinology
                Hindawi
                1687-8337
                1687-8345
                2018
                29 April 2018
                : 2018
                : 7965071
                Affiliations
                Department of Animal Physiology, Faculty of Biology and Biotechnology, University of Warmia and Mazury in Olsztyn, Oczapowskiego 1A, 10-719 Olsztyn-Kortowo, Poland
                Author notes

                Academic Editor: Joëlle Dupont

                Author information
                http://orcid.org/0000-0003-0997-7355
                http://orcid.org/0000-0002-8677-5282
                http://orcid.org/0000-0003-1643-026X
                Article
                10.1155/2018/7965071
                5949163
                29853884
                d92d82fb-c570-47ef-8e11-0891e931575f
                Copyright © 2018 Kamil Dobrzyn et al.

                This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 20 December 2017
                : 11 March 2018
                : 22 March 2018
                Categories
                Review Article

                Endocrinology & Diabetes
                Endocrinology & Diabetes

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