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      Growth Hormone and Adipocyte Function in Obesity

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          In obesity, growth hormone (GH) secretion is impaired which is considered a consequence rather than a cause of obesity. GH regulates the expression of GH receptor and the synthesis of insulin-like growth factor I (IGF-I) in adipocytes. Although GH hyposecretion in obesity may decrease the generation of IGF-I in each adipocyte, increased amounts of IGF-I and GH-binding protein could be secreted from the excessively enlarged amounts of adipose tissue. This may contribute to the normal/high serum-IGF-I and high GH-binding protein levels in obesity. Hyperinsulinemia and increased GH receptor activity may also affect the GH-IGF-I axis. Favorable effects of GH treatment have been observed in obese children and adults. GH treatment decreases adiposity, reduces triglyceride accumulation by inhibiting lipoprotein lipase and enhances lipolysis both via increased hormone-sensitive lipase activity and via induction of beta adrenoreceptors. GH treatment also has a favorable effect on obesity-associated dyslipidemia, but the effects on insulin sensitivity have been conflicting.

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          Most cited references 18

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          Do obese children become obese adults? A review of the literature.

          Obese children may be at increased risk of becoming obese adults. To examine the relationship between obesity in childhood and obesity in adulthood, we reviewed the epidemiologic literature published between 1970 and July 1992. Comparison between studies was complicated by differences in study design, definitions of obesity, and analytic methods used. Although the correlations between anthropometric measures of obesity in childhood and those in adulthood varied considerably among studies, the associations were consistently positive. About a third (26 to 41%) of obese preschool children were obese as adults, and about half (42 to 63%) of obese school-age children were obese as adults. For all studies and across all ages, the risk of adult obesity was at least twice as high for obese children as for nonobese children. The risk of adult obesity was greater for children who were at higher levels of obesity and for children who were obese at older ages. The wide range of estimates in this literature are, in part, due to differences in study designs, definitions of obesity, ages at which participants were measured, intervals between measurements, and population and cultural differences.
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            Inhibition of Adipogenesis Through MAP Kinase-Mediated Phosphorylation of PPAR 

             P Sarraf,  J. B. Kim,  E Hu (1996)
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              Insulin-like growth factor binding proteins and their role in controlling IGF actions.

              The insulin-like growth factor binding proteins (IGFBPs) are a family of six proteins that bind to insulin-like growth factor-I and -II with very high affinity. Because their affinity constants are between two- and 50-fold greater than the IGF-I receptor, they control the distribution of the IGFs among soluble IGFBPs in interstitial fluids, IGFBPs bound to cell surfaces or extracellular matrix (ECM) and cell surface receptors. Although there are six forms of insulin-like growth factor binding proteins, most interstitial fluids contain only three or four forms, and usually only one or two predominate. The proteins differ significantly in their biochemical characteristics, and this accounts for many of the differences that have been observed in their biological actions. Several different types of protease cleave these binding proteins. Proteolytic cleavage generally inactivates the binding proteins or reduces their ability to bind to IGF-I or -II substantially. Several cell types have been shown to secrete these proteases; therefore, the factors that regulate protease activity can control binding protein actions indirectly. Other post-translational modifications, such as glycosylation and phosphorylation, have been shown to alter IGF binding protein activity. While binding protein actions have been studied extensively in vitro, many of the in vivo activities of these proteins remain to be defined.

                Author and article information

                Horm Res Paediatr
                Hormone Research in Paediatrics
                S. Karger AG
                July 2000
                17 November 2004
                : 53
                : Suppl 1
                : 87-97
                aDivision of Endocrinology, Department of Internal Medicine, Yonsei University College of Medicine, Seoul, Korea; bDepartment of Pediatrics, Endocrine Research Unit, Karolinska Institute, Huddinge University Hospital, Stockholm, Sweden
                53211 Horm Res 2000;53(suppl 1):87–97
                © 2000 S. Karger AG, Basel

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                Page count
                Figures: 3, References: 151, Pages: 11


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