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Epidemiology of Childhood Obesity in Korea
Ha, Kyoung Hwa,Kim, Dae Jung Korean Endocrine Society 2016 Endocrinology and metabolism Vol.31 No.4
<P>Over the past several decades, the prevalence of obesity has increased dramatically worldwide and is increasing not only in developed countries, but also in developing countries. This increase may lead to an increase in the incidence of chronic diseases throughout the lifespan. In Korean children and adolescents, the prevalence of obesity increased from 6.8% in 1998 to 10.0% in 2013. Obesity is a state that more commonly influences children and adolescents of lower socioeconomic status (SES) than those with a higher SES. However, the prevalence of metabolic syndrome in a nationally representative sample of Korean adolescents decreased from 1998 to 2012. According to the Diabetes Fact Sheet of the Korean Diabetes Association, the prevalence of type 2 diabetes among children aged 18 years or younger was 153.5 per 100,000 in 2006 and 205.0 per 100,000 in 2013. Obesity is a complex disease influenced by many interacting factors, such as adipocytokines, lipopolysaccharide-binding protein, adenovirus 36 infection, birth weight, lifestyle, and endocrine-disrupting chemicals. Obesity in youth can adversely impact practically every organ system and lead to serious consequences, such as metabolic, gastrointestinal, pulmonary, cardiovascular, and psychosocial complications. Therefore, coordinated efforts by governments, organizations, communities, and individuals are needed to prevent and treat childhood obesity. In particular, a long-term policy to improve the social environment will also be necessary.</P>
Chung, Hyunju,Chung, Ho-Yeon,Bae, Chong Woo,Kim, Chong-Jin,Park, Seungjoon The Japan Endocrine Society 2011 Endocrine journal Vol.58 No.5
<P>Ghrelin functions as a neuroprotective agent and rescues neurons from various insults. However, the molecular mechanisms underlying ghrelin neuroprotection remains to be elucidated. An accumulation of unfolded proteins in the endoplasmic reticulum (ER) leads to ER stress and then induces ER stress-mediated cell death. Here, we report that acylated ghrelin inhibited tunicamycin- or thapsigargin-triggered ER stress-induced apoptotic cell death in primary rat cortical neurons. An analysis using a specific inhibitor of phosphatidylinositol-3-kinase (PI3K), LY294002, showed that ghrelin prevented apoptosis via the activation of PI3K signaling pathway. Ghrelin suppressed tunicamycin- or thapsigargin-induced upregulation and nuclear translocation of C/EBP homologous protein (CHOP). Ghrelin also inhibited tunicamycin or thapsigargin induction of PRK-like ER kinase (PERK), eukaryotic translation initiation factor-2α (eIF2α) and activating transcription factor (ATF) 4. Exposure of cells to tunicamycin or thapsigargin resulted in nuclear translocation of forkhead box protein O1 (Foxo1), which was reduced by pretreatment with ghrelin. The protective effect of ghrelin was accompanied by an increased phosphorylation of Akt and glycogen synthase kinase (GSK)-3β. Furthermore, ghrelin phosphorylated and inactivated pro-apoptotic BAD and Foxo1. In addition, phospho-Akt was translocated to the nucleus in response to ghrelin and PI3K inhibition by LY294002 prevented ghrelin-induced effect on phospho-Akt localization. Our study suggests that suppression of CHOP activation via the inhibition of PERK/eIF2α/ATF4 pathway and prevention of Foxo1 activation and nuclear translocation may contribute to ghrelin-mediated neuroprotection during ER stress responses. Our data also suggest that PI3K/Akt-mediated inactivation of GSK-3β, BAD and Foxo1 may be associated with the anti-apoptotic effect of ghrelin.</P>