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Preemptive Medicine and Lifestyle Related Disease Research Center, Kyoto University Hospital, Kyoto, Japan
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, and adipose tissue ( Usdin et al . 1993 , Seino et al . 2013 , Joo et al . 2017 ), and the expression levels of GIPR mRNA did not differ among the three groups ( Fig. 4A ). Expression levels of adiponectin mRNA in adipose tissue were significantly
Department of Molecular Biosciences, Department of Nutrition, Department of Pediatrics, Department of Physiology, Division of Endocrinology, School of Veterinary Medicine, University of California Davis, One Shields Avenue, Davis, California 95616, USA
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Department of Molecular Biosciences, Department of Nutrition, Department of Pediatrics, Department of Physiology, Division of Endocrinology, School of Veterinary Medicine, University of California Davis, One Shields Avenue, Davis, California 95616, USA
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), proinsulin (B), glucagon (C), and leptin (D). +++ P <0.001, + P <0.05 by one-factor ANOVA, *** P <0.001, * P <0.05 by Bonferroni's posttest compared with baseline. Changes of circulating leptin and adiponectin levels were also assessed. Similar to what has
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Department of Biomedical Sciences, Department of Molecular Biosciences, Department of Nutrition, Department of Internal Medicine, College of Veterinary Medicine, Cornell University, T7 022A Veterinary Research Tower (Box 17), Ithaca, New York 14850, USA
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Department of Biomedical Sciences, Department of Molecular Biosciences, Department of Nutrition, Department of Internal Medicine, College of Veterinary Medicine, Cornell University, T7 022A Veterinary Research Tower (Box 17), Ithaca, New York 14850, USA
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Department of Biomedical Sciences, Department of Molecular Biosciences, Department of Nutrition, Department of Internal Medicine, College of Veterinary Medicine, Cornell University, T7 022A Veterinary Research Tower (Box 17), Ithaca, New York 14850, USA
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Department of Biomedical Sciences, Department of Molecular Biosciences, Department of Nutrition, Department of Internal Medicine, College of Veterinary Medicine, Cornell University, T7 022A Veterinary Research Tower (Box 17), Ithaca, New York 14850, USA
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circulating adiponectin concentrations ( Fig. 3 B) with corresponding increases in AMPK phosphorylation (Thr 172 ) in subcutaneous WAT and brown adipose tissue (BAT) ( Fig. 3 C). Interestingly, animals treated with alogliptin alone exhibited a significant
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Extracellular-superoxide dismutase (EC-SOD) is a secretory glycoprotein located in blood vessel walls at high levels and may be important in the antioxidant capability of vascular walls. The aim of this study was to assess plasma levels of EC-SOD and to evaluate the relationship of the EC-SOD level with insulin resistance in type 2 diabetic patients. We determined plasma EC-SOD in 122 patients and found for the first time that the EC-SOD level was strongly and positively related to adiponectin (r=0.503, P < 0.001), and significantly and inversely related to fasting plasma glucose (FPG) (r=-0.209, P=0.022), body-mass index (BMI) (r=-0.187, P=0.040) and homeostasis model assessment-insulin resistance index (HOMA-R) (r=-0.190, P=0.039). Stepwise-multiple regression analysis also showed a significant influence of adiponectin (F=33.27) on the EC-SOD level. Administration of pioglitazone to 19 diabetic patients significantly increased the plasma levels of EC-SOD (69.9+/-19.3 ng/ml to 97.4+/-25.9 ng/ml; P < 0.0001) and adiponectin, while it decreased tumor necrosis factor-alpha (TNF-alpha). The present observations suggest that factors related to the pathogenesis of insulin resistance play an important role in the regulation of the plasma EC-SOD concentration. It is possible that the increase in the EC-SOD level by pioglitazone administration in diabetic patients is due to a decline of TNF-alpha, which is known to suppress EC-SOD expression.
The authors and the journal apologise for an error that occurred in the article by Simons et al. in the February issue of the Journal of Endocrinology 191 289–299 , entitled ‘Pro-inflammatory delipidizing cytokines reduce adiponectin secretion
and/or insulin-stimulated p85α PI3K, HKII, adiponectin, and leptin expression levels.’ and not as published.
Department of Internal Medicine, Department of Oncological Endocrinology, Burnett School of Biomedical Sciences, Institute of Human Genetics, Geriatrics Research, Southern Illinois University School of Medicine, 801 North Rutledge Street, Room 4389, Springfield, Illinois 62794-9628, USA
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Department of Internal Medicine, Department of Oncological Endocrinology, Burnett School of Biomedical Sciences, Institute of Human Genetics, Geriatrics Research, Southern Illinois University School of Medicine, 801 North Rutledge Street, Room 4389, Springfield, Illinois 62794-9628, USA
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plasma adiponectin, increased plasma resistin and cholesterol, elevated levels of tumor necrosis factor α (TNFα) and interleukin-6 (IL6) in adipocytes, hyperinsulinemia and increased insulin resistance ( Bartke 2003 , Wang et al . 2007 ), as well as
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stalled attempts to target leptin for anti-obesity and anti-diabetic therapies. Adiponectin Several research groups identified adiponectin almost simultaneously as an abundantly secreted adipokine ( Scherer et al . 1995 , Hu et al . 1996 , Maeda et al
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factor α (TNFα), interleukin 6 (IL6), IL10, and adiponectin are considered to be the major inflammatory mediators found in NAFLD and insulin resistance and will thus be discussed here in more detail. Therefore, we also aim at updating and discussing
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protection against inflammation-impaired insulin secretion ( Clark 2002 ). Induction of adipokines Adiponectin is one of the adipokines most abundantly produced by adipose tissue and is a key regulator of fatty acid and glucose metabolism ( Karbowska & Kochan
