The postprandial response of adiponectin to a high-fat meal in normal and insulin-resistant subjects
- 22 May 2003
- journal article
- Published by Springer Nature in International Journal of Obesity
- Vol. 27 (6) , 657-662
- https://doi.org/10.1038/sj.ijo.0802289
Abstract
OBJECTIVE: Adiponectin is an adipose-specific protein with short-term effects in vivo on glucose and fatty acid levels. We studied the plasma concentration and the proteolytic activation status of adiponectin following the consumption of a high-fat, low-carbohydrate meal. DESIGN: Analysis of adiponectin concentration and polypeptide structure after consumption of a fat meal. SUBJECTS: Normal subjects (n=24) and first-degree relatives of patients with type II diabetes (n=20). MEASUREMENTS: All subjects had a normal fasting plasma glucose and glucose tolerance. Blood was collected for the determination of plasma insulin, adiponectin, triglyceride, and free fatty acids. Body composition was assessed with dual-energy X-ray absorptiometry and whole-body insulin sensitivity with a euglycaemic, hyperinsulinaemic clamp. Postprandial response over 6 h was determined for plasma adiponectin, glucose, insulin, triglyceride, and free fatty acids. Adiponectin was measured by commercial RIA and its polypeptide structure examined by Western blotting. RESULTS: The relatives were more insulin resistant and had increased adiposity compared with control subjects. There was no significant difference in postprandial response in fatty acids, triglyceride, or insulin between the groups. Postprandial levels of adiponectin measured by radioimmunoassay were not significantly different from fasting levels, and no breakdown products of adiponectin were detectable in postprandial samples by Western blotting. CONCLUSIONS: Levels of circulating adiponectin do not alter in response to a fat meal, despite evidence in mice that acute changes in adiponectin significantly affect postprandial fatty acid flux. Moreover, a fat meal challenge did not lead to significant activation of adiponectin by proteolytic conversion.Keywords
This publication has 15 references indexed in Scilit:
- Atherosclerotic Renal Artery StenosisJournal of the American Society of Nephrology, 2002
- ACRP30/adiponectin: an adipokine regulating glucose and lipid metabolismTrends in Endocrinology & Metabolism, 2002
- The adipose tissue—a novel endocrine organ of interest to the nephrologistNephrology Dialysis Transplantation, 2002
- PPARγ Ligands Increase Expression and Plasma Concentrations of Adiponectin, an Adipose-Derived ProteinDiabetes, 2001
- The adipocyte-secreted protein Acrp30 enhances hepatic insulin actionNature Medicine, 2001
- Hypoadiponectinemia in Obesity and Type 2 Diabetes: Close Association with Insulin Resistance and HyperinsulinemiaJournal of Clinical Endocrinology & Metabolism, 2001
- Proteolytic cleavage product of 30-kDa adipocyte complement-related protein increases fatty acid oxidation in muscle and causes weight loss in miceProceedings of the National Academy of Sciences, 2001
- Adiponectin, an Adipocyte-Derived Plasma Protein, Inhibits Endothelial NF-κB Signaling Through a cAMP-Dependent PathwayCirculation, 2000
- Plasma Concentrations of a Novel, Adipose-Specific Protein, Adiponectin, in Type 2 Diabetic PatientsArteriosclerosis, Thrombosis, and Vascular Biology, 2000
- Glucose-fatty acid interactions in health and diseaseThe American Journal of Clinical Nutrition, 1998