Post-translational Modifications of Adiponectin: Mechanisms and Functional Implications

作者: Yu Wang , Karen S. L. Lam , Ming-hon Yau , Aimin Xu

DOI: 10.1042/BJ20071492

关键词: BiochemistrySecretionSignal transductionGene isoformAdipokinePlasma protein bindingAdiponectinBiologyGlycosylationEndoplasmic reticulum

摘要: Adiponectin is an insulin-sensitizing adipokine with anti-diabetic, anti-atherogenic, anti-inflammatory and cardioprotective properties. This secreted from adipocytes into the circulation as three oligomeric isoforms, including trimeric, hexameric HMW (high-molecular-mass) complex consisting of at least 18 protomers. Each isoform adiponectin exerts distinct biological properties in its various target tissues. The oligomer major active form mediating effects adiponectin, whereas central actions this are attributed primarily to trimeric oligomers. In patients Type 2 diabetes coronary heart disease, circulating levels selectively decreased due impaired secretion adipocytes. biosynthesis oligomers a process involving extensive post-translational modifications. Hydroxylation glycosylation several conserved lysine residues collagenous domain necessary for intracellular assembly stabilization high-order structures. Secretion tightly controlled by pair molecular chaperones ER (endoplasmic reticulum), ERp44 (ER protein 44 kDa) Ero1-Lα oxidoreductase 1-Lα). inhibits through thiol-mediated retention. contrast, releases trapped ERp44. PPARγ (peroxisome-proliferator-activated receptor γ) agonists thiazolidinediones enhance up-regulation Ero1-Lα. present review, we discuss recent advances our understanding structural isoforms highlight role modifications regulating adiponectin.

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