The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Post-translational modifications of adiponectin: mechanisms and functional implications
Abstract
Adiponectin is an insulin-sensitizing adipokine with anti-diabetic, anti-atherogenic, anti-inflammatory and cardioprotective properties. This adipokine is secreted from adipocytes into the circulation as three oligomeric isoforms, including trimeric, hexameric and the HMW (high-molecular-mass) oligomeric complex consisting of at least 18 protomers. Each oligomeric isoform of adiponectin exerts distinct biological properties in its various target tissues. The HMW oligomer is the major active form mediating the insulin-sensitizing effects of adiponectin, whereas the central actions of this adipokine are attributed primarily to the hexameric and trimeric oligomers. In patients with Type 2 diabetes and coronary heart disease, circulating levels of HMW adiponectin are selectively decreased due to an impaired secretion of this oligomer from adipocytes. The biosynthesis of the adiponectin oligomers is a complex process involving extensive post-translational modifications. Hydroxylation and glycosylation of several conserved lysine residues in the collagenous domain of adiponectin are necessary for the intracellular assembly and stabilization of its high-order oligomeric structures. Secretion of the adiponectin oligomers is tightly controlled by a pair of molecular chaperones in the ER (endoplasmic reticulum), including ERp44 (ER protein of 44 kDa) and Ero1-Lα (ER oxidoreductase 1-Lα). ERp44 inhibits the secretion of adiponectin oligomers through a thiol-mediated retention. In contrast, Ero1-Lα releases HMW adiponectin trapped by ERp44. The PPARγ (peroxisome-proliferator-activated receptor γ) agonists thiazolidinediones selectively enhance the secretion of HMW adiponectin through up-regulation of Ero1-Lα. In the present review, we discuss the recent advances in our understanding of the structural and biological properties of the adiponectin oligomeric isoforms and highlight the role of post-translational modifications in regulating the biosynthesis of HMW adiponectin.
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Adiponectin and adiponectin receptors in insulin resistance, diabetes, and the metabolic syndrome
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The adipocyte-secreted protein Acrp30 enhances hepatic insulin action
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Self-citationPajvani, U. B., Hawkins, M., Combs, T. P., Rajala, M. W., Doebber, T., Berger, J. P., Wagner, J. A., Wu, M., Knopps, A., Xiang, A. H., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311113200 · Cited by 1,163
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Adiponectin Stimulates AMP-Activated Protein Kinase in the Hypothalamus and Increases Food Intake
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Androgens Decrease Plasma Adiponectin, an Insulin-Sensitizing Adipocyte-Derived Protein
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Cited by
Lin, Z., Tian, H., Lam, K. S. L., Lin, S., Hoo, R. C. L., Konishi, M., Itoh, N., Wang, Y., Bornstein, S. R., Xu, A., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.04.005 · Cited by 691
Self-citationAdiponectin regulation and function
Fang, H., & Judd, R. L. (2018) · Comprehensive physiology · doi:10.1002/cphy.c170046 · Cited by 631
Pettinelli, P., & Videla, L. A. (2011) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2010-2129 · Cited by 351
Yau, S. Y., Li, A., Hoo, R. L. C., Ching, Y. P., Christie, B. R., Lee, T. M. C., Xu, A., & So, K.-F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1415219111 · Cited by 326
Self-citationAdiponectin receptor signalling in the brain
Thundyil, J., Pavlovski, D., Sobey, C. G., & Arumugam, T. V. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01560.x · Cited by 280
Metadata
- Authors
- Wang, Y., Lam, K. S. L., Yau, M.-H., & Xu, A.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2008-01-15
- Volume
- 409
- Issue
- 3
- Pages
- 623-633
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W1995252260
- Cited by
- 407
- References
- 13
- FWCI
- 26.28
- Type
- journal article
- Language
- en
- Open access
- closed
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