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Paradoxically Low Levels of Total and HMW Adiponectin in Relation to Metabolic Parameters in a Tongan Population

DOI: 10.1155/2013/873507

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Abstract:

Aim. Adiponectin has demonstrated anti-inflammatory and insulin sensitising properties, and low circulating levels may be an important risk factor for diabetes. We examined levels of adiponectin and its insulin-sensitising HMW isoform and their relationship with metabolic parameters in Tongans, a population prone to type II diabetes. Methods. Adiponectin and its HMW isoform were quantitated by Elisa in specimens from a randomly recruited, multistage cluster population survey of Tongans and from a group of Caucasians. Anthropometric, clinical, and biochemical data were collected on each subject. Results. Both male and female Tongans had lower levels of total and HMW adiponectin than their Caucasian counterparts. Levels of total and HMW adiponectin were higher in females than males in each group. Adiponectin levels were inversely related to BMI, weight, and HOMA in Tongan males and females, as well as to dyslipidemia in both sexes. Conclusion. Tongans had lower levels of both total and HMW adiponectin than Caucasians population, even after matching Tongans to their Caucasian counterparts based on BMI, age, and sex. These findings may reflect differences in body composition between the populations not adequately assessed by BMI, lifestyle factors, or a genetic variant likely in a genetically homogenous population. 1. Introduction Insulin resistance is a major risk factor for type II diabetes and commonly associated with obesity and a high fat diet. The adipose-specific glycoprotein adiponectin, one of several adipokines produced by adipose tissue, promotes insulin sensitivity, protects against atherosclerosis, and has anti-inflammatory properties [1]. Adiponectin’s HMW isomer is the most important correlate of insulin sensitivity [2], and mutant forms of adiponectin unable to form HMW species are associated with diabetes in man [3]. Adiponectin has also been shown to activate different pathways in vitro according to its oligomeric state [4], while the two receptors for adiponectin, adiponectin receptor 1 (AdipoR1) and AdipoR2, display differing functionalities [5]. In mice, simultaneous disruption of both receptors abolished adiponectin binding and resulted in increased levels of tissue triglyceride, inflammation, insulin resistance, and marked glucose intolerance [6] demonstrating the important role for adiponectin in the regulation of glucose and lipid metabolism. Levels of adiponectin are decreased in the obese, those with coronary artery disease, and in type II diabetes [1]. The Tongan population is an ideal group to examine the pathophysiology of

References

[1]  K. Hara, T. Yamauchi, and T. Kadowaki, “Adiponectin: an adipokine linking adipocytes and type 2 diabetes in humans,” Current Diabetes Reports, vol. 5, no. 2, pp. 136–140, 2005.
[2]  U. B. Pajvani, M. Hawkins, T. P. Combs et al., “Complex distribution, not absolute amount of adiponectin, correlates with thiazolidinedione-mediated improvement in insulin sensitivity,” Journal of Biological Chemistry, vol. 279, no. 13, pp. 12152–12162, 2004.
[3]  H. Waki, T. Yamauchi, J. Kamon et al., “Impaired multimerization of human adiponectin mutants associated with diabetes. Molecular structure and multimer formation of adiponectin,” Journal of Biological Chemistry, vol. 278, no. 41, pp. 40352–40363, 2003.
[4]  T.-S. Tsao, E. Tomas, H. E. Murrey et al., “Role of disulfide bonds in ACRP30/adiponectin structure and signaling specificity: different oligomers activate different signal transduction pathways,” Journal of Biological Chemistry, vol. 278, no. 50, pp. 50810–50817, 2003.
[5]  T. Yamauchi, J. Kamon, Y. Ito et al., “Cloning of adiponectin receptors that mediate antidiabetic metabolic effects,” Nature, vol. 423, no. 6941, pp. 762–769, 2003.
[6]  T. Yamauchi, Y. Nio, T. Maki et al., “Targeted disruption of AdipoR1 and AdipoR2 causes abrogation of adiponectin binding and metabolic actions,” Nature Medicine, vol. 13, no. 3, pp. 332–339, 2007.
[7]  S. Colagiuri, R. Colagiuri, S. Na'ati, S. Muimuiheata, Z. Hussain, and T. Palu, “The prevalence of diabetes in the Kingdom of Tonga,” Diabetes Care, vol. 25, no. 8, pp. 1378–1383, 2002.
[8]  P. Craig, K. Samaras, J. Freund, N. Culton, V. Halavatau, and L. Campbell, “BMI inaccurately reflects total body and abdominal fat in Tongans,” Acta Diabetologica, vol. 40, no. 1, supplement, pp. S282–S285, 2003.
[9]  B. Shand, P. Elder, R. Scott, C. Frampton, and J. Willis, “Biovariability of plasma adiponectin,” Clinical Chemistry and Laboratory Medicine, vol. 44, no. 10, pp. 1264–1268, 2006.
[10]  Y. Shen, J. A. Charlesworth, J. J. Kelly, K. W. Loi, and P. W. Peake, “Up-regulation of adiponectin, its isoforms and receptors in end-stage kidney disease,” Nephrology Dialysis Transplantation, vol. 22, no. 1, pp. 171–178, 2007.
[11]  P. W. Peake, A. D. Kriketos, L. V. Campbell, Y. Shen, and J. A. Charlesworth, “The metabolism of isoforms of human adiponectin: studies in human subjects and in experimental animals,” European Journal of Endocrinology, vol. 153, no. 3, pp. 409–417, 2005.
[12]  T. Pischon, G. S. Hotamisligil, and E. B. Rimm, “Adiponectin: stability in plasma over 36 hours and within-person variation over 1 year,” Clinical Chemistry, vol. 49, no. 4, pp. 650–652, 2003.
[13]  P. Craig, V. Halavatau, E. Comino, and I. Caterson, “Differences in body composition between Tongans and Australians: time to rethink the healthy weight ranges?” International Journal of Obesity, vol. 25, no. 12, pp. 1806–1814, 2001.
[14]  D. Fujimatsu, N. Kotooka, T. Inoue, M. Nishiyama, and K. Node, “Association between high molecular weight adiponectin levels and metabolic parameters,” Journal of Atherosclerosis and Thrombosis, vol. 16, no. 5, pp. 553–559, 2009.
[15]  J. Krakoff, T. Funahashi, C. D. A. Stehouwer et al., “Inflammatory markers, adiponectin, and risk of type 2 diabetes in the Pima Indian,” Diabetes Care, vol. 26, no. 6, pp. 1745–1751, 2003.
[16]  S. Kaser, T. Tatarczyk, A. Stadlmayr et al., “Effect of obesity and insulin sensitivity on adiponectin isoform distribution,” European Journal of Clinical Investigation, vol. 38, no. 11, pp. 827–834, 2008.
[17]  C. Lara-Castro, E. C. Doud, P. C. Tapia et al., “Adiponectin multimers and metabolic syndrome traits: relative adiponectin resistance in African Americans,” Obesity, vol. 16, no. 12, pp. 2616–2623, 2008.
[18]  M. Cnop, P. J. Havel, K. M. Utzschneider et al., “Relationship of adiponectin to body fat distribution, insulin sensitivity and plasma lipoproteins: evidence for independent roles of age and sex,” Diabetologia, vol. 46, no. 4, pp. 459–469, 2003.
[19]  N. L. Duarte, S. Colagiuri, T. Palu, X. L. Wang, and D. E. L. Wilcken, “Obesity, Type II diabetes and the β2 adrenoceptor gene Gln27Glu polymorphism in the Tongan population,” Clinical Science, vol. 104, no. 3, pp. 211–215, 2003.
[20]  S. Myles, R. A. Lea, J. Ohashi et al., “Testing the thrifty gene hypothesis: the Gly482Ser variant in PPARGC1A is associated with BMI in Tongans,” BMC Medical Genetics, vol. 12, article 10, 2011.
[21]  M. Cesari, K. Narkiewicz, R. De Toni, E. Aldighieri, C. J. Williams, and G. P. Rossi, “Heritability of plasma adiponectin levels and body mass index in twins,” Journal of Clinical Endocrinology and Metabolism, vol. 92, no. 8, pp. 3082–3088, 2007.
[22]  C. Menzaghi, V. Trischitta, and A. Doria, “Genetic influences of adiponectin on insulin resistance, type 2 diabetes, and cardiovascular disease,” Diabetes, vol. 56, no. 5, pp. 1198–1209, 2007.
[23]  C. Menzaghi, L. Salvemini, G. Paroni et al., “Circulating high molecular weight adiponectin isoform is heritable and shares a common genetic background with insulin resistance in nondiabetic White Caucasians from Italy: evidence from a family-based study,” Journal of Internal Medicine, vol. 267, no. 3, pp. 287–294, 2010.
[24]  B. Shand, P. Elder, R. Scott, N. Poa, and C. M. Frampton, “Comparison of plasma adiponectin levels in New Zealand Māori and Caucasian individuals,” New Zealand Medical Journal, vol. 120, no. 1257, 2007.
[25]  M. Evans, R. C. Sinclair, C. Fusimalohi, and V. Liava'a, “Diet, health and the nutrition transition: some impacts of economic and socio-economic factors on food consumption patterns in the Kingdom of Tonga,” Pacific Health Dialog, vol. 9, no. 2, pp. 309–315, 2002.
[26]  H. M. Mavoa and M. McCabe, “Sociocultural factors relating to Tongans' and Indigenous Fijians' patterns of eating, physical activity and body size,” Asia Pacific Journal of Clinical Nutrition, vol. 17, no. 3, pp. 375–384, 2008.
[27]  E. H. Yeung, L. J. Appel, E. R. Miller, and W. H. L. Kao, “The effects of macronutrient intake on total and high-molecular weight adiponectin: results from the OMNI-heart trial,” Obesity, vol. 18, no. 8, pp. 1632–1637, 2010.
[28]  L. K. Heilbronn, S. Gregersen, D. Shirkhedkar, D. Hu, and L. V. Campbell, “Impaired fat oxidation after a single high-fat meal in insulin-sensitive nondiabetic individuals with a family history of type 2 diabetes,” Diabetes, vol. 56, no. 8, pp. 2046–2053, 2007.
[29]  W. L. Holland, R. A. Miller, Z. V. Wang et al., “Receptor-mediated activation of ceramidase activity initiates the pleiotropic actions of adiponectin,” Nature Medicine, vol. 17, no. 1, pp. 55–63, 2011.
[30]  N. Maeda, I. Shimomura, K. Kishida et al., “Diet-induced insulin resistance in mice lacking adiponectin/ACRP30,” Nature Medicine, vol. 8, no. 7, pp. 731–737, 2002.

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