Association of 4-hydroxynonenal with classical adipokines and insulin resistance in a Chinese non-diabetic obese population

Lin Guo, Xi-Mei Zhang, Yun-Bo Zhang, Xiang Huang, Mei-Hua Chi

Resumen


Background: The prevalence of obesity is increasing worldwide. Oxidative stress plays an etiological role in a variety of obesity-related metabolic disorders. 4-hydroxynonenal (4-HNE) is the most abundant and reactive aldehydic product derived from the peroxidation of n-6 polyunsaturated fatty acids with diverse biological effects that are not well detailed. Obesity is associated with decreased plasma adiponectin concentrations and increased production of lipid peroxidation products, including 4-HNE, in adipose tissue. There may be some association between the level of adipokines and 4-HNE.

Material and methods: To analyze the associations between 4-HNE and classical adipokines, namely, adiponectin and leptin in a Chinese population, the plasma 4-HNE, adiponectin and leptin levels of 160 non-diabetic obese (NDO) patients and 160 healthy subjects were determined by ELISA, and their associations with adiposity, glucose, lipid profiles, insulin secretion and insulin sensitivity were studied.

Results: Plasma 4-HNE levels were significantly increased in patients with NDO compared with healthy controls (p < 0.01). 4-HNE was negatively correlated with adiponectin and positively correlated with leptin. The plasma levels of 4-HNE were significantly correlated to several parameters involved in body mass index (BMI) and insulin resistance (IR). The 4-HNE levels were positively correlated with BMI and negatively correlated with insulin sensitivity.

Conclusion: We conclude that 4-HNE is associated with the secretion of adiponectin and leptin and is correlated with IR in NDO humans. These findings indicate a pro-inflammatory role of 4-HNE in NDO patients, which supports the potential role of 4-HNE in the development of obesity-related disorders.


Palabras clave


Obesity. Inflammation. Adipokine. Insulin resistance. Metabolism.

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Referencias


Arita Y, Kihara S, Ouchi N, Takahashi M, Maeda K, Miyagawa J, et al. Paradoxical decrease of an adipose-specific protein, adiponectin, in obesity. Biochem Biophys Res Commun. 1999;257:79-83.

Wang Z, Dou X, Gu D, Shen C, Yao T, Nguyen V, et al. 4-Hydroxynonenal differentially regulates adiponectin gene expression and secretion via activating PPARgamma and accelerating ubiquitin-proteasome degradation. Mol Cell Endocrinol. 2012;349:222-31.

Cohen B, Novick D, Rubinstein M. Modulation of insulin activities by leptin. Science. 1996;274:1185-8.

Steppan CM, Bailey ST, Bhat S, Brown EJ, Banerjee RR, Wright CM, et al. The hormone resistin links obesity to diabetes. Nature. 2001;409:307-12.

Xu LL, Shi CM, Xu GF, Chen L, Zhu LL, Zhu L, et al. TNF-alpha, IL-6, and leptin increase the expression of miR-378, an adipogenesis-related microRNA in human adipocytes. Cell Biochem Biophys. 2014;70:771-6.

Fulop P, Seres I, Lorincz H, Harangi M, Somodi S, Paragh G. Association of chemerin with oxidative stress, inflammation and classical adipokines in non-diabetic obese patients. J Cell Mol Med. 2014;18:1313-20.

Ntaios G, Gatselis NK, Makaritsis K, Dalekos GN. Adipokines as mediators of endothelial function and atherosclerosis. Atherosclerosis. 2013;227:216-21.

Baynes JW, Thorpe SR. Role of oxidative stress in diabetic complications: a new perspective on an old paradigm. Diabetes. 1999;48:1-9.

Furukawa S, Fujita T, Shimabukuro M, Iwaki M, Yamada Y, Nakajima Y, et al. Increased oxidative stress in obesity and its impact on metabolic syndrome. J Clin Invest. 2004;114:1752-61.

Pennathur S, Heinecke JW. Mechanisms for oxidative stress in diabetic cardiovascular disease. Antioxid Redox Signal. 2007;9:955-69.

Whaley-Connell A, McCullough PA, Sowers JR. The role of oxidative stress in the metabolic syndrome. Rev Cardiovasc Med. 2011;12:21-9.

Zhang X, Wang Z, Li J, Gu D, Li S, Shen C, et al. Increased 4-hydroxynonenal formation contributes to obesity-related lipolytic activation in adipocytes. PLoS One. 2013;8:e70663.

Curtis JM, Grimsrud PA, Wright WS, Xu X, Foncea RE, Graham DW, et al. Downregulation of adipose glutathione S-transferase A4 leads to increased protein carbonylation, oxidative stress, and mitochondrial dysfunction. Diabetes. 2010;59:1132-42.

Grimsrud PA, Picklo MJ, Sr., Griffin TJ, Bernlohr DA. Carbonylation of adipose proteins in obesity and insulin resistance: identification of adipocyte fatty acid-binding protein as a cellular target of 4-hydroxynonenal. Mol Cell Proteomics. 2007;6:624-37.

Matthews DR, Hosker JP, Rudenski AS, Naylor BA, Treacher DF, Turner RC. Homeostasis model assessment: insulin resistance and beta-cell function from fasting plasma glucose and insulin concentrations in man. Diabetologia. 1985;28:412-9.

Anderson JW, Blake JE, Turner J, Smith BM. Effects of soy protein on renal function and proteinuria in patients with type 2 diabetes. Am J Clin Nutr. 1998;68:1347S-53S.

Hulsmans M, Holvoet P. The vicious circle between oxidative stress and inflammation in atherosclerosis. J Cell Mol Med. 2010;14:70-8.

Demozay D, Mas JC, Rocchi S, Van Obberghen E. FALDH reverses the deleterious action of oxidative stress induced by lipid peroxidation product 4-hydroxynonenal on insulin signaling in 3T3-L1 adipocytes. Diabetes. 2008;57:1216-26.

Samjoo IA, Safdar A, Hamadeh MJ, Raha S, Tarnopolsky MA. The effect of endurance exercise on both skeletal muscle and systemic oxidative stress in previously sedentary obese men. Nutr Diabetes. 2013;3:e88.

Soares AF, Guichardant M, Cozzone D, Bernoud-Hubac N, Bouzaidi-Tiali N, Lagarde M, et al. Effects of oxidative stress on adiponectin secretion and lactate production in 3T3-L1 adipocytes. Free Radic Biol Med. 2005;38:882-9.

Weber D, Milkovic L, Bennett SJ, Griffiths HR, Zarkovic N, Grune T. Measurement of HNE-protein adducts in human plasma and serum by ELISA-Comparison of two primary antibodies. Redox Biol. 2013;1:226-33.

Dianzani MU. 4-hydroxynonenal from pathology to physiology. Mol Aspects Med. 2003;24:263-72.

Doorn JA, Petersen DR. Covalent modification of amino acid nucleophiles by the lipid peroxidation products 4-hydroxy-2-nonenal and 4-oxo-2-nonenal. Chem Res Toxicol. 2002;15:1445-50.

Esterbauer H, Puhl H, Dieber-Rotheneder M, Waeg G, Rabl H. Effect of antioxidants on oxidative modification of LDL. Ann Med. 1991;23:573-81.

Lubrano C, Valacchi G, Specchia P, Gnessi L, Rubanenko EP, Shuginina EA, et al. Integrated Haematological Profiles of Redox Status, Lipid, and Inflammatory Protein Biomarkers in Benign Obesity and Unhealthy Obesity with Metabolic Syndrome. Oxid Med Cell Longev. 2015;2015:490613.

Liu M, Liu F. Transcriptional and post-translational regulation of adiponectin. Biochem J. 2010;425:41-52.

Wang Z, Yao T, Song Z. Involvement and mechanism of DGAT2 upregulation in the pathogenesis of alcoholic fatty liver disease. J Lipid Res. 2010;51:3158-65.

Matsubara M, Maruoka S, Katayose S. Inverse relationship between plasma adiponectin and leptin concentrations in normal-weight and obese women. Eur J Endocrinol. 2002;147:173-80.

Kwon H, Pessin JE. Adipokines mediate inflammation and insulin resistance. Front Endocrinol (Lausanne). 2013;4:71.




DOI: http://dx.doi.org/10.20960/nh.212

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