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Review Article

糖尿病肾病的脂肪-肾轴

卷 30, 期 16, 2023

发表于: 03 October, 2022

页: [1860 - 1874] 页: 15

弟呕挨: 10.2174/0929867329666220806115518

价格: $65

摘要

长期糖尿病可导致肾损伤，称为糖尿病肾病（DN），这是晚期肾病（ESRD）的主要原因。然而，其发病机制尚未得到很好的解释。脂肪组织被认为是身体重要的能量储存装置。有趣的是，许多研究表明，脂肪组织也可以作为内分泌器官，通过分泌多种脂肪因子来维持体内平衡。在此，我们总结了迄今为止已鉴定的一些脂肪因子，更具体地说，强调它们在DN进展中的作用，并提出“脂肪-肾轴”可能是治疗DN的潜在靶点。

关键词: 糖尿病肾病（DN）、脂肪组织、脂肪因子、脂联素、肾脏、糖尿病。

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[1]
Cheung, N.; Mitchell, P.; Wong, T.Y. Diabetic retinopathy. Lancet, 2010, 376(9735), 124-136.
[http://dx.doi.org/10.1016/S0140-6736(09)62124-3] [PMID: 20580421]
[2]
Zuo, Y.; Chen, L.; Gu, H.; He, X.; Ye, Z.; Wang, Z.; Shao, Q.; Xue, C. GSDMD-mediated pyroptosis: A critical mechanism of diabetic nephropathy. Expert Rev. Mol. Med., 2021, 23, e23.
[http://dx.doi.org/10.1017/erm.2021.27] [PMID: 34955116]
[3]
Yang, M.; Li, C.; Yang, S.; Xiao, Y.; Chen, W.; Gao, P.; Jiang, N.; Xiong, S.; Wei, L.; Zhang, Q.; Yang, J.; Zeng, L.; Sun, L. Mitophagy: A novel therapeutic target for treating DN. Curr. Med. Chem., 2021, 28(14), 2717-2728.
[http://dx.doi.org/10.2174/0929867327666201006152656] [PMID: 33023427]
[4]
Jha, J.C.; Banal, C.; Chow, B.S.; Cooper, M.E.; Jandeleit-Dahm, K. Diabetes and kidney disease: Role of oxidative stress. Antioxid. Redox Signal., 2016, 25(12), 657-684.
[http://dx.doi.org/10.1089/ars.2016.6664] [PMID: 26906673]
[5]
Cui, J.; Bai, X.; Chen, X. Autophagy and diabetic nephropathy. Adv. Exp. Med. Biol., 2020, 1207, 487-494.
[http://dx.doi.org/10.1007/978-981-15-4272-5_36] [PMID: 32671771]
[6]
Tsai, Y.Z.; Tsai, M.L.; Hsu, L.Y.; Ho, C.T.; Lai, C.S. Tetrahydrocurcumin upregulates the Adiponectin-AdipoR pathway and improves insulin signaling and pancreatic beta-Cell function in high-fat diet/streptozotocin-induced diabetic obese mice. Nutrients, 2021, 13(12), 13.
[http://dx.doi.org/10.3390/nu13124552] [PMID: 34960104]
[7]
Ceja-Galicia, Z.; Calderón-DuPont, D.; Daniel, A.; Chiu, L.M.; Díaz-Villaseñor, A. Leptin and adiponectin synthesis and secretion in mature 3T3-L1 adipocytes are differentially down-regulated by arsenic and palmitic acid exposure throughout different stages of adipogenesis. Life Sci., 2022, 291, 120262.
[http://dx.doi.org/10.1016/j.lfs.2021.120262] [PMID: 34968464]
[8]
Miao, J.; He, X.; Hu, J.; Cai, W. Emodin inhibits NF-κB signaling pathway to protect obese asthmatic rats from pathological damage via Visfatin. Tissue Cell, 2022, 74, 101713.
[http://dx.doi.org/10.1016/j.tice.2021.101713] [PMID: 34952398]
[9]
Zhang, Y.; Cai, Y.; Zhang, H.; Zhang, J.; Zeng, Y.; Fan, C.; Zou, S.; Wu, C.; Fang, S.; Li, P.; Lin, X.; Wang, L.; Guan, M. Brown adipose tissue transplantation ameliorates diabetic nephropathy through the miR-30b pathway by targeting Runx1. Metabolism, 2021, 125, 154916.
[http://dx.doi.org/10.1016/j.metabol.2021.154916] [PMID: 34666067]
[10]
Cai, Y.Y.; Zhang, H.B.; Fan, C.X.; Zeng, Y.M.; Zou, S.Z.; Wu, C.Y.; Wang, L.; Fang, S.; Li, P.; Xue, Y.M.; Guan, M.P. Renoprotective effects of brown adipose tissue activation in diabetic mice. J. Diabetes, 2019, 11(12), 958-970.
[http://dx.doi.org/10.1111/1753-0407.12938] [PMID: 31020790]
[11]
Zhu, Q.; Scherer, P.E. Immunologic and endocrine functions of adipose tissue: Implications for kidney disease. Nat. Rev. Nephrol., 2018, 14(2), 105-120.
[http://dx.doi.org/10.1038/nrneph.2017.157] [PMID: 29199276]
[12]
Frigolet, M.E.; Gutiérrez-Aguilar, R. The colors of adipose tissue. Gac. Med. Mex., 2020, 156(2), 142-149.
[http://dx.doi.org/10.24875/GMM.M20000356] [PMID: 32285854]
[13]
Kershaw, E.E.; Flier, J.S. Adipose tissue as an endocrine organ. J. Clin. Endocrinol. Metab., 2004, 89(6), 2548-2556.
[http://dx.doi.org/10.1210/jc.2004-0395] [PMID: 15181022]
[14]
Chouchani, E.T.; Kajimura, S. Metabolic adaptation and maladaptation in adipose tissue. Nat. Metab., 2019, 1(2), 189-200.
[http://dx.doi.org/10.1038/s42255-018-0021-8] [PMID: 31903450]
[15]
Lehnig, A.C.; Stanford, K.I. Exercise-induced adaptations to white and brown adipose tissue. J. Exp. Biol., 2018, 221(Suppl. 1), 221.
[http://dx.doi.org/10.1242/jeb.161570] [PMID: 29514893]
[16]
Ibrahim, M.M. Subcutaneous and visceral adipose tissue: Structural and functional differences. Obes. Rev., 2010, 11(1), 11-18.
[http://dx.doi.org/10.1111/j.1467-789X.2009.00623.x] [PMID: 19656312]
[17]
Longo, M.; Zatterale, F.; Naderi, J.; Parrillo, L.; Formisano, P.; Raciti, G.A.; Beguinot, F.; Miele, C. Adipose tissue dysfunction as determinant of obesity-associated metabolic complications. Int. J. Mol. Sci., 2019, 20(9), 20.
[http://dx.doi.org/10.3390/ijms20092358] [PMID: 31085992]
[18]
Heinonen, S.; Jokinen, R.; Rissanen, A.; Pietiläinen, K.H. White adipose tissue mitochondrial metabolism in health and in obesity. Obes. Rev., 2020, 21(2), e12958.
[http://dx.doi.org/10.1111/obr.12958] [PMID: 31777187]
[19]
Martínez-Sánchez, N. There and back again: Leptin actions in white adipose tissue. Int. J. Mol. Sci., 2020, 21(17), 21.
[http://dx.doi.org/10.3390/ijms21176039] [PMID: 32839413]
[20]
Choi, H.M.; Doss, H.M.; Kim, K.S. Multifaceted physiological roles of adiponectin in inflammation and diseases. Int. J. Mol. Sci., 2020, 21(4), 21.
[http://dx.doi.org/10.3390/ijms21041219] [PMID: 32059381]
[21]
Fenzl, A.; Kiefer, F.W. Brown adipose tissue and thermogenesis. Horm. Mol. Biol. Clin. Investig., 2014, 19(1), 25-37.
[http://dx.doi.org/10.1515/hmbci-2014-0022] [PMID: 25390014]
[22]
Nedergaard, J.; Bengtsson, T.; Cannon, B. Unexpected evidence for active brown adipose tissue in adult humans. Am. J. Physiol. Endocrinol. Metab., 2007, 293(2), E444-E452.
[http://dx.doi.org/10.1152/ajpendo.00691.2006] [PMID: 17473055]
[23]
Ikeda, K.; Yamada, T. UCP1 dependent and independent thermogenesis in brown and beige adipocytes. Front. Endocrinol. (Lausanne), 2020, 11, 498.
[http://dx.doi.org/10.3389/fendo.2020.00498] [PMID: 32849287]
[24]
Enerbäck, S.; Jacobsson, A.; Simpson, E.M.; Guerra, C.; Yamashita, H.; Harper, M.E.; Kozak, L.P. Mice lacking mitochondrial uncoupling protein are cold-sensitive but not obese. Nature, 1997, 387(6628), 90-94.
[http://dx.doi.org/10.1038/387090a0] [PMID: 9139827]
[25]
Zoico, E.; Rubele, S.; De Caro, A.; Nori, N.; Mazzali, G.; Fantin, F.; Rossi, A.; Zamboni, M. Brown and beige adipose tissue and aging. Front. Endocrinol. (Lausanne), 2019, 10, 368.
[http://dx.doi.org/10.3389/fendo.2019.00368] [PMID: 31281288]
[26]
Petrovic, N.; Walden, T.B.; Shabalina, I.G.; Timmons, J.A.; Cannon, B.; Nedergaard, J. Chronic peroxisome proliferator-activated receptor gamma (PPARgamma) activation of epididymally derived white adipocyte cultures reveals a population of thermogenically competent, UCP1-containing adipocytes molecularly distinct from classic brown adipocytes. J. Biol. Chem., 2010, 285(10), 7153-7164.
[http://dx.doi.org/10.1074/jbc.M109.053942] [PMID: 20028987]
[27]
Wu, J.; Boström, P.; Sparks, L.M.; Ye, L.; Choi, J.H.; Giang, A.H.; Khandekar, M.; Virtanen, K.A.; Nuutila, P.; Schaart, G.; Huang, K.; Tu, H.; van Marken Lichtenbelt, W.D.; Hoeks, J.; Enerbäck, S.; Schrauwen, P.; Spiegelman, B.M. Beige adipocytes are a distinct type of thermogenic fat cell in mouse and human. Cell, 2012, 150(2), 366-376.
[http://dx.doi.org/10.1016/j.cell.2012.05.016] [PMID: 22796012]
[28]
Rui, L. Brown and beige adipose tissues in health and disease. Compr. Physiol., 2017, 7(4), 1281-1306.
[http://dx.doi.org/10.1002/cphy.c170001] [PMID: 28915325]
[29]
Singh, R.; Parveen, M.; Basgen, J.M.; Fazel, S.; Meshesha, M.F.; Thames, E.C.; Moore, B.; Martinez, L.; Howard, C.B.; Vergnes, L.; Reue, K.; Pervin, S. Increased expression of beige/brown adipose markers from host and breast cancer cells influence xenograft formation in mice. Mol. Cancer Res., 2016, 14(1), 78-92.
[http://dx.doi.org/10.1158/1541-7786.MCR-15-0151] [PMID: 26464213]
[30]
Azamar-Llamas, D.; Hernández-Molina, G.; Ramos-Ávalos, B.; Furuzawa-Carballeda, J. Adipokine contribution to the pathogenesis of osteoarthritis. Mediators Inflamm., 2017, 2017, 5468023.
[http://dx.doi.org/10.1155/2017/5468023] [PMID: 28490838]
[31]
Maximus, P.S.; Al Achkar, Z.; Hamid, P.F.; Hasnain, S.S.; Peralta, C.A. Adipocytokines: Are they the theory of everything? Cytokine, 2020, 133, 155144.
[http://dx.doi.org/10.1016/j.cyto.2020.155144] [PMID: 32559663]
[32]
Francisco, V.; Ruiz-Fernández, C.; Pino, J.; Mera, A.; González-Gay, M.A.; Gómez, R.; Lago, F.; Mobasheri, A.; Gualillo, O. Adipokines: Linking metabolic syndrome, the immune system, and arthritic diseases. Biochem. Pharmacol., 2019, 165, 196-206.
[http://dx.doi.org/10.1016/j.bcp.2019.03.030] [PMID: 30910694]
[33]
Abella, V.; Scotece, M.; Conde, J.; Pino, J.; Gonzalez-Gay, M.A.; Gómez-Reino, J.J.; Mera, A.; Lago, F.; Gómez, R.; Gualillo, O. Leptin in the interplay of inflammation, metabolism and immune system disorders. Nat. Rev. Rheumatol., 2017, 13(2), 100-109.
[http://dx.doi.org/10.1038/nrrheum.2016.209] [PMID: 28053336]
[34]
Briffa, J.F.; McAinch, A.J.; Poronnik, P.; Hryciw, D.H. Adipokines as a link between obesity and chronic kidney disease. Am. J. Physiol. Renal Physiol., 2013, 305(12), F1629-F1636.
[http://dx.doi.org/10.1152/ajprenal.00263.2013] [PMID: 24107418]
[35]
Fang, H.; Judd, R.L. Adiponectin regulation and function. Compr. Physiol., 2018, 8(3), 1031-1063.
[http://dx.doi.org/10.1002/cphy.c170046] [PMID: 29978896]
[36]
Achari, A.E.; Jain, S.K. Adiponectin, a therapeutic target for obesity, diabetes, and endothelial dysfunction. Int. J. Mol. Sci., 2017, 18(6), 18.
[http://dx.doi.org/10.3390/ijms18061321] [PMID: 28635626]
[37]
Tsao, T.S. Assembly of adiponectin oligomers. Rev. Endocr. Metab. Disord., 2014, 15(2), 125-136.
[http://dx.doi.org/10.1007/s11154-013-9256-6] [PMID: 23990400]
[38]
Wang, Z.V.; Scherer, P.E. Adiponectin, the past two decades. J. Mol. Cell Biol., 2016, 8(2), 93-100.
[http://dx.doi.org/10.1093/jmcb/mjw011] [PMID: 26993047]
[39]
Yamauchi, T.; Kamon, J.; Ito, Y.; Tsuchida, A.; Yokomizo, T.; Kita, S.; Sugiyama, T.; Miyagishi, M.; Hara, K.; Tsunoda, M.; Murakami, K.; Ohteki, T.; Uchida, S.; Takekawa, S.; Waki, H.; Tsuno, N.H.; Shibata, Y.; Terauchi, Y.; Froguel, P.; Tobe, K.; Koyasu, S.; Taira, K.; Kitamura, T.; Shimizu, T.; Nagai, R.; Kadowaki, T. Cloning of adiponectin receptors that mediate antidiabetic metabolic effects. Nature, 2003, 423(6941), 762-769.
[http://dx.doi.org/10.1038/nature01705] [PMID: 12802337]
[40]
Fukuda, S.; Kita, S.; Obata, Y.; Fujishima, Y.; Nagao, H.; Masuda, S.; Tanaka, Y.; Nishizawa, H.; Funahashi, T.; Takagi, J.; Maeda, N.; Shimomura, I. The unique prodomain of T-cadherin plays a key role in adiponectin binding with the essential extracellular cadherin repeats 1 and 2. J. Biol. Chem., 2017, 292(19), 7840-7849.
[http://dx.doi.org/10.1074/jbc.M117.780734] [PMID: 28325833]
[41]
Ranscht, B.; Dours-Zimmermann, M.T. T-cadherin, a novel cadherin cell adhesion molecule in the nervous system lacks the conserved cytoplasmic region. Neuron, 1991, 7(3), 391-402.
[http://dx.doi.org/10.1016/0896-6273(91)90291-7] [PMID: 1654948]
[42]
Denzel, M.S.; Scimia, M.C.; Zumstein, P.M.; Walsh, K.; Ruiz-Lozano, P.; Ranscht, B. T-cadherin is critical for adiponectin-mediated cardioprotection in mice. J. Clin. Invest., 2010, 120(12), 4342-4352.
[http://dx.doi.org/10.1172/JCI43464] [PMID: 21041950]
[43]
Matsuda, K.; Fujishima, Y.; Maeda, N.; Mori, T.; Hirata, A.; Sekimoto, R.; Tsushima, Y.; Masuda, S.; Yamaoka, M.; Inoue, K.; Nishizawa, H.; Kita, S.; Ranscht, B.; Funahashi, T.; Shimomura, I. Positive feedback regulation between adiponectin and T-cadherin impacts adiponectin levels in tissue and plasma of male mice. Endocrinology, 2015, 156(3), 934-946.
[http://dx.doi.org/10.1210/en.2014-1618] [PMID: 25514086]
[44]
Zha, D.; Wu, X.; Gao, P. Adiponectin and its receptors in diabetic kidney disease: Molecular mechanisms and clinical potential. Endocrinology, 2017, 158(7), 2022-2034.
[http://dx.doi.org/10.1210/en.2016-1765] [PMID: 28402446]
[45]
Cammisotto, P.G.; Londono, I.; Gingras, D.; Bendayan, M. Control of glycogen synthase through ADIPOR1-AMPK pathway in renal distal tubules of normal and diabetic rats. Am. J. Physiol. Renal Physiol., 2008, 294(4), F881-F889.
[http://dx.doi.org/10.1152/ajprenal.00373.2007] [PMID: 18256313]
[46]
Gavrila, A.; Peng, C.K.; Chan, J.L.; Mietus, J.E.; Goldberger, A.L.; Mantzoros, C.S. Diurnal and ultradian dynamics of serum adiponectin in healthy men: Comparison with leptin, circulating soluble leptin receptor, and cortisol patterns. J. Clin. Endocrinol. Metab., 2003, 88(6), 2838-2843.
[http://dx.doi.org/10.1210/jc.2002-021721] [PMID: 12788897]
[47]
Halleux, C.M.; Takahashi, M.; Delporte, M.L.; Detry, R.; Funahashi, T.; Matsuzawa, Y.; Brichard, S.M. Secretion of adiponectin and regulation of apM1 gene expression in human visceral adipose tissue. Biochem. Biophys. Res. Commun., 2001, 288(5), 1102-1107.
[http://dx.doi.org/10.1006/bbrc.2001.5904] [PMID: 11700024]
[48]
Seo, J.B.; Moon, H.M.; Noh, M.J.; Lee, Y.S.; Jeong, H.W.; Yoo, E.J.; Kim, W.S.; Park, J.; Youn, B.S.; Kim, J.W.; Park, S.D.; Kim, J.B. Adipocyte determination- and differentiation-dependent factor 1/sterol regulatory element-binding protein 1c regulates mouse adiponectin expression. J. Biol. Chem., 2004, 279(21), 22108-22117.
[http://dx.doi.org/10.1074/jbc.M400238200] [PMID: 15037635]
[49]
Mao, X.; Kikani, C.K.; Riojas, R.A.; Langlais, P.; Wang, L.; Ramos, F.J.; Fang, Q.; Christ-Roberts, C.Y.; Hong, J.Y.; Kim, R.Y.; Liu, F.; Dong, L.Q. APPL1 binds to adiponectin receptors and mediates adiponectin signalling and function. Nat. Cell Biol., 2006, 8(5), 516-523.
[http://dx.doi.org/10.1038/ncb1404] [PMID: 16622416]
[50]
Deepa, S.S.; Dong, L.Q. APPL1: Role in adiponectin signaling and beyond. Am. J. Physiol. Endocrinol. Metab., 2009, 296(1), E22-E36.
[http://dx.doi.org/10.1152/ajpendo.90731.2008] [PMID: 18854421]
[51]
Li, P.; Zhang, S.; Song, H.; Traore, S.S.; Li, J.; Raubenheimer, D.; Cui, Z.; Kou, G. Naringin promotes skeletal muscle fiber remodeling by the AdipoR1-APPL1-AMPK signaling pathway. J. Agric. Food Chem., 2021, 69(40), 11890-11899.
[http://dx.doi.org/10.1021/acs.jafc.1c04481] [PMID: 34586803]
[52]
Ryu, J.; Galan, A.K.; Xin, X.; Dong, F.; Abdul-Ghani, M.A.; Zhou, L.; Wang, C.; Li, C.; Holmes, B.M.; Sloane, L.B.; Austad, S.N.; Guo, S.; Musi, N.; DeFronzo, R.A.; Deng, C.; White, M.F.; Liu, F.; Dong, L.Q. APPL1 potentiates insulin sensitivity by facilitating the binding of IRS1/2 to the insulin receptor. Cell Rep., 2014, 7(4), 1227-1238.
[http://dx.doi.org/10.1016/j.celrep.2014.04.006] [PMID: 24813896]
[53]
Sayeed, M.; Gautam, S.; Verma, D.P.; Afshan, T.; Kumari, T.; Srivastava, A.K.; Ghosh, J.K. A collagen domain-derived short adiponectin peptide activates APPL1 and AMPK signaling pathways and improves glucose and fatty acid metabolisms. J. Biol. Chem., 2018, 293(35), 13509-13523.
[http://dx.doi.org/10.1074/jbc.RA118.001801] [PMID: 29991592]
[54]
Prudente, S.; Jungtrakoon, P.; Marucci, A.; Ludovico, O.; Buranasupkajorn, P.; Mazza, T.; Hastings, T.; Milano, T.; Morini, E.; Mercuri, L.; Bailetti, D.; Mendonca, C.; Alberico, F.; Basile, G.; Romani, M.; Miccinilli, E.; Pizzuti, A.; Carella, M.; Barbetti, F.; Pascarella, S.; Marchetti, P.; Trischitta, V.; Di Paola, R.; Doria, A. Loss-of-Function mutations in APPL1 in familial diabetes mellitus. Am. J. Hum. Genet., 2015, 97(1), 177-185.
[http://dx.doi.org/10.1016/j.ajhg.2015.05.011] [PMID: 26073777]
[55]
Fan, L.; Ye, H.; Wan, Y.; Qin, L.; Zhu, L.; Su, J.; Zhu, X.; Zhang, L.; Miao, Q.; Zhang, Q.; Zhang, Z.; Xu, A.; Li, Y.; Li, X.; Wang, Y. Adaptor protein APPL1 coordinates HDAC3 to modulate brown adipose tissue thermogenesis in mice. Metabolism, 2019, 100, 153955.
[http://dx.doi.org/10.1016/j.metabol.2019.153955] [PMID: 31390528]
[56]
Miaczynska, M.; Christoforidis, S.; Giner, A.; Shevchenko, A.; Uttenweiler-Joseph, S.; Habermann, B.; Wilm, M.; Parton, R.G.; Zerial, M. APPL proteins link Rab5 to nuclear signal transduction via an endosomal compartment. Cell, 2004, 116(3), 445-456.
[http://dx.doi.org/10.1016/S0092-8674(04)00117-5] [PMID: 15016378]
[57]
Zhu, G.; Chen, J.; Liu, J.; Brunzelle, J.S.; Huang, B.; Wakeham, N.; Terzyan, S.; Li, X.; Rao, Z.; Li, G.; Zhang, X.C. Structure of the APPL1 BAR-PH domain and characterization of its interaction with Rab5. EMBO J., 2007, 26(14), 3484-3493.
[http://dx.doi.org/10.1038/sj.emboj.7601771] [PMID: 17581628]
[58]
Wang, C.; Xin, X.; Xiang, R.; Ramos, F.J.; Liu, M.; Lee, H.J.; Chen, H.; Mao, X.; Kikani, C.K.; Liu, F.; Dong, L.Q. Yin-Yang regulation of adiponectin signaling by APPL isoforms in muscle cells. J. Biol. Chem., 2009, 284(46), 31608-31615.
[http://dx.doi.org/10.1074/jbc.M109.010355] [PMID: 19661063]
[59]
Jiang, S.; Fang, Q.; Yu, W.; Zhang, R.; Hu, C.; Dong, K.; Bao, Y.; Wang, C.; Xiang, K.; Jia, W. Genetic variations in APPL2 are associated with overweight and obesity in a Chinese population with normal glucose tolerance. BMC Med. Genet., 2012, 13(1), 22.
[http://dx.doi.org/10.1186/1471-2350-13-22] [PMID: 22462604]
[60]
Cheng, K.K.; Zhu, W.; Chen, B.; Wang, Y.; Wu, D.; Sweeney, G.; Wang, B.; Lam, K.S.; Xu, A. The adaptor protein APPL2 inhibits insulin-stimulated glucose uptake by interacting with TBC1D1 in skeletal muscle. Diabetes, 2014, 63(11), 3748-3758.
[http://dx.doi.org/10.2337/db14-0337] [PMID: 24879834]
[61]
El-Shal, A.S.; Zidan, H.E.; Rashad, N.M. Adiponectin gene polymorphisms in Egyptian type 2 diabetes mellitus patients with and without diabetic nephropathy. Mol. Biol. Rep., 2014, 41(4), 2287-2298.
[http://dx.doi.org/10.1007/s11033-014-3082-0] [PMID: 24469713]
[62]
Martinez Cantarin, M.P.; Waldman, S.A.; Doria, C.; Frank, A.M.; Maley, W.R.; Ramirez, C.B.; Keith, S.W.; Falkner, B. The adipose tissue production of adiponectin is increased in end-stage renal disease. Kidney Int., 2013, 83(3), 487-494.
[http://dx.doi.org/10.1038/ki.2012.421] [PMID: 23283133]
[63]
Zoccali, C.; Mallamaci, F.; Tripepi, G.; Benedetto, F.A.; Cutrupi, S.; Parlongo, S.; Malatino, L.S.; Bonanno, G.; Seminara, G.; Rapisarda, F.; Fatuzzo, P.; Buemi, M.; Nicocia, G.; Tanaka, S.; Ouchi, N.; Kihara, S.; Funahashi, T.; Matsuzawa, Y. Adiponectin, metabolic risk factors, and cardiovascular events among patients with end-stage renal disease. J. Am. Soc. Nephrol., 2002, 13(1), 134-141.
[http://dx.doi.org/10.1681/ASN.V131134] [PMID: 11752030]
[64]
Martinez Cantarin, M.P.; Keith, S.W.; Waldman, S.A.; Falkner, B. Adiponectin receptor and adiponectin signaling in human tissue among patients with end-stage renal disease. Nephrol. Dial. Transplant., 2014, 29(12), 2268-2277.
[http://dx.doi.org/10.1093/ndt/gfu249] [PMID: 25049200]
[65]
Cha, J.J.; Min, H.S.; Kim, K.; Lee, M.J.; Lee, M.H.; Kim, J.E.; Song, H.K.; Cha, D.R.; Kang, Y.S. Long-term study of the association of adipokines and glucose variability with diabetic complications. Korean J. Intern. Med. (Korean. Assoc. Intern. Med.), 2018, 33(2), 367-382.
[http://dx.doi.org/10.3904/kjim.2016.114] [PMID: 27809453]
[66]
Jorsal, A.; Tarnow, L.; Frystyk, J.; Lajer, M.; Flyvbjerg, A.; Parving, H.H.; Vionnet, N.; Rossing, P. Serum adiponectin predicts all-cause mortality and end stage renal disease in patients with type I diabetes and diabetic nephropathy. Kidney Int., 2008, 74(5), 649-654.
[http://dx.doi.org/10.1038/ki.2008.201] [PMID: 18496510]
[67]
Sharma, K.; Ramachandrarao, S.; Qiu, G.; Usui, H.K.; Zhu, Y.; Dunn, S.R.; Ouedraogo, R.; Hough, K.; McCue, P.; Chan, L.; Falkner, B.; Goldstein, B.J. Adiponectin regulates albuminuria and podocyte function in mice. J. Clin. Invest., 2008, 118(5), 1645-1656.
[http://dx.doi.org/10.1172/JCI32691] [PMID: 18431508]
[68]
Han, Y.; Xiong, S.; Zhao, H.; Yang, S.; Yang, M.; Zhu, X.; Jiang, N.; Xiong, X.; Gao, P.; Wei, L.; Xiao, Y.; Sun, L. Lipophagy deficiency exacerbates ectopic lipid accumulation and tubular cells injury in diabetic nephropathy. Cell Death Dis., 2021, 12(11), 1031.
[http://dx.doi.org/10.1038/s41419-021-04326-y] [PMID: 34718329]
[69]
Kim, Y.; Lim, J.H.; Kim, M.Y.; Kim, E.N.; Yoon, H.E.; Shin, S.J.; Choi, B.S.; Kim, Y.S.; Chang, Y.S.; Park, C.W. The adiponectin receptor agonist AdipoRon ameliorates diabetic nephropathy in a model of type 2 diabetes. J. Am. Soc. Nephrol., 2018, 29(4), 1108-1127.
[http://dx.doi.org/10.1681/ASN.2017060627] [PMID: 29330340]
[70]
Sugiyama, S.; Fukushima, H.; Kugiyama, K.; Maruyoshi, H.; Kojima, S.; Funahashi, T.; Sakamoto, T.; Horibata, Y.; Watanabe, K.; Koga, H.; Sugamura, K.; Otsuka, F.; Shimomura, I.; Ogawa, H. Pravastatin improved glucose metabolism associated with increasing plasma adiponectin in patients with impaired glucose tolerance and coronary artery disease. Atherosclerosis, 2007, 194(2), e43-e51.
[http://dx.doi.org/10.1016/j.atherosclerosis.2006.08.023] [PMID: 17112529]
[71]
Hasan, A.U.; Ohmori, K.; Hashimoto, T.; Kamitori, K.; Yamaguchi, F.; Ishihara, Y.; Ishihara, N.; Noma, T.; Tokuda, M.; Kohno, M. Valsartan ameliorates the constitutive adipokine expression pattern in mature adipocytes: A role for inverse agonism of the angiotensin II type 1 receptor in obesity. Hypertens. Res., 2014, 37(7), 621-628.
[http://dx.doi.org/10.1038/hr.2014.51] [PMID: 24599011]
[72]
Miyazaki, Y.; Cersosimo, E.; Triplitt, C.; DeFronzo, R.A. Rosiglitazone decreases albuminuria in type 2 diabetic patients. Kidney Int., 2007, 72(11), 1367-1373.
[http://dx.doi.org/10.1038/sj.ki.5002516] [PMID: 17805239]
[73]
Kennedy, G.C. The role of depot fat in the hypothalamic control of food intake in the rat. Proc. R. Soc. Lond., B, 1953, 140(901), 578-596.
[http://dx.doi.org/10.1098/rspb.1953.0009] [PMID: 13027283]
[74]
Coleman, D.L. Effects of parabiosis of obese with diabetes and normal mice. Diabetologia, 1973, 9(4), 294-298.
[http://dx.doi.org/10.1007/BF01221857] [PMID: 4767369]
[75]
Zhang, Y.; Proenca, R.; Maffei, M.; Barone, M.; Leopold, L.; Friedman, J.M. Positional cloning of the mouse obese gene and its human homologue. Nature, 1994, 372(6505), 425-432.
[http://dx.doi.org/10.1038/372425a0] [PMID: 7984236]
[76]
Münzberg, H.; Morrison, C.D. Structure, production and signaling of leptin. Metabolism, 2015, 64(1), 13-23.
[http://dx.doi.org/10.1016/j.metabol.2014.09.010] [PMID: 25305050]
[77]
Akther, A.; Khan, K.H.; Begum, M.; Parveen, S.; Kaiser, M.S.; Chowdhury, A.Z. Leptin: A mysterious hormone; its physiology and pathophysiology. Mymensingh Med. J., 2009, 18(1), S140-S144.
[PMID: 19436260]
[78]
Bado, A.; Levasseur, S.; Attoub, S.; Kermorgant, S.; Laigneau, J.P.; Bortoluzzi, M.N.; Moizo, L.; Lehy, T.; Guerre-Millo, M.; Le Marchand-Brustel, Y.; Lewin, M.J. The stomach is a source of leptin. Nature, 1998, 394(6695), 790-793.
[http://dx.doi.org/10.1038/29547] [PMID: 9723619]
[79]
Vernooy, J.H.; Drummen, N.E.; van Suylen, R.J.; Cloots, R.H.; Möller, G.M.; Bracke, K.R.; Zuyderduyn, S.; Dentener, M.A.; Brusselle, G.G.; Hiemstra, P.S.; Wouters, E.F. Enhanced pulmonary leptin expression in patients with severe COPD and asymptomatic smokers. Thorax, 2009, 64(1), 26-32.
[http://dx.doi.org/10.1136/thx.2007.085423] [PMID: 18835960]
[80]
Hoggard, N.; Hunter, L.; Duncan, J.S.; Williams, L.M.; Trayhurn, P.; Mercer, J.G. Leptin and leptin receptor mRNA and protein expression in the murine fetus and placenta. Proc. Natl. Acad. Sci. USA, 1997, 94(20), 11073-11078.
[http://dx.doi.org/10.1073/pnas.94.20.11073] [PMID: 9380761]
[81]
Wiesner, G.; Vaz, M.; Collier, G.; Seals, D.; Kaye, D.; Jennings, G.; Lambert, G.; Wilkinson, D.; Esler, M. Leptin is released from the human brain: Influence of adiposity and gender. J. Clin. Endocrinol. Metab., 1999, 84(7), 2270-2274.
[http://dx.doi.org/10.1210/jc.84.7.2270] [PMID: 10404789]
[82]
Friedman, J.M.; Halaas, J.L. Leptin and the regulation of body weight in mammals. Nature, 1998, 395(6704), 763-770.
[http://dx.doi.org/10.1038/27376] [PMID: 9796811]
[83]
Schwartz, M.W.; Woods, S.C.; Porte, D., Jr.; Seeley, R.J.; Baskin, D.G. Central nervous system control of food intake. Nature, 2000, 404(6778), 661-671.
[http://dx.doi.org/10.1038/35007534] [PMID: 10766253]
[84]
Ahima, R.S.; Prabakaran, D.; Mantzoros, C.; Qu, D.; Lowell, B.; Maratos-Flier, E.; Flier, J.S. Role of leptin in the neuroendocrine response to fasting. Nature, 1996, 382(6588), 250-252.
[http://dx.doi.org/10.1038/382250a0] [PMID: 8717038]
[85]
Zhang, Y.; Chua, S., Jr. Leptin function and regulation. Compr. Physiol., 2017, 8(1), 351-369.
[http://dx.doi.org/10.1002/cphy.c160041] [PMID: 29357132]
[86]
Pereira, S.; Cline, D.L.; Glavas, M.M.; Covey, S.D.; Kieffer, T.J. Tissue-specific effects of leptin on glucose and lipid metabolism. Endocr. Rev., 2021, 42(1), 1-28.
[http://dx.doi.org/10.1210/endrev/bnaa027] [PMID: 33150398]
[87]
La Cava, A. Leptin in inflammation and autoimmunity. Cytokine, 2017, 98, 51-58.
[http://dx.doi.org/10.1016/j.cyto.2016.10.011] [PMID: 27916613]
[88]
Poetsch, M.S.; Strano, A.; Guan, K. Role of leptin in cardiovascular diseases. Front. Endocrinol. (Lausanne), 2020, 11, 354.
[http://dx.doi.org/10.3389/fendo.2020.00354] [PMID: 32655492]
[89]
Greco, M.; De Santo, M.; Comandè, A.; Belsito, E.L.; Andò, S.; Liguori, A.; Leggio, A. Leptin-Activity modulators and their potential pharmaceutical applications. Biomolecules, 2021, 11(7), 11.
[http://dx.doi.org/10.3390/biom11071045] [PMID: 34356668]
[90]
Wauman, J.; Zabeau, L.; Tavernier, J. The leptin receptor complex: Heavier than expected? Front. Endocrinol. (Lausanne), 2017, 8, 30.
[http://dx.doi.org/10.3389/fendo.2017.00030] [PMID: 28270795]
[91]
Myers, M.G.; Cowley, M.A.; Münzberg, H. Mechanisms of leptin action and leptin resistance. Annu. Rev. Physiol., 2008, 70(1), 537-556.
[http://dx.doi.org/10.1146/annurev.physiol.70.113006.100707] [PMID: 17937601]
[92]
Yassin, M.M.; AbuMustafa, A.M.; Yassin, M.M. Serum leptin in diabetic nephropathy male patients from Gaza Strip. Diabetes Metab. Syndr., 2019, 13(2), 1245-1250.
[http://dx.doi.org/10.1016/j.dsx.2019.02.004] [PMID: 31336472]
[93]
Huang, J.; Peng, X.; Dong, K.; Tao, J.; Yang, Y. The association between insulin resistance, leptin, and resistin and diabetic nephropathy in type 2 diabetes mellitus patients with different body mass indexes. Diabetes Metab. Syndr. Obes., 2021, 14, 2357-2365.
[http://dx.doi.org/10.2147/DMSO.S305054] [PMID: 34079314]
[94]
Chung, F.M.; Tsai, J.C.; Chang, D.M.; Shin, S.J.; Lee, Y.J. Peripheral total and differential leukocyte count in diabetic nephropathy: The relationship of plasma leptin to leukocytosis. Diabetes Care, 2005, 28(7), 1710-1717.
[http://dx.doi.org/10.2337/diacare.28.7.1710] [PMID: 15983324]
[95]
Hanai, K.; Babazono, T.; Mugishima, M.; Yoshida, N.; Nyumura, I.; Toya, K.; Bouchi, R.; Tanaka, N.; Uchigata, Y. Association of serum leptin levels with progression of diabetic kidney disease in patients with type 2 diabetes. Diabetes Care, 2011, 34(12), 2557-2559.
[http://dx.doi.org/10.2337/dc11-1039] [PMID: 21994433]
[96]
Sharma, K.; McCue, P.; Dunn, S.R. Diabetic kidney disease in the db/db mouse. Am. J. Physiol. Renal Physiol., 2003, 284(6), F1138-F1144.
[http://dx.doi.org/10.1152/ajprenal.00315.2002] [PMID: 12736165]
[97]
Tesch, G.H.; Lim, A.K. Recent insights into diabetic renal injury from the db/db mouse model of type 2 diabetic nephropathy. Am. J. Physiol. Renal Physiol., 2011, 300(2), F301-F310.
[http://dx.doi.org/10.1152/ajprenal.00607.2010] [PMID: 21147843]
[98]
Suganami, T.; Mukoyama, M.; Mori, K.; Yokoi, H.; Koshikawa, M.; Sawai, K.; Hidaka, S.; Ebihara, K.; Tanaka, T.; Sugawara, A.; Kawachi, H.; Vinson, C.; Ogawa, Y.; Nakao, K. Prevention and reversal of renal injury by leptin in a new mouse model of diabetic nephropathy. FASEB J., 2005, 19(1), 127-129.
[http://dx.doi.org/10.1096/fj.04-2183fje] [PMID: 15496495]
[99]
Wolf, G.; Hamann, A.; Han, D.C.; Helmchen, U.; Thaiss, F.; Ziyadeh, F.N.; Stahl, R.A. Leptin stimulates proliferation and TGF-beta expression in renal glomerular endothelial cells: Potential role in glomerulosclerosis [seecomments]. Kidney Int., 1999, 56(3), 860-872.
[http://dx.doi.org/10.1046/j.1523-1755.1999.00626.x] [PMID: 10469355]
[100]
Samal, B.; Sun, Y.; Stearns, G.; Xie, C.; Suggs, S.; Mc- Niece, I. Cloning and characterization of the cDNA encoding a novel human pre-B-cell colony-enhancing factor. Mol. Cell. Biol., 1994, 14(2), 1431-1437.
[PMID: 8289818]
[101]
Martin, P.R.; Shea, R.J.; Mulks, M.H. Identification of a plasmid-encoded gene from Haemophilus ducreyi which confers NAD independence. J. Bacteriol., 2001, 183(4), 1168-1174.
[http://dx.doi.org/10.1128/JB.183.4.1168-1174.2001] [PMID: 11157928]
[102]
Rongvaux, A.; Shea, R.J.; Mulks, M.H.; Gigot, D.; Urbain, J.; Leo, O.; Andris, F. Pre-B-cell colony-enhancing factor, whose expression is up-regulated in activated lymphocytes, is a nicotinamide phosphoribosyltransferase, a cytosolic enzyme involved in NAD biosynthesis. Eur. J. Immunol., 2002, 32(11), 3225-3234.
[http://dx.doi.org/10.1002/1521-4141(200211)32:11<3225::AID-IMMU3225>3.0.CO;2-L] [PMID: 12555668]
[103]
Radzicka, S.; Pietryga, M.; Iciek, R.; Brązert, J. The role of visfatin in pathogenesis of gestational diabetes (GDM). Ginekol. Pol., 2018, 89(9), 518-521.
[http://dx.doi.org/10.5603/GP.a2018.0088] [PMID: 30318580]
[104]
Ognjanovic, S.; Bao, S.; Yamamoto, S.Y.; Garibay-Tupas, J.; Samal, B.; Bryant-Greenwood, G.D. Genomic organization of the gene coding for human pre-B-cell colony enhancing factor and expression in human fetal membranes. J. Mol. Endocrinol., 2001, 26(2), 107-117.
[http://dx.doi.org/10.1677/jme.0.0260107] [PMID: 11241162]
[105]
Revollo, J.R.; Körner, A.; Mills, K.F.; Satoh, A.; Wang, T.; Garten, A.; Dasgupta, B.; Sasaki, Y.; Wolberger, C.; Townsend, R.R.; Milbrandt, J.; Kiess, W.; Imai, S. Nampt/PBEF/Visfatin regulates insulin secretion in beta cells as a systemic NAD biosynthetic enzyme. Cell Metab., 2007, 6(5), 363-375.
[http://dx.doi.org/10.1016/j.cmet.2007.09.003] [PMID: 17983582]
[106]
Yoon, M.J.; Yoshida, M.; Johnson, S.; Takikawa, A.; Usui, I.; Tobe, K.; Nakagawa, T.; Yoshino, J.; Imai, S. SIRT1-Mediated eNAMPT secretion from adipose tissue regulates hypothalamic NAD+ and function in mice. Cell Metab., 2015, 21(5), 706-717.
[http://dx.doi.org/10.1016/j.cmet.2015.04.002] [PMID: 25921090]
[107]
Dakroub, A. Visfatin: A possible role in cardiovasculo-metabolic disorders. Cells-Basel, 2020, 9(11), 2444.
[108]
Mageswari, R.; Sridhar, M.G.; Nandeesha, H.; Parameshwaran, S.; Vinod, K.V. Irisin and visfatin predicts severity of diabetic nephropathy. Indian J. Clin. Biochem., 2019, 34(3), 342-346.
[http://dx.doi.org/10.1007/s12291-018-0749-7] [PMID: 31391726]
[109]
Akbarian, N.; Zarghami, N.; Mota, A.; Abediazar, S.; Abroon, S.; Mihanfar, A.; Amanzadeh, M.; Darbin, A.; Bannazadeh Baghi, H.; Rahmati-Yamchi, M. Correlation between circulating visfatin and nitric oxide metabolites levels in patients with diabetic nephropathy. Iran. J. Kidney Dis., 2018, 12(3), 163-168.
[PMID: 29891746]
[110]
Eyileten, T.; Sonmez, A.; Saglam, M.; Cakir, E.; Caglar, K.; Oguz, Y.; Vural, A.; Yenicesu, M.; Yilmaz, M.I. Effect of renin-angiotensin-aldosterone system (RAAS) blockade on visfatin levels in diabetic nephropathy. Nephrology (Carlton), 2010, 15(2), 225-229.
[http://dx.doi.org/10.1111/j.1440-1797.2009.01173.x] [PMID: 20470283]
[111]
El Samahi, M.H.; Ismail, N.A.; Matter, R.M.; Selim, A.; Ibrahim, A.A.; Nabih, W. Study of visfatin level in type 1 diabetic children and adolescents. Open Access Maced. J. Med. Sci., 2017, 5(3), 299-304.
[http://dx.doi.org/10.3889/oamjms.2017.065] [PMID: 28698746]
[112]
Song, H.K.; Lee, M.H.; Kim, B.K.; Park, Y.G.; Ko, G.J.; Kang, Y.S.; Han, J.Y.; Han, S.Y.; Han, K.H.; Kim, H.K.; Cha, D.R. Visfatin: A new player in mesangial cell physiology and diabetic nephropathy. Am. J. Physiol. Renal Physiol., 2008, 295(5), F1485-F1494.
[http://dx.doi.org/10.1152/ajprenal.90231.2008] [PMID: 18768589]
[113]
Kang, Y.S.; Song, H.K.; Lee, M.H.; Ko, G.J.; Han, J.Y.; Han, S.Y.; Han, K.H.; Kim, H.K.; Cha, D.R. Visfatin is upregulated in type-2 diabetic rats and targets renal cells. Kidney Int., 2010, 78(2), 170-181.
[http://dx.doi.org/10.1038/ki.2010.98] [PMID: 20375985]
[114]
Muraoka, H.; Hasegawa, K.; Sakamaki, Y.; Minakuchi, H.; Kawaguchi, T.; Yasuda, I.; Kanda, T.; Tokuyama, H.; Wakino, S.; Itoh, H. Role of Nampt-Sirt6 axis in renal proximal tubules in extracellular matrix deposition in diabetic nephropathy. Cell Rep., 2019, 27(1), 199-212.e5.
[http://dx.doi.org/10.1016/j.celrep.2019.03.024] [PMID: 30943401]
[115]
Kacso, A.C.; Bondor, C.I.; Coman, A.L.; Potra, A.R.; Georgescu, C.E. Determinants of visfatin in type 2 diabetes patients with diabetic kidney disease: Relationship to inflammation, adiposity and undercarboxylated osteocalcin. Scand. J. Clin. Lab. Invest., 2016, 76(3), 217-225.
[http://dx.doi.org/10.3109/00365513.2015.1137349] [PMID: 26922969]
[116]
Steppan, C.M.; Brown, E.J.; Wright, C.M.; Bhat, S.; Banerjee, R.R.; Dai, C.Y.; Enders, G.H.; Silberg, D.G.; Wen, X.; Wu, G.D.; Lazar, M.A. A family of tissue-specific resistin-like molecules. Proc. Natl. Acad. Sci. USA, 2001, 98(2), 502-506.
[http://dx.doi.org/10.1073/pnas.98.2.502] [PMID: 11209052]
[117]
Steppan, C.M.; Bailey, S.T.; Bhat, S.; Brown, E.J.; Banerjee, R.R.; Wright, C.M.; Patel, H.R.; Ahima, R.S.; Lazar, M.A. The hormone resistin links obesity to diabetes. Nature, 2001, 409(6818), 307-312.
[http://dx.doi.org/10.1038/35053000] [PMID: 11201732]
[118]
Lazar, M.A. Resistin- and Obesity-associated metabolic diseases. Horm. Metab. Res., 2007, 39(10), 710-716.
[http://dx.doi.org/10.1055/s-2007-985897] [PMID: 17952831]
[119]
Filková, M.; Haluzík, M.; Gay, S.; Senolt, L. The role of resistin as a regulator of inflammation: Implications for various human pathologies. Clin. Immunol., 2009, 133(2), 157-170.
[http://dx.doi.org/10.1016/j.clim.2009.07.013] [PMID: 19740705]
[120]
Lehrke, M.; Reilly, M.P.; Millington, S.C.; Iqbal, N.; Rader, D.J.; Lazar, M.A. An inflammatory cascade leading to hyperresistinemia in humans. PLoS Med., 2004, 1(2), e45.
[http://dx.doi.org/10.1371/journal.pmed.0010045] [PMID: 15578112]
[121]
Acquarone, E.; Monacelli, F.; Borghi, R.; Nencioni, A.; Odetti, P. Resistin: A reappraisal. Mech. Ageing Dev., 2019, 178, 46-63.
[http://dx.doi.org/10.1016/j.mad.2019.01.004] [PMID: 30650338]
[122]
Yang, R.Z.; Huang, Q.; Xu, A.; McLenithan, J.C.; Eisen, J.A.; Shuldiner, A.R.; Alkan, S.; Gong, D.W. Comparative studies of resistin expression and phylogenomics in human and mouse. Biochem. Biophys. Res. Commun., 2003, 310(3), 927-935.
[http://dx.doi.org/10.1016/j.bbrc.2003.09.093] [PMID: 14550293]
[123]
Codoñer-Franch, P.; Alonso-Iglesias, E. Resistin: Insulin resistance to malignancy. Clin. Chim. Acta, 2015, 438, 46-54.
[http://dx.doi.org/10.1016/j.cca.2014.07.043] [PMID: 25128719]
[124]
Sudan, S.K.; Deshmukh, S.K.; Poosarla, T.; Holliday, N.P.; Dyess, D.L.; Singh, A.P.; Singh, S. Resistin: An inflammatory cytokine with multi-faceted roles in cancer. Biochim. Biophys. Acta Rev. Cancer, 2020, 1874(2), 188419.
[http://dx.doi.org/10.1016/j.bbcan.2020.188419] [PMID: 32822824]
[125]
Benomar, Y.; Gertler, A.; De Lacy, P.; Crépin, D.; Ould Hamouda, H.; Riffault, L.; Taouis, M. Central resistin overexposure induces insulin resistance through toll-like receptor 4. Diabetes, 2013, 62(1), 102-114.
[http://dx.doi.org/10.2337/db12-0237] [PMID: 22961082]
[126]
Wang, C.H.; Wang, P.J.; Hsieh, Y.C.; Lo, S.; Lee, Y.C.; Chen, Y.C.; Tsai, C.H.; Chiu, W.C.; Chu-Sung Hu, S.; Lu, C.W.; Yang, Y.F.; Chiu, C.C.; Ou-Yang, F.; Wang, Y.M.; Hou, M.F.; Yuan, S.S. Resistin facilitates breast cancer progression via TLR4-mediated induction of mesenchymal phenotypes and stemness properties. Oncogene, 2018, 37(5), 589-600.
[http://dx.doi.org/10.1038/onc.2017.357] [PMID: 28991224]
[127]
Hayder, Z.S.; Kareem, Z.S. Resistin hormone in diabetic kidney disease and its relation to iron status and hepcidin. Int. Urol. Nephrol., 2020, 52(4), 749-756.
[http://dx.doi.org/10.1007/s11255-020-02434-w] [PMID: 32173772]
[128]
Bonito, B.; Silva, A.P.; Rato, F.; Santos, N.; Neves, P.L. Resistin as a predictor of cardiovascular hospital admissions and renal deterioration in diabetic patients with chronic kidney disease. J. Diabetes Complicat., 2019, 33(11), 107422.
[http://dx.doi.org/10.1016/j.jdiacomp.2019.107422] [PMID: 31484628]
[129]
Cebeci, E.; Cakan, C.; Gursu, M.; Uzun, S.; Karadag, S.; Koldas, M.; Calhan, T.; Helvaci, S.A.; Ozturk, S. The main determinants of serum resistin level in type 2 diabetic patients are renal function and inflammation not presence of microvascular complication, obesity and insulin resistance. Exp. Clin. Endocrinol. Diabetes, 2019, 127(4), 189-194.
[http://dx.doi.org/10.1055/s-0043-121262] [PMID: 29421824]
[130]
Bauer, S.; Neumeier, M.; Wanninger, J.; Walter, R.; Kopp, A.; Bala, M.; Schäffler, A.; Buechler, C. Systemic resistin is increased in type 2 diabetic patients treated with loop diuretics. J. Diabetes Complicat., 2011, 25(6), 377-381.
[http://dx.doi.org/10.1016/j.jdiacomp.2011.06.001] [PMID: 21813294]
[131]
Hida, K.; Wada, J.; Eguchi, J.; Zhang, H.; Baba, M.; Seida, A.; Hashimoto, I.; Okada, T.; Yasuhara, A.; Nakatsuka, A.; Shikata, K.; Hourai, S.; Futami, J.; Watanabe, E.; Matsuki, Y.; Hiramatsu, R.; Akagi, S.; Makino, H.; Kanwar, Y.S. Visceral adipose tissue-derived serine protease inhibitor: A unique insulin-sensitizing adipocytokine in obesity. Proc. Natl. Acad. Sci. USA, 2005, 102(30), 10610-10615.
[http://dx.doi.org/10.1073/pnas.0504703102] [PMID: 16030142]
[132]
Heiker, J.T. Vaspin (serpinA12) in obesity, insulin resistance, and inflammation. J. Pept. Sci., 2014, 20(5), 299-306.
[http://dx.doi.org/10.1002/psc.2621] [PMID: 24596079]
[133]
Kurowska, P.; Mlyczynska, E.; Dawid, M.; Jurek, M.; Klimczyk, D.; Dupont, J.; Rak, A. Review: Vaspin (SERPINA12) expression and function in endocrine cells. Cells-Basel, 2021, 10(7), 1710.
[134]
Heiker, J.T.; Klöting, N.; Kovacs, P.; Kuettner, E.B.; Sträter, N.; Schultz, S.; Kern, M.; Stumvoll, M.; Blüher, M.; Beck-Sickinger, A.G. Vaspin inhibits kallikrein 7 by serpin mechanism. Cell. Mol. Life Sci., 2013, 70(14), 2569-2583.
[http://dx.doi.org/10.1007/s00018-013-1258-8] [PMID: 23370777]
[135]
Nakatsuka, A.; Wada, J.; Iseda, I.; Teshigawara, S.; Higashio, K.; Murakami, K.; Kanzaki, M.; Inoue, K.; Terami, T.; Katayama, A.; Hida, K.; Eguchi, J.; Horiguchi, C.S.; Ogawa, D.; Matsuki, Y.; Hiramatsu, R.; Yagita, H.; Kakuta, S.; Iwakura, Y.; Makino, H. Vaspin is an adipokine ameliorating ER stress in obesity as a ligand for cell-surface GRP78/MTJ-1 complex. Diabetes, 2012, 61(11), 2823-2832.
[http://dx.doi.org/10.2337/db12-0232] [PMID: 22837305]
[136]
Nicholson, T.; Church, C.; Tsintzas, K.; Jones, R.; Breen, L.; Davis, E.T.; Baker, D.J.; Jones, S.W. Vaspin promotes insulin sensitivity of elderly muscle and is upregulated in obesity. J. Endocrinol., 2019, 241(1), JOE-18-0528.R3.
[http://dx.doi.org/10.1530/JOE-18-0528] [PMID: 30721136]
[137]
Yang, W.; Li, Y.; Tian, T.; Wang, L.; Lee, P.; Hua, Q. Serum vaspin concentration in elderly patients with type 2 diabetes mellitus and macrovascular complications. BMC Endocr. Disord., 2017, 17(1), 67.
[http://dx.doi.org/10.1186/s12902-017-0216-0] [PMID: 29065866]
[138]
Karadag, S.; Sakci, E.; Uzun, S.; Aydin, Z.; Cebeci, E.; Sumnu, A.; Ozkan, O.; Yamak, M.; Koldas, M.; Behlul, A.; Gursu, M.; Ataoglu, E.; Ozturk, S. The correlation of inflammatory markers and plasma vaspin levels in patients with diabetic nephropathy. Ren. Fail., 2016, 38(7), 1044-1049.
[http://dx.doi.org/10.1080/0886022X.2016.1183444] [PMID: 27216464]
[139]
Nakatsuka, A.; Yamaguchi, S.; Eguchi, J.; Kakuta, S.; Iwakura, Y.; Sugiyama, H.; Wada, J. A Vaspin-HSPA1L complex protects proximal tubular cells from organelle stress in diabetic kidney disease. Commun. Biol., 2021, 4(1), 373.
[http://dx.doi.org/10.1038/s42003-021-01902-y] [PMID: 33742129]
[140]
Nicholas, S.B.; Liu, J.; Kim, J.; Ren, Y.; Collins, A.R.; Nguyen, L.; Hsueh, W.A. Critical role for osteopontin in diabetic nephropathy. Kidney Int., 2010, 77(7), 588-600.
[http://dx.doi.org/10.1038/ki.2009.518] [PMID: 20130530]
[141]
Oz, O.; Tuncel, E.; Eryilmaz, S.; Fazlioglu, M.; Gul, C.B.; Ersoy, C.; Ocak, N.; Dirican, M.; Cangur, S.; Baran, I.; Imamoglu, S. Arterial elasticity and plasma levels of adiponectin and leptin in type 2 diabetic patients treated with thiazolidinediones. Endocrine, 2008, 33(1), 101-105.
[http://dx.doi.org/10.1007/s12020-008-9058-x] [PMID: 18392690]
[142]
Rose, F.J.; Webster, J.; Barry, J.B.; Phillips, L.K.; Richards, A.A.; Whitehead, J.P. Synergistic effects of ascorbic acid and thiazolidinedione on secretion of high molecular weight adiponectin from human adipocytes. Diabetes Obes. Metab., 2010, 12(12), 1084-1089.
[http://dx.doi.org/10.1111/j.1463-1326.2010.01297.x] [PMID: 20977580]
[143]
Oki, K.; Koide, J.; Nakanishi, S.; Nakashima, R.; Yamane, K. Fenofibrate increases high molecular weight adiponectin in subjects with hypertriglyceridemia. Endocr. J., 2007, 54(3), 431-435.
[http://dx.doi.org/10.1507/endocrj.K06-172] [PMID: 17457016]
[144]
Lely, A.T.; Krikken, J.A.; Bakker, S.J.; Boomsma, F.; Dullaart, R.P.; Wolffenbuttel, B.H.; Navis, G. Low dietary sodium and exogenous angiotensin II infusion decrease plasma adiponectin concentrations in healthy men. J. Clin. Endocrinol. Metab., 2007, 92(5), 1821-1826.
[http://dx.doi.org/10.1210/jc.2006-2092] [PMID: 17341566]
[145]
Gholamin, S.; Razavi, S.M.; Taghavi-Garmestani, S.M.; Ghorbanihaghjo, A.; Rashtchizadeh, N.; Safa, J.; Vatankhah, A.M.; Azizi, T.; Argani, H. Lovastatin for reduction of leptin in nondialysis patients with type 2 diabetic nephropathy. Iran. J. Kidney Dis., 2014, 8(3), 201-206.
[PMID: 24878942]

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