Obesity and Adipose Tissue-derived Cytokines in the Pathogenesis of Multiple Sclerosis

Wallin, M.T.; Culpepper, W.J.; Nichols, E.; Bhutta, Z.A.; Gebrehiwot, T.T.; Hay, S.I.; Khalil, I.A.; Krohn, K.J.; Liang, X.; Naghavi, M.; Mokdad, A.H.; Nixon, M.R.; Reiner, R.C.; Sartorius, B.; Smith, M.; Topor-Madry, R.; Wersdecker, A.; Vos, T.; Feigin, V.L.; Murray, C.J.L. GBD 2016 Multiple Sclerosis Collaborators. Global, regional, and national burden of multiple sclerosis 1990-2016: A systematic analysis for the Global Burden of Disease Study 2016. Lancet Neurol., 2019, 18(3), 269-285.
[http://dx.doi.org/10.1016/S1474-4422(18)30443-5] [PMID: 30679040]

Walton, C.; King, R.; Rechtman, L.; Kaye, W.; Leray, E.; Marrie, R.A.; Robertson, N.; La Rocca, N.; Uitdehaag, B.; van der Mei, I.; Wallin, M.; Helme, A.; Angood Napier, C.; Rijke, N.; Baneke, P. Rising prevalence of multiple sclerosis worldwide: Insights from the Atlas of MS, third edition. Mult. Scler., 2020, 26(14), 1816-1821.
[http://dx.doi.org/10.1177/1352458520970841] [PMID: 33174475]

Olsson, T.; Barcellos, L.F.; Alfredsson, L. Interactions between genetic, lifestyle and environmental risk factors for multiple sclerosis. Nat. Rev. Neurol., 2017, 13(1), 25-36.
[http://dx.doi.org/10.1038/nrneurol.2016.187] [PMID: 27934854]

Lassmann, H.; Brück, W.; Lucchinetti, C. Heterogeneity of multiple sclerosis pathogenesis: Implications for diagnosis and therapy. Trends Mol. Med., 2001, 7(3), 115-121.
[http://dx.doi.org/10.1016/S1471-4914(00)01909-2] [PMID: 11286782]

Peiravian, F.; Rajaian, H.; Samiei, A.; Gholijani, N.; Gharesi-Fard, B.; Mokaram, P.; Rahimi-Jaberi, A.; Kamali Sarvestani, E. Altered se-rum cytokine profiles in relapse phase of relapsing-remitting multiple sclerosis. Iran. J. Immunol., 2016, 13(3), 186-196.
[PMID: 27671510]

Goldenberg, M.M. Multiple sclerosis review. P&T, 2012, 37(3), 175-184.
[PMID: 22605909]

Ouchi, N.; Parker, J.L.; Lugus, J.J.; Walsh, K. Adipokines in inflammation and metabolic disease. Nat. Rev. Immunol., 2011, 11(2), 85-97.
[http://dx.doi.org/10.1038/nri2921] [PMID: 21252989]

Hurt, R.T.; Kulisek, C.; Buchanan, L.A.; McClave, S.A. The obesity epidemic: Challenges, health initiatives, and implications for gastroen-terologists. Gastroenterol. Hepatol. (N. Y.), 2010, 6(12), 780-792.
[PMID: 21301632]

Daryabor, G.; Kabelitz, D.; Kalantar, K. An update on immune dysregulation in obesity-related insulin resistance. Scand. J. Immunol., 2019, 89(4), e12747.
[http://dx.doi.org/10.1111/sji.12747] [PMID: 30593678]

Zorena, K.; Jachimowicz-Duda, O.; Ślęzak, D.; Robakowska, M.; Mrugacz, M. Adipokines and obesity. potential link to metabolic disorders and chronic complications. Int. J. Mol. Sci., 2020, 21(10), e3570.
[http://dx.doi.org/10.3390/ijms21103570] [PMID: 32443588]

Engin, A. The definition and prevalence of obesity and metabolic syndrome. Adv. Exp. Med. Biol., 2017, 960, 1-17.
[http://dx.doi.org/10.1007/978-3-319-48382-5_1] [PMID: 28585193]

Mazon, J.N.; de Mello, A.H.; Ferreira, G.K.; Rezin, G.T. The impact of obesity on neurodegenerative diseases. Life Sci., 2017, 182, 22-28.
[http://dx.doi.org/10.1016/j.lfs.2017.06.002] [PMID: 28583368]

Soliman, R.H.; Farhan, H.M.H.; Mohamed, O.; Mohammed, I.K.; Shaimaa, H.H.; Amr, H. Impact of insulin resistance and metabolic syn-drome on disability in patients with multiple sclerosis. Egypt. J. Neurol. Psychiat. Neurosurg., 2020, 56(1), e18.
[http://dx.doi.org/10.1186/s41983-020-0155-y]

Gianfrancesco, M.A.; Barcellos, L.F. Obesity and multiple sclerosis susceptibility: A review. J. Neurol. Neuromedicine, 2016, 1(7), 1-5.
[http://dx.doi.org/10.29245/2572.942X/2016/7.1064] [PMID: 27990499]

Kanoski, S.E.; Zhang, Y.; Zheng, W.; Davidson, T.L. The effects of a high-energy diet on hippocampal function and blood-brain barrier integrity in the rat. J. Alzheimers Dis., 2010, 21(1), 207-219.
[http://dx.doi.org/10.3233/JAD-2010-091414] [PMID: 20413889]

Stampanoni Bassi, M.; Iezzi, E.; Buttari, F.; Gilio, L.; Simonelli, I.; Carbone, F.; Micillo, T.; De Rosa, V.; Sica, F.; Furlan, R.; Finardi, A.; Fantozzi, R.; Storto, M.; Bellantonio, P.; Pirollo, P.; Di Lemme, S.; Musella, A.; Mandolesi, G.; Centonze, D.; Matarese, G. Obesity worsens central inflammation and disability in multiple sclerosis. Mult. Scler., 2020, 26(10), 1237-1246.
[http://dx.doi.org/10.1177/1352458519853473] [PMID: 31161863]

Hoffler, U.; Hobbie, K.; Wilson, R.; Bai, R.; Rahman, A.; Malarkey, D.; Travlos, G.; Ghanayem, B.I. Diet-induced obesity is associated with hyperleptinemia, hyperinsulinemia, hepatic steatosis, and glomerulopathy in C57Bl/6J mice. Endocrine, 2009, 36(2), 311-325.
[http://dx.doi.org/10.1007/s12020-009-9224-9] [PMID: 19669948]

Çoban, A.; Düzel, B.; Tüzün, E.; Tamam, Y. Investigation of the prognostic value of adipokines in multiple sclerosis. Mult. Scler. Relat. Disord., 2017, 15, 11-14.
[http://dx.doi.org/10.1016/j.msard.2017.04.006] [PMID: 28641765]

Düzel, B.; Tamam, Y.; Çoban, A.; Tüzün, E. Adipokines in multiple sclerosis patients with and without optic neuritis as the first clinical presentation. Immunol. Invest., 2019, 48(2), 190-197.
[http://dx.doi.org/10.1080/08820139.2018.1528270] [PMID: 30321074]

Daryabor, G.; Atashzar, M.R.; Kabelitz, D.; Meri, S.; Kalantar, K. The effects of type 2 diabetes mellitus on organ metabolism and the immune system. Front. Immunol., 2020, 11, 1582.
[http://dx.doi.org/10.3389/fimmu.2020.01582] [PMID: 32793223]

Li, V.L.; Kim, J.T.; Long, J.Z. Adipose tissue lipokines: Recent progress and future directions. Diabetes, 2020, 69(12), 2541-2548.
[http://dx.doi.org/10.2337/dbi20-0012] [PMID: 33219098]

Lefterova, M.I.; Haakonsson, A.K.; Lazar, M.A.; Mandrup, S. PPARγ and the global map of adipogenesis and beyond. Trends Endocrinol. Metab., 2014, 25(6), 293-302.
[http://dx.doi.org/10.1016/j.tem.2014.04.001] [PMID: 24793638]

Ruiz-Ojeda, F.J.; Méndez-Gutiérrez, A.; Aguilera, C.M.; Plaza-Díaz, J. Extracellular matrix remodeling of adipose tissue in obesity and metabolic diseases. Int. J. Mol. Sci., 2019, 20(19), e4888.
[http://dx.doi.org/10.3390/ijms20194888] [PMID: 31581657]

Goldberg, I. J.; Eckel, R. H.; Abumrad, N. A. Regulation of fatty acid uptake into tissues: Lipoprotein lipase- and CD36-mediated pathways. J. Lipid Res., 2009, 50(Suppl.), S86-S90.

Martyniak, K.; Masternak, M.M. Changes in adipose tissue cellular composition during obesity and aging as a cause of metabolic dysregulation. Exp. Gerontol., 2017, 94, 59-63.
[http://dx.doi.org/10.1016/j.exger.2016.12.007] [PMID: 27939445]

Makki, K.; Froguel, P.; Wolowczuk, I. Adipose tissue in obesity-related inflammation and insulin resistance: Cells, cytokines, and chemokines. ISRN Inflamm., 2013, 2013, 139239.
[http://dx.doi.org/10.1155/2013/139239] [PMID: 24455420]

Reilly, S.M.; Saltiel, A.R. Adapting to obesity with adipose tissue inflammation. Nat. Rev. Endocrinol., 2017, 13(11), 633-643.
[http://dx.doi.org/10.1038/nrendo.2017.90] [PMID: 28799554]

Hersoug, L.G.; Møller, P.; Loft, S. Role of microbiota-derived lipopolysaccharide in adipose tissue inflammation, adipocyte size and pyroptosis during obesity. Nutr. Res. Rev., 2018, 31(2), 153-163.
[http://dx.doi.org/10.1017/S0954422417000269] [PMID: 29362018]

Teixeira, T.F.; Souza, N.C.; Chiarello, P.G.; Franceschini, S.C.; Bressan, J.; Ferreira, C.L.; Peluzio, M.C. Intestinal permeability parameters in obese patients are correlated with metabolic syndrome risk factors. Clin. Nutr., 2012, 31(5), 735-740.
[http://dx.doi.org/10.1016/j.clnu.2012.02.009] [PMID: 22444236]

Cheru, L.; Saylor, C.F.; Lo, J. Gastrointestinal barrier breakdown, and adipose tissue inflammation. Curr. Obes. Rep., 2019, 8(2), 165-174.
[http://dx.doi.org/10.1007/s13679-019-00332-6] [PMID: 30847735]

Okamura, T.; Hashimoto, Y.; Hamaguchi, M.; Obora, A.; Kojima, T.; Fukui, M. Ectopic fat obesity presents the greatest risk for incident type 2 diabetes: A population-based longitudinal study. Int. J. Obes., 2019, 43(1), 139-148.
[http://dx.doi.org/10.1038/s41366-018-0076-3] [PMID: 29717276]

Koliaki, C.; Liatis, S.; Kokkinos, A. Obesity and cardiovascular disease: Revisiting an old relationship. Metabolism, 2019, 92, 98-107.
[http://dx.doi.org/10.1016/j.metabol.2018.10.011] [PMID: 30399375]

Avgerinos, K.I.; Spyrou, N.; Mantzoros, C.S.; Dalamaga, M. Obesity and cancer risk: Emerging biological mechanisms and perspectives. Metabolism, 2019, 92, 121-135.
[http://dx.doi.org/10.1016/j.metabol.2018.11.001] [PMID: 30445141]

O’Brien, P.D.; Hinder, L.M.; Callaghan, B.C.; Feldman, E.L. Neurological consequences of obesity. Lancet Neurol., 2017, 16(6), 465-477.
[http://dx.doi.org/10.1016/S1474-4422(17)30084-4] [PMID: 28504110]

Michalakis, K.; Ilias, I. SARS-CoV-2 infection and obesity: Common inflammatory and metabolic aspects. Diabetes Metab. Syndr., 2020, 14(4), 469-471.
[http://dx.doi.org/10.1016/j.dsx.2020.04.033] [PMID: 32387864]

Mauvais-Jarvis, F. Aging, Male Sex, Obesity, and metabolic inflammation create the perfect storm for COVID-19. Diabetes, 2020, 69(9), 1857-1863.
[http://dx.doi.org/10.2337/dbi19-0023] [PMID: 32669390]

Vlaicu, S.I.; Tatomir, A.; Boodhoo, D.; Vesa, S.; Mircea, P.A.; Rus, H. The role of complement system in adipose tissue-related inflammation. Immunol. Res., 2016, 64(3), 653-664.
[http://dx.doi.org/10.1007/s12026-015-8783-5] [PMID: 26754764]

Tripathy, D.; Mohanty, P.; Dhindsa, S.; Syed, T.; Ghanim, H.; Aljada, A.; Dandona, P. Elevation of free fatty acids induces inflammation and impairs vascular reactivity in healthy subjects. Diabetes, 2003, 52(12), 2882-2887.
[http://dx.doi.org/10.2337/diabetes.52.12.2882] [PMID: 14633847]

Hahm, J.R.; Jo, M.H.; Ullah, R.; Kim, M.W.; Kim, M.O. Metabolic stress alters antioxidant systems, suppresses the adiponectin receptor 1 and induces Alzheimer’s like pathology in mice brain. Cells, 2020, 9(1), e249.
[http://dx.doi.org/10.3390/cells9010249] [PMID: 31963819]

Noronha, S.S.R.; Lima, P.M.; Campos, G.S.V.; Chírico, M.T.T.; Abreu, A.R.; Figueiredo, A.B.; Silva, F.C.S.; Chianca, D.A., Jr; Lowry, C.A.; De Menezes, R.C.A. Association of high-fat diet with neuroinflammation, anxiety-like defensive behavioral responses, and altered thermoregulatory responses in male rats. Brain Behav. Immun., 2019, 80, 500-511.
[http://dx.doi.org/10.1016/j.bbi.2019.04.030] [PMID: 31022457]

Buckman, L.B.; Hasty, A.H.; Flaherty, D.K.; Buckman, C.T.; Thompson, M.M.; Matlock, B.K.; Weller, K.; Ellacott, K.L.J. Obesity in-duced by a high-fat diet is associated with increased immune cell entry into the central nervous system. Brain Behav. Immun., 2014, 35, 33-42.
[http://dx.doi.org/10.1016/j.bbi.2013.06.007] [PMID: 23831150]

Bai, M.; Wang, Y.; Han, R.; Xu, L.; Huang, M.; Zhao, J.; Lin, Y.; Song, S.; Chen, Y. Intermittent caloric restriction with a modified fasting-mimicking diet ameliorates autoimmunity and promotes recovery in a mouse model of multiple sclerosis. J. Nutr. Biochem., 2021, 87, 108493.
[http://dx.doi.org/10.1016/j.jnutbio.2020.108493] [PMID: 32920091]

Fontana, L.; Ghezzi, L.; Cross, A.H.; Piccio, L. Effects of dietary restriction on neuroinflammation in neurodegenerative diseases. J. Exp. Med., 2021, 218(2), e20190086.
[http://dx.doi.org/10.1084/jem.20190086] [PMID: 33416892]

Daneman, R.; Prat, A. The blood-brain barrier. Cold Spring Harb. Perspect. Biol., 2015, 7(1), a020412.
[http://dx.doi.org/10.1101/cshperspect.a020412] [PMID: 25561720]

Arcuri, C.; Mecca, C.; Bianchi, R.; Giambanco, I.; Donato, R. The pathophysiological role of microglia in dynamic surveillance, phagocytosis, and structural remodeling of the developing CNS. Front. Mol. Neurosci., 2017, 10, 191.
[http://dx.doi.org/10.3389/fnmol.2017.00191] [PMID: 28674485]

Jäkel, S.; Dimou, L. Glial cells and their function in the adult brain: A journey through the history of their ablation. Front. Cell. Neurosci., 2017, 11, 24.
[http://dx.doi.org/10.3389/fncel.2017.00024] [PMID: 28243193]

Antel, J.P.; Becher, B.; Ludwin, S.K.; Prat, A.; Quintana, F.J. Glial cells as regulators of neuroimmune interactions in the central nervous system. J. Immunol., 2020, 204(2), 251-255.
[http://dx.doi.org/10.4049/jimmunol.1900908] [PMID: 31907266]

Kuhn, S.; Gritti, L.; Crooks, D.; Dombrowski, Y. Oligodendrocytes in development, myelin generation and beyond. Cells, 2019, 8(11), e1424.
[http://dx.doi.org/10.3390/cells8111424] [PMID: 31726662]

Abbott, N.J. Astrocyte-endothelial interactions and blood-brain barrier permeability. J. Anat., 2002, 200(6), 629-638.
[http://dx.doi.org/10.1046/j.1469-7580.2002.00064.x] [PMID: 12162730]

Prins, M.; Schul, E.; Geurts, J.; van der Valk, P.; Drukarch, B.; van Dam, A.M. Pathological differences between white and grey matter multiple sclerosis lesions. Ann. N. Y. Acad. Sci., 2015, 1351(1), 99-113.
[http://dx.doi.org/10.1111/nyas.12841] [PMID: 26200258]

Sospedra, M.; Martin, R. Immunology of multiple sclerosis. Semin. Neurol., 2016, 36(2), 115-127.
[http://dx.doi.org/10.1055/s-0036-1579739] [PMID: 27116718]

McCaffrey, G.; Davis, T.P. Physiology and pathophysiology of the blood-brain barrier: P-glycoprotein and occludin trafficking as therapeutic targets to optimize central nervous system drug delivery. J. Investig. Med., 2012, 60(8), 1131-1140.
[http://dx.doi.org/10.2310/JIM.0b013e318276de79] [PMID: 23138008]

Minagar, A.; Alexander, J.S. Blood-brain barrier disruption in multiple sclerosis. Mult. Scler., 2003, 9(6), 540-549.
[http://dx.doi.org/10.1191/1352458503ms965oa] [PMID: 14664465]

Haghayegh Jahromi, N.; Marchetti, L.; Moalli, F.; Duc, D.; Basso, C.; Tardent, H.; Kaba, E.; Deutsch, U.; Pot, C.; Sallusto, F.; Stein, J.V.; Engelhardt, B. Intercellular adhesion molecule-1 (ICAM-1) and ICAM-2 differentially contribute to peripheral activation and CNS entry of autoaggressive Th1 and Th17 cells in experimental autoimmune encephalomyelitis. Front. Immunol., 2020, 10(10), 3056.
[http://dx.doi.org/10.3389/fimmu.2019.03056] [PMID: 31993059]

Wang, J.; Wang, J.; Wang, J.; Yang, B.; Weng, Q.; He, Q. Targeting microglia and macrophages: A potential treatment strategy for multiple sclerosis. Front. Pharmacol., 2019, 10, 286.
[http://dx.doi.org/10.3389/fphar.2019.00286] [PMID: 30967783]

Veroni, C.; Serafini, B.; Rosicarelli, B.; Fagnani, C.; Aloisi, F.; Agresti, C. Connecting immune cell infiltration to the multitasking microglia response and TNF receptor 2 induction in the multiple sclerosis brain. Front. Cell. Neurosci., 2020, 14, 190.
[http://dx.doi.org/10.3389/fncel.2020.00190] [PMID: 32733206]

Dong, Y.; Yong, V.W. When encephalitogenic T cells collaborate with microglia in multiple sclerosis. Nat. Rev. Neurol., 2019, 15(12), 704-717.
[http://dx.doi.org/10.1038/s41582-019-0253-6] [PMID: 31527807]

Wolf, Y.; Shemer, A.; Levy-Efrati, L.; Gross, M.; Kim, J-S.; Engel, A.; David, E.; Chappell-Maor, L.; Grozovski, J.; Rotkopf, R.; Biton, I.; Eilam-Altstadter, R.; Jung, S. Microglial MHC class II is dispensable for experimental autoimmune encephalomyelitis and cuprizone-induced demyelination. Eur. J. Immunol., 2018, 48(8), 1308-1318.
[http://dx.doi.org/10.1002/eji.201847540] [PMID: 29697861]

Magnus, T.; Schreiner, B.; Korn, T.; Jack, C.; Guo, H.; Antel, J.; Ifergan, I.; Chen, L.; Bischof, F.; Bar-Or, A.; Wiendl, H. Microglial expression of the B7 family member B7 homolog 1 confers strong immune inhibition: Implications for immune responses and autoimmunity in the CNS. J. Neurosci., 2005, 25(10), 2537-2546.
[http://dx.doi.org/10.1523/JNEUROSCI.4794-04.2005] [PMID: 15758163]

Karmiris, K.; Koutroubakis, I.E.; Xidakis, C.; Polychronaki, M.; Voudouri, T.; Kouroumalis, E.A. Circulating levels of leptin, adiponectin, resistin, and ghrelin in inflammatory bowel disease. Inflamm. Bowel Dis., 2006, 12(2), 100-105.
[http://dx.doi.org/10.1097/01.MIB.0000200345.38837.46] [PMID: 16432373]

Biström, M.; Hultdin, J.; Andersen, O.; Alonso-Magdalena, L.; Jons, D.; Gunnarsson, M.; Vrethem, M.; Sundström, P. Leptin levels are associated with multiple sclerosis risk. Mult. Scler., 2021, 27(1), 19-27.
[http://dx.doi.org/10.1177/1352458520905033] [PMID: 32028836]

Chougule, D.; Nadkar, M.; Venkataraman, K.; Rajadhyaksha, A.; Hase, N.; Jamale, T.; Kini, S.; Khadilkar, P.; Anand, V.; Madkaikar, M.; Pradhan, V. Adipokine interactions promote the pathogenesis of systemic lupus erythematosus. Cytokine, 2018, 111, 20-27.
[http://dx.doi.org/10.1016/j.cyto.2018.08.002] [PMID: 30098476]

Neumann, E.; Lepper, N.; Vasile, M.; Riccieri, V.; Peters, M.; Meier, F.; Hülser, M-L.; Distler, O.; Gay, S.; Mahavadi, P.; Günther, A.; Roeb, E.; Frommer, K.W.; Diller, M.; Müller-Ladner, U. Adipokine expression in systemic sclerosis lung and gastrointestinal organ involvement. Cytokine, 2019, 117, 41-49.
[http://dx.doi.org/10.1016/j.cyto.2018.11.013] [PMID: 30784899]

Matarese, G.; Sanna, V.; Lechler, R.I.; Sarvetnick, N.; Fontana, S.; Zappacosta, S.; La Cava, A. Leptin accelerates autoimmune diabetes in female NOD mice. Diabetes, 2002, 51(5), 1356-1361.
[http://dx.doi.org/10.2337/diabetes.51.5.1356] [PMID: 11978630]

Polito, R.; Nigro, E.; Messina, A.; Monaco, M.L.; Monda, V.; Scudiero, O.; Cibelli, G.; Valenzano, A.; Picciocchi, E.; Zammit, C.; Pisanelli, D.; Monda, M.; Cincione, I.R.; Daniele, A.; Messina, G. Adiponectin and orexin-A as a potential immunity link between Adipose tissue and central nervous system. Front. Physiol., 2018, 9, 982.
[http://dx.doi.org/10.3389/fphys.2018.00982] [PMID: 30140232]

Krause, M.P.; Liu, Y.; Vu, V.; Chan, L.; Xu, A.; Riddell, M.C.; Sweeney, G.; Hawke, T.J. Adiponectin is expressed by skeletal muscle fibers and influences muscle phenotype and function. Am. J. Physiol. Cell Physiol., 2008, 295(1), C203-C212.
[http://dx.doi.org/10.1152/ajpcell.00030.2008] [PMID: 18463233]

Weyer, C.; Funahashi, T.; Tanaka, S.; Hotta, K.; Matsuzawa, Y.; Pratley, R.E.; Tataranni, P.A. Hypoadiponectinemia in obesity and type 2 diabetes: Close association with insulin resistance and hyperinsulinemia. J. Clin. Endocrinol. Metab., 2001, 86(5), 1930-1935.
[http://dx.doi.org/10.1210/jcem.86.5.7463] [PMID: 11344187]

Wang, Y.; Lau, W.B.; Gao, E.; Tao, L.; Yuan, Y.; Li, R.; Wang, X.; Koch, W.J.; Ma, X-L. Cardiomyocyte-derived adiponectin is biologically active in protecting against myocardial ischemia-reperfusion injury. Am. J. Physiol. Endocrinol. Metab., 2010, 298(3), E663-E670.
[http://dx.doi.org/10.1152/ajpendo.00663.2009] [PMID: 20028965]

Yokota, T.; Oritani, K.; Takahashi, I.; Ishikawa, J.; Matsuyama, A.; Ouchi, N.; Kihara, S.; Funahashi, T.; Tenner, A.J.; Tomiyama, Y.; Matsuzawa, Y. Adiponectin, a new member of the family of soluble defense collagens, negatively regulates the growth of myelomonocytic progenitors and the functions of macrophages. Blood, 2000, 96(5), 1723-1732.
[http://dx.doi.org/10.1182/blood.V96.5.1723] [PMID: 10961870]

Leth, H.; Andersen, K.K.; Frystyk, J.; Tarnow, L.; Rossing, P.; Parving, H-H.; Flyvbjerg, A. Elevated levels of high-molecular-weight adiponectin in type 1 diabetes. J. Clin. Endocrinol. Metab., 2008, 93(8), 3186-3191.
[http://dx.doi.org/10.1210/jc.2008-0360] [PMID: 18505763]

Yamauchi, T.; Iwabu, M.; Okada-Iwabu, M.; Kadowaki, T. Adiponectin receptors: A review of their structure, function and how they work. Best Pract. Res. Clin. Endocrinol. Metab., 2014, 28(1), 15-23.
[http://dx.doi.org/10.1016/j.beem.2013.09.003] [PMID: 24417942]

Kadowaki, T.; Yamauchi, T.; Kubota, N. The physiological and pathophysiological role of adiponectin and adiponectin receptors in the peripheral tissues and CNS. FEBS Lett., 2008, 582(1), 74-80.
[http://dx.doi.org/10.1016/j.febslet.2007.11.070] [PMID: 18054335]

Neumeier, M.; Weigert, J.; Buettner, R.; Wanninger, J.; Schäffler, A.; Müller, A.M.; Killian, S.; Sauerbruch, S.; Schlachetzki, F.; Steinbrecher, A.; Aslanidis, C.; Schölmerich, J.; Buechler, C. Detection of adiponectin in cerebrospinal fluid in humans. Am. J. Physiol. Endocrinol. Metab., 2007, 293(4), E965-E969.
[http://dx.doi.org/10.1152/ajpendo.00119.2007] [PMID: 17623750]

Kusminski, C.M.; McTernan, P.G.; Schraw, T.; Kos, K.; O’Hare, J.P.; Ahima, R.; Kumar, S.; Scherer, P.E. Adiponectin complexes in human cerebrospinal fluid: Distinct complex distribution from serum. Diabetologia, 2007, 50(3), 634-642.
[http://dx.doi.org/10.1007/s00125-006-0577-9] [PMID: 17242917]

Thundyil, J.; Pavlovski, D.; Sobey, C.G.; Arumugam, T.V. Adiponectin receptor signalling in the brain. Br. J. Pharmacol., 2012, 165(2), 313-327.
[http://dx.doi.org/10.1111/j.1476-5381.2011.01560.x] [PMID: 21718299]

Wan, Z.; Mah, D.; Simtchouk, S.; Klegeris, A.; Little, J.P. Globular adiponectin induces a pro-inflammatory response in human astrocytic cells. Biochem. Biophys. Res. Commun., 2014, 446(1), 37-42.
[http://dx.doi.org/10.1016/j.bbrc.2014.02.077] [PMID: 24582565]

Song, J.; Choi, S-M.; Kim, B.C. Adiponectin regulates the polarization and function of microglia via PPAR-γ signaling under amyloid β toxicity. Front. Cell. Neurosci., 2017, 11, 64.
[http://dx.doi.org/10.3389/fncel.2017.00064] [PMID: 28326017]

Nicolas, S.; Cazareth, J.; Zarif, H.; Guyon, A.; Heurteaux, C.; Chabry, J.; Petit-Paitel, A. Globular adiponectin limits microglia pro-inflammatory phenotype through an AdipoR1/NF-κB signaling pathway. Front. Cell. Neurosci., 2017, 11, 352.
[http://dx.doi.org/10.3389/fncel.2017.00352] [PMID: 29184485]

Song, J.; Choi, S-M.; Whitcomb, D.J.; Kim, B.C. Adiponectin controls the apoptosis and the expression of tight junction proteins in brain endothelial cells through AdipoR1 under beta amyloid toxicity. Cell Death Dis., 2017, 8(10), e3102.
[http://dx.doi.org/10.1038/cddis.2017.491] [PMID: 29022894]

Sun, L.; Li, H.; Tai, L.W.; Gu, P.; Cheung, C.W. Adiponectin regulates thermal nociception in a mouse model of neuropathic pain. Br. J. Anaesth., 2018, 120(6), 1356-1367.
[http://dx.doi.org/10.1016/j.bja.2018.01.016] [PMID: 29793601]

Spranger, J.; Verma, S.; Göhring, I.; Bobbert, T.; Seifert, J.; Sindler, A.L.; Pfeiffer, A.; Hileman, S.M.; Tschöp, M.; Banks, W.A. Adiponectin does not cross the blood-brain barrier but modifies cytokine expression of brain endothelial cells. Diabetes, 2006, 55(1), 141-147.
[http://dx.doi.org/10.2337/diabetes.55.01.06.db05-1077] [PMID: 16380487]

Luo, Y.; Liu, M. Adiponectin: A versatile player of innate immunity. J. Mol. Cell Biol., 2016, 8(2), 120-128.
[http://dx.doi.org/10.1093/jmcb/mjw012] [PMID: 26993045]

Jasinski-Bergner, S.; Büttner, M.; Quandt, D.; Seliger, B.; Kielstein, H. Adiponectin and its receptors are differentially expressed in human tissues and cell lines of distinct origin. Obes. Facts, 2017, 10(6), 569-583.
[http://dx.doi.org/10.1159/000481732] [PMID: 29207395]

Yamaguchi, N.; Argueta, J.G.M.; Masuhiro, Y.; Kagishita, M.; Nonaka, K.; Saito, T.; Hanazawa, S.; Yamashita, Y. Adiponectin inhibits Toll-like receptor family-induced signaling. FEBS Lett., 2005, 579(30), 6821-6826.
[http://dx.doi.org/10.1016/j.febslet.2005.11.019] [PMID: 16325814]

Ohashi, K.; Parker, J.L.; Ouchi, N.; Higuchi, A.; Vita, J.A.; Gokce, N.; Pedersen, A.A.; Kalthoff, C.; Tullin, S.; Sams, A.; Summer, R.; Walsh, K. Adiponectin promotes macrophage polarization toward an anti-inflammatory phenotype. J. Biol. Chem., 2010, 285(9), 6153-6160.
[http://dx.doi.org/10.1074/jbc.M109.088708] [PMID: 20028977]

Mandal, P.; Pratt, B.T.; Barnes, M.; McMullen, M.R.; Nagy, L.E. Molecular mechanism for adiponectin-dependent M2 macrophage polari-zation: Link between the metabolic and innate immune activity of full-length adiponectin. J. Biol. Chem., 2011, 286(15), 13460-13469.
[http://dx.doi.org/10.1074/jbc.M110.204644] [PMID: 21357416]

Hui, X.; Gu, P.; Zhang, J.; Nie, T.; Pan, Y.; Wu, D.; Feng, T.; Zhong, C.; Wang, Y.; Lam, K.S.; Xu, A. Adiponectin enhances cold-induced browning of subcutaneous adipose tissue via promoting M2 macrophage proliferation. Cell Metab., 2015, 22(2), 279-290.
[http://dx.doi.org/10.1016/j.cmet.2015.06.004] [PMID: 26166748]

Wilk, S.; Scheibenbogen, C.; Bauer, S.; Jenke, A.; Rother, M.; Guerreiro, M.; Kudernatsch, R.; Goerner, N.; Poller, W.; Elligsen-Merkel, D.; Utku, N.; Magrane, J.; Volk, H.D.; Skurk, C. Adiponectin is a negative regulator of antigen-activated T cells. Eur. J. Immunol., 2011, 41(8), 2323-2332.
[http://dx.doi.org/10.1002/eji.201041349] [PMID: 21538348]

Yokota, T.; Meka, C.S.; Kouro, T.; Medina, K.L.; Igarashi, H.; Takahashi, M.; Oritani, K.; Funahashi, T.; Tomiyama, Y.; Matsuzawa, Y.; Kincade, P.W. Adiponectin, a fat cell product, influences the earliest lymphocyte precursors in bone marrow cultures by activation of the cyclooxygenase-prostaglandin pathway in stromal cells. J. Immunol., 2003, 171(10), 5091-5099.
[http://dx.doi.org/10.4049/jimmunol.171.10.5091] [PMID: 14607907]

Obeid, S.; Wankell, M.; Charrez, B.; Sternberg, J.; Kreuter, R.; Esmaili, S.; Ramezani-Moghadam, M.; Devine, C.; Read, S.; Bhathal, P.; Lopata, A.; Ahlensteil, G.; Qiao, L.; George, J.; Hebbard, L. Adiponectin confers protection from acute colitis and restricts a B cell immune response. J. Biol. Chem., 2017, 292(16), 6569-6582.
[http://dx.doi.org/10.1074/jbc.M115.712646] [PMID: 28258220]

Niu, T.; Cheng, L.; Wang, H.; Zhu, S.; Yang, X.; Liu, K.; Jin, H.; Xu, X. KS23, a novel peptide derived from adiponectin, inhibits retinal inflammation and downregulates the proportions of Th1 and Th17 cells during experimental autoimmune uveitis. J. Neuroinflammation, 2019, 16(1), 278.
[http://dx.doi.org/10.1186/s12974-019-1686-y] [PMID: 31883532]

Surendar, J.; Frohberger, S.J.; Karunakaran, I.; Schmitt, V.; Stamminger, W.; Neumann, A-L.; Wilhelm, C.; Hoerauf, A.; Hübner, M.P. Adiponectin limits IFN-γ and IL-17 producing CD4 T cells in obesity and restraining cell intrinsic glycolysis. Front. Immunol., 2019, 10, 2555.
[http://dx.doi.org/10.3389/fimmu.2019.02555] [PMID: 31736971]

Galvan, M.D.; Hulsebus, H.; Heitker, T.; Zeng, E.; Bohlson, S.S. Complement protein C1q and adiponectin stimulate Mer tyrosine kinase-dependent engulfment of apoptotic cells through a shared pathway. J. Innate Immun., 2014, 6(6), 780-792.
[http://dx.doi.org/10.1159/000363295] [PMID: 24942043]

Chen, B.; Liao, W-Q.; Xu, N.; Xu, H.; Wen, J-Y.; Yu, C-A.; Liu, X-Y.; Li, C-L.; Zhao, S-M.; Campbell, W. Adiponectin protects against cerebral ischemia-reperfusion injury through anti-inflammatory action. Brain Res., 2009, 1273, 129-137.
[http://dx.doi.org/10.1016/j.brainres.2009.04.002] [PMID: 19362080]

Lee, H.; Tu, T.H.; Park, B.S.; Yang, S.; Kim, J.G. Adiponectin reverses the hypothalamic microglial inflammation during short-term exposure to fat-rich diet. Int. J. Mol. Sci., 2019, 20(22), e5738.
[http://dx.doi.org/10.3390/ijms20225738] [PMID: 31731705]

Wu, X.; Luo, J.; Liu, H.; Cui, W.; Guo, K.; Zhao, L.; Bai, H.; Guo, W.; Guo, H.; Feng, D.; Qu, Y. Recombinant adiponectin peptide ameliorates brain injury following intracerebral hemorrhage by suppressing astrocyte-derived inflammation via the inhibition of Drp1-mediated mitochondrial fission. Transl. Stroke Res., 2020, 11(5), 924-939.
[http://dx.doi.org/10.1007/s12975-019-00768-x] [PMID: 31902083]

Wang, S.; Yao, Q.; Wan, Y.; Wang, J.; Huang, C.; Li, D.; Yang, B. Adiponectin reduces brain injury after intracerebral hemorrhage by reducing NLRP3 inflammasome expression. Int. J. Neurosci., 2020, 130(3), 301-308.
[http://dx.doi.org/10.1080/00207454.2019.1679810] [PMID: 31607194]

Piccio, L.; Cantoni, C.; Henderson, J.G.; Hawiger, D.; Ramsbottom, M.; Mikesell, R.; Ryu, J.; Hsieh, C.S.; Cremasco, V.; Haynes, W.; Dong, L.Q.; Chan, L.; Galimberti, D.; Cross, A.H. Lack of adiponectin leads to increased lymphocyte activation and increased disease severity in a mouse model of multiple sclerosis. Eur. J. Immunol., 2013, 43(8), 2089-2100.
[http://dx.doi.org/10.1002/eji.201242836] [PMID: 23640763]

Zhang, K.; Guo, Y.; Ge, Z.; Zhang, Z.; Da, Y.; Li, W.; Zhang, Z.; Xue, Z.; Li, Y.; Ren, Y.; Jia, L.; Chan, K-H.; Yang, F.; Yan, J.; Yao, Z.; Xu, A.; Zhang, R. Adiponectin suppresses T helper 17 cell differentiation and limits autoimmune CNS inflammation via the SIRT1/PPARγ/RORγt pathway. Mol. Neurobiol., 2017, 54(7), 4908-4920.
[http://dx.doi.org/10.1007/s12035-016-0036-7] [PMID: 27514756]

Rasooli Tehrani, A.; Gholipour, S.; Sharifi, R.; Yadegari, S.; Abbasi-Kolli, M.; Masoudian, N. Plasma levels of CTRP-3, CTRP-9 and apelin in women with multiple sclerosis. J. Neuroimmunol., 2019, 333, 576968.
[http://dx.doi.org/10.1016/j.jneuroim.2019.576968] [PMID: 31129285]

Yousefian, M.; Nemati, R.; Daryabor, G.; Gholijani, N.; Nikseresht, A.; Borhani-Haghighi, A.; Kamali-Sarvestani, E. Gender-specific association of leptin and adiponectin genes with multiple sclerosis. Am. J. Med. Sci., 2018, 356(2), 159-167.
[http://dx.doi.org/10.1016/j.amjms.2018.03.008] [PMID: 30219158]

Kraszula, L.; Jasińska, A.; Eusebio, M.; Kuna, P.; Głąbiński, A.; Pietruczuk, M. Evaluation of the relationship between leptin, resistin, adiponectin and natural regulatory T cells in relapsing-remitting multiple sclerosis. Neurol. Neurochir. Pol., 2012, 46(1), 22-28.
[http://dx.doi.org/10.5114/ninp.2012.27211] [PMID: 22426759]

Signoriello, E.; Mallardo, M.; Nigro, E.; Polito, R.; Casertano, S.; Di Pietro, A.; Coletta, M.; Monaco, M.L.; Rossi, F.; Lus, G.; Daniele, A. Adiponectin in cerebrospinal fluid from patients affected by multiple sclerosis is correlated with the progression and severity of disease. Mol. Neurobiol., 2021, 58(6), 2663-2670.
[http://dx.doi.org/10.1007/s12035-021-02287-z] [PMID: 33486671]

Nyirenda, M.H.; Fadda, G.; Healy, L.M.; Mexhitaj, I.; Poliquin-Lasnier, L.; Hanwell, H.; Saveriano, A.W.; Rozenberg, A.; Li, R.; Moore, C.S.; Belabani, C.; Johnson, T.; O’Mahony, J.; Arnold, D.L.; Yeh, E.A.; Marrie, R.A.; Dunn, S.; Banwell, B.; Bar, O. Amit, Pro-inflammatory adiponectin in pediatric-onset multiple sclerosis. Mult. Scler. J., 2021, 1, e1352458521989090.

Cheng, X.; Folco, E.J.; Shimizu, K.; Libby, P. Adiponectin induces pro-inflammatory programs in human macrophages and CD4+ T cells. J. Biol. Chem., 2012, 287(44), 36896-36904.
[http://dx.doi.org/10.1074/jbc.M112.409516] [PMID: 22948153]

Fayad, R.; Pini, M.; Sennello, J.A.; Cabay, R.J.; Chan, L.; Xu, A.; Fantuzzi, G. Adiponectin deficiency protects mice from chemically in-duced colonic inflammation. Gastroenterology, 2007, 132(2), 601-614.
[http://dx.doi.org/10.1053/j.gastro.2006.11.026] [PMID: 17258715]

Signoriello, E.; Lus, G.; Polito, R.; Casertano, S.; Scudiero, O.; Coletta, M.; Monaco, M.L.; Rossi, F.; Nigro, E.; Daniele, A. Adiponectin profile at baseline is correlated to progression and severity of multiple sclerosis. Eur. J. Neurol., 2019, 26(2), 348-355.
[http://dx.doi.org/10.1111/ene.13822] [PMID: 30300462]

Kvistad, S.S.; Myhr, K-M.; Holmøy, T.; Benth, J.Š.; Wergeland, S.; Beiske, A.G.; Bjerve, K.S.; Hovdal, H.; Midgard, R.; Sagen, J.V.; Torkildsen, Ø. Serum levels of leptin and adiponectin are not associated with disease activity or treatment response in multiple sclerosis. J. Neuroimmunol., 2018, 323, 73-77.
[http://dx.doi.org/10.1016/j.jneuroim.2018.07.011] [PMID: 30196837]

Gholamreza, D.; Sara, H.; Nima, R. Immunopathogenesis of ankylosing spondylitis: An updated review. Acta Med. Iran., 2018, 56(4), 214-225.

Beecham, A.H.; Patsopoulos, N.A.; Xifara, D.K.; Davis, M.F.; Kemppinen, A.; Cotsapas, C.; Shah, T.S.; Spencer, C.; Booth, D.; Goris, A.; Oturai, A.; Saarela, J.; Fontaine, B.; Hemmer, B.; Martin, C.; Zipp, F.; D’Alfonso, S.; Martinelli-Boneschi, F.; Taylor, B.; Harbo, H.F.; Kockum, I.; Hillert, J.; Olsson, T.; Ban, M.; Oksenberg, J.R.; Hintzen, R.; Barcellos, L.F.; Agliardi, C.; Alfredsson, L.; Alizadeh, M.; An-derson, C.; Andrews, R.; Søndergaard, H.B.; Baker, A.; Band, G.; Baranzini, S.E.; Barizzone, N.; Barrett, J.; Bellenguez, C.; Bergamaschi, L.; Bernardinelli, L.; Berthele, A.; Biberacher, V.; Binder, T.M.; Blackburn, H.; Bomfim, I.L.; Brambilla, P.; Broadley, S.; Brochet, B.; Brundin, L.; Buck, D.; Butzkueven, H.; Caillier, S.J.; Camu, W.; Carpentier, W.; Cavalla, P.; Celius, E.G.; Coman, I.; Comi, G.; Corrado, L.; Cosemans, L.; Cournu-Rebeix, I.; Cree, B.A.; Cusi, D.; Damotte, V.; Defer, G.; Delgado, S.R.; Deloukas, P.; di Sapio, A.; Dilthey, A.T.; Donnelly, P.; Dubois, B.; Duddy, M.; Edkins, S.; Elovaara, I.; Esposito, F.; Evangelou, N.; Fiddes, B.; Field, J.; Franke, A.; Freeman, C.; Frohlich, I.Y.; Galimberti, D.; Gieger, C.; Gourraud, P.A.; Graetz, C.; Graham, A.; Grummel, V.; Guaschino, C.; Hadjixenofontos, A.; Ha-konarson, H.; Halfpenny, C.; Hall, G.; Hall, P.; Hamsten, A.; Harley, J.; Harrower, T.; Hawkins, C.; Hellenthal, G.; Hillier, C.; Hobart, J.; Hoshi, M.; Hunt, S.E.; Jagodic, M. Jelčić I.; Jochim, A.; Kendall, B.; Kermode, A.; Kilpatrick, T.; Koivisto, K.; Konidari, I.; Korn, T.; Kronsbein, H.; Langford, C.; Larsson, M.; Lathrop, M.; Lebrun-Frenay, C.; Lechner-Scott, J.; Lee, M.H.; Leone, M.A.; Leppä, V.; Libera-tore, G.; Lie, B.A.; Lill, C.M.; Lindén, M.; Link, J.; Luessi, F.; Lycke, J.; Macciardi, F.; Männistö, S.; Manrique, C.P.; Martin, R.; Marti-nelli, V.; Mason, D.; Mazibrada, G.; McCabe, C.; Mero, I.L.; Mescheriakova, J.; Moutsianas, L.; Myhr, K.M.; Nagels, G.; Nicholas, R.; Nilsson, P.; Piehl, F.; Pirinen, M.; Price, S.E.; Quach, H.; Reunanen, M.; Robberecht, W.; Robertson, N.P.; Rodegher, M.; Rog, D.; Salvetti, M.; Schnetz-Boutaud, N.C.; Sellebjerg, F.; Selter, R.C.; Schaefer, C.; Shaunak, S.; Shen, L.; Shields, S.; Siffrin, V.; Slee, M.; Sorensen, P.S.; Sorosina, M.; Sospedra, M.; Spurkland, A.; Strange, A.; Sundqvist, E.; Thijs, V.; Thorpe, J.; Ticca, A.; Tienari, P.; van Duijn, C.; Visser, E.M.; Vucic, S.; Westerlind, H.; Wiley, J.S.; Wilkins, A.; Wilson, J.F.; Winkelmann, J.; Zajicek, J.; Zindler, E.; Haines, J.L.; Peri-cak-Vance, M.A.; Ivinson, A.J.; Stewart, G.; Hafler, D.; Hauser, S.L.; Compston, A.; McVean, G.; De Jager, P.; Sawcer, S.J.; McCauley, J.L. International Multiple Sclerosis Genetics Consortium (IMSGC)Wellcome Trust Case Control Consortium 2 (WTCCC2); International IBD Genetics Consortium (IIBDGC). Analysis of immune-related loci identifies 48 new susceptibility variants for multiple sclerosis. Nat. Genet., 2013, 45(11), 1353-1360.
[http://dx.doi.org/10.1038/ng.2770] [PMID: 24076602]

Visscher, P.M.; Brown, M.A.; McCarthy, M.I.; Yang, J. Five years of GWAS discovery. Am. J. Hum. Genet., 2012, 90(1), 7-24.
[http://dx.doi.org/10.1016/j.ajhg.2011.11.029] [PMID: 22243964]

Albert, P.R. What is a functional genetic polymorphism? Defining classes of functionality. J. Psychiatry Neurosci., 2011, 36(6), 363-365.
[http://dx.doi.org/10.1503/jpn.110137] [PMID: 22011561]

Farh, K.K-H.; Marson, A.; Zhu, J.; Kleinewietfeld, M.; Housley, W.J.; Beik, S.; Shoresh, N.; Whitton, H.; Ryan, R.J.H.; Shishkin, A.A.; Hatan, M.; Carrasco-Alfonso, M.J.; Mayer, D.; Luckey, C.J.; Patsopoulos, N.A.; De Jager, P.L.; Kuchroo, V.K.; Epstein, C.B.; Daly, M.J.; Hafler, D.A.; Bernstein, B.E. Genetic and epigenetic fine mapping of causal autoimmune disease variants. Nature, 2015, 518(7539), 337-343.
[http://dx.doi.org/10.1038/nature13835] [PMID: 25363779]

Iwamoto, J.; Takeda, T.; Sato, Y.; Matsumoto, H. Serum leptin concentration positively correlates with body weight and total fat mass in postmenopausal Japanese women with osteoarthritis of the knee. Arthritis (Egypt), 2011, 2011, 580632.
[http://dx.doi.org/10.1155/2011/580632] [PMID: 22046520]

Vadacca, M.; Margiotta, D.P.E.; Navarini, L.; Afeltra, A. Leptin in immuno-rheumatological diseases. Cell. Mol. Immunol., 2011, 8(3), 203-212.
[http://dx.doi.org/10.1038/cmi.2010.75] [PMID: 21399656]

Zabeau, L.; Peelman, F.; Tavernier, J. Leptin: From structural insights to the design of antagonists. Life Sci., 2015, 140, 49-56.
[http://dx.doi.org/10.1016/j.lfs.2015.04.015] [PMID: 25998027]

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]

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]

Matoba, K.; Muramatsu, R.; Yamashita, T. Leptin sustains spontaneous remyelination in the adult central nervous system. Sci. Rep., 2017, 7(1), 40397.
[http://dx.doi.org/10.1038/srep40397] [PMID: 28091609]

Tang, C-H.; Lu, D-Y.; Yang, R-S.; Tsai, H-Y.; Kao, M-C.; Fu, W-M.; Chen, Y-F. Leptin-induced IL-6 production is mediated by leptin receptor, insulin receptor substrate-1, phosphatidylinositol 3-kinase, Akt, NF-kappaB, and p300 pathway in microglia. J. Immunol., 2007, 179(2), 1292-1302.
[http://dx.doi.org/10.4049/jimmunol.179.2.1292] [PMID: 17617622]

Martín-Romero, C.; Santos-Alvarez, J.; Goberna, R.; Sánchez-Margalet, V. Human leptin enhances activation and proliferation of human circulating T lymphocytes. Cell. Immunol., 2000, 199(1), 15-24.
[http://dx.doi.org/10.1006/cimm.1999.1594] [PMID: 10675271]

Zarkesh-Esfahani, H.; Pockley, G.; Metcalfe, R.A.; Bidlingmaier, M.; Wu, Z.; Ajami, A.; Weetman, A.P.; Strasburger, C.J.; Ross, R.J. High-dose leptin activates human leukocytes via receptor expression on monocytes. J. Immunol., 2001, 167(8), 4593-4599.
[http://dx.doi.org/10.4049/jimmunol.167.8.4593] [PMID: 11591788]

Busso, N.; So, A.; Chobaz-Péclat, V.; Morard, C.; Martinez-Soria, E.; Talabot-Ayer, D.; Gabay, C. Leptin signaling deficiency impairs humoral and cellular immune responses and attenuates experimental arthritis. J. Immunol., 2002, 168(2), 875-882.
[http://dx.doi.org/10.4049/jimmunol.168.2.875] [PMID: 11777985]

Forny-Germano, L.; De Felice, F.G.; Vieira, M.N.D.N. The role of leptin and adiponectin in obesity-associated cognitive decline and Alz-heimer’s disease. Front. Neurosci., 2019, 12, 1027.
[http://dx.doi.org/10.3389/fnins.2018.01027] [PMID: 30692905]

Banks, W.A.; Farr, S.A.; Salameh, T.S.; Niehoff, M.L.; Rhea, E.M.; Morley, J.E.; Hanson, A.J.; Hansen, K.M.; Craft, S. Triglycerides cross the blood-brain barrier and induce central leptin and insulin receptor resistance. Int. J. Obes., 2018, 42(3), 391-397.
[http://dx.doi.org/10.1038/ijo.2017.231] [PMID: 28990588]

Banks, W.A.; Coon, A.B.; Robinson, S.M.; Moinuddin, A.; Shultz, J.M.; Nakaoke, R.; Morley, J.E. Triglycerides induce leptin resistance at the blood-brain barrier. Diabetes, 2004, 53(5), 1253-1260.
[http://dx.doi.org/10.2337/diabetes.53.5.1253] [PMID: 15111494]

Ramos-Lobo, A.M.; Donato, J., Jr The role of leptin in health and disease. Temperature, 2017, 4(3), 258-291.
[http://dx.doi.org/10.1080/23328940.2017.1327003] [PMID: 28944270]

Tsiotra, P.C.; Boutati, E.; Dimitriadis, G.; Raptis, S.A. High insulin and leptin increase resistin and inflammatory cytokine production from human mononuclear cells. BioMed Res. Int., 2013, 2013, 487081.
[http://dx.doi.org/10.1155/2013/487081] [PMID: 23484124]

Pinteaux, E.; Inoue, W.; Schmidt, L.; Molina-Holgado, F.; Rothwell, N.J.; Luheshi, G.N. Leptin induces interleukin-1γ release from rat microglial cells through a caspase 1 independent mechanism. J. Neurochem., 2007, 102(3), 826-833.
[http://dx.doi.org/10.1111/j.1471-4159.2007.04559.x] [PMID: 17419800]

Koga, S.; Kojima, A.; Ishikawa, C.; Kuwabara, S.; Arai, K.; Yoshiyama, Y. Effects of diet-induced obesity and voluntary exercise in a tauopathy mouse model: Implications of persistent hyperleptinemia and enhanced astrocytic leptin receptor expression. Neurobiol. Dis., 2014, 71, 180-192.
[http://dx.doi.org/10.1016/j.nbd.2014.08.015] [PMID: 25132556]

Hosoi, T.; Okuma, Y.; Nomura, Y. Expression of leptin receptors and induction of IL-1β transcript in glial cells. Biochem. Biophys. Res. Commun., 2000, 273(1), 312-315.
[http://dx.doi.org/10.1006/bbrc.2000.2937] [PMID: 10873603]

Reis, B.S.; Lee, K.; Fanok, M.H.; Mascaraque, C.; Amoury, M.; Cohn, L.B.; Rogoz, A.; Dallner, O.S.; Moraes-Vieira, P.M.; Domingos, A.I.; Mucida, D. Leptin receptor signaling in T cells is required for Th17 differentiation. J. Immunol., 2015, 194(11), 5253-5260.
[http://dx.doi.org/10.4049/jimmunol.1402996] [PMID: 25917102]

Mattioli, B.; Straface, E.; Quaranta, M.G.; Giordani, L.; Viora, M. Leptin promotes differentiation and survival of human dendritic cells and licenses them for Th1 priming. J. Immunol., 2005, 174(11), 6820-6828.
[http://dx.doi.org/10.4049/jimmunol.174.11.6820] [PMID: 15905523]

Procaccini, C.; Pucino, V.; Mantzoros, C.S.; Matarese, G. Leptin in autoimmune diseases. Metabolism, 2015, 64(1), 92-104.
[http://dx.doi.org/10.1016/j.metabol.2014.10.014] [PMID: 25467840]

Kolić I.; Stojković L.; Dinčić E.; Jovanović I.; Stanković A.; Živković M. Expression of LEP, LEPR and PGC1A genes is altered in peripheral blood mononuclear cells of patients with relapsing-remitting multiple sclerosis. J. Neuroimmunol., 2020, 338, 577090.
[http://dx.doi.org/10.1016/j.jneuroim.2019.577090] [PMID: 31704454]

Abd Elhafeez, M.A.; Zamzam, D.A.; Fouad, M.M.; Elkhawas, H.M.; Abdel Rahman, H.A. Serum leptin and body mass index in a sample of Egyptian multiple sclerosis patients. Egypt. J. Neurol. Psychiat. Neurosurg., 2020, 56(1), e107.
[http://dx.doi.org/10.1186/s41983-020-00239-3]

Matarese, G.; Di Giacomo, A.; Sanna, V.; Lord, G.M.; Howard, J.K.; Di Tuoro, A.; Bloom, S.R.; Lechler, R.I.; Zappacosta, S.; Fontana, S. Requirement for leptin in the induction and progression of autoimmune encephalomyelitis. J. Immunol., 2001, 166(10), 5909-5916.
[http://dx.doi.org/10.4049/jimmunol.166.10.5909] [PMID: 11342605]

Matarese, G.; Carrieri, P.B.; La Cava, A.; Perna, F.; Sanna, V.; De Rosa, V.; Aufiero, D.; Fontana, S.; Zappacosta, S. Leptin increase in multiple sclerosis associates with reduced number of CD4(+)CD25+ regulatory T cells. Proc. Natl. Acad. Sci. USA, 2005, 102(14), 5150-5155.
[http://dx.doi.org/10.1073/pnas.0408995102] [PMID: 15788534]

Lanzillo, R.; Carbone, F.; Quarantelli, M.; Bruzzese, D.; Carotenuto, A.; De Rosa, V.; Colamatteo, A.; Micillo, T.; De Luca Picione, C.; Saccà, F.; De Rosa, A.; Moccia, M.; Brescia Morra, V.; Matarese, G. Immunometabolic profiling of patients with multiple sclerosis identi-fies new biomarkers to predict disease activity during treatment with interferon beta-1a. Clin. Immunol., 2017, 183, 249-253.
[http://dx.doi.org/10.1016/j.clim.2017.08.011] [PMID: 28823971]

Dashti, M.; Alroughani, R.; Jacob, S.; Al-Temaimi, R. Leptin rs7799039 polymorphism is associated with multiple sclerosis risk in Ku-wait. Mult. Scler. Relat. Disord., 2019, 36, 101409.
[http://dx.doi.org/10.1016/j.msard.2019.101409] [PMID: 31563075]

Kolić I.; Stojković L.; Stankovic, A.; Stefanović M.; Dinčić E.; Zivkovic, M. Association study of rs7799039, rs1137101 and rs8192678 gene variants with disease susceptibility/severity and corresponding LEP, LEPR and PGC1A gene expression in multiple scle-rosis. Gene, 2021, 774, 145422.
[http://dx.doi.org/10.1016/j.gene.2021.145422] [PMID: 33450350]

Harroud, A.; Manousaki, D.; Butler-Laporte, G.; Mitchell, R.E.; Davey Smith, G.; Richards, J.B.; Baranzini, S.E. The relative contributions of obesity, vitamin D, leptin, and adiponectin to multiple sclerosis risk: A Mendelian randomization mediation analysis. Mult. Scler., 2021, 27(13), 1994-2000.
[http://dx.doi.org/10.1177/1352458521995484] [PMID: 33605807]

Rey, L.K.; Wieczorek, S.; Akkad, D.A.; Linker, R.A.; Chan, A.; Hoffjan, S. Polymorphisms in genes encoding leptin, ghrelin and their receptors in German multiple sclerosis patients. Mol. Cell. Probes, 2011, 25(5-6), 255-259.
[http://dx.doi.org/10.1016/j.mcp.2011.05.004] [PMID: 21664965]

Farrokhi, M.; Dabirzadeh, M.; Fadaee, E.; Beni, A.A.; Saadatpour, Z.; Rezaei, A.; Heidari, Z. Polymorphism in leptin and leptin receptor genes may modify leptin levels and represent risk factors for multiple sclerosis. Immunol. Invest., 2016, 45(4), 328-335.
[http://dx.doi.org/10.3109/08820139.2016.1157811] [PMID: 27105071]

Helfer, G.; Wu, Q-F. Chemerin: A multifaceted adipokine involved in metabolic disorders. J. Endocrinol., 2018, 238(2), R79-R94.
[http://dx.doi.org/10.1530/JOE-18-0174] [PMID: 29848608]

Zhao, L.; Yamaguchi, Y.; Sharif, S.; Du, X.Y.; Song, J.J.; Lee, D.M.; Recht, L.D.; Robinson, W.H.; Morser, J.; Leung, L.L. Chemerin158K protein is the dominant chemerin isoform in synovial and cerebrospinal fluids but not in plasma. J. Biol. Chem., 2011, 286(45), 39520-39527.
[http://dx.doi.org/10.1074/jbc.M111.258954] [PMID: 21930706]

De Henau, O.; Degroot, G-N.; Imbault, V.; Robert, V.; De Poorter, C.; Mcheik, S.; Galés, C.; Parmentier, M.; Springael, J-Y. Signaling properties of chemerin receptors CMKLR1, GPR1 and CCRL2. PLoS One, 2016, 11(10), e0164179.
[http://dx.doi.org/10.1371/journal.pone.0164179] [PMID: 27716822]

Yoshimura, T.; Oppenheim, J.J. Chemokine-like receptor 1 (CMKLR1) and chemokine (C-C motif) receptor-like 2 (CCRL2); two multi-functional receptors with unusual properties. Exp. Cell Res., 2011, 317(5), 674-684.
[http://dx.doi.org/10.1016/j.yexcr.2010.10.023] [PMID: 21056554]

Herová, M.; Schmid, M.; Gemperle, C.; Hersberger, M. ChemR23, the receptor for chemerin and resolvin E1, is expressed and functional on M1 but not on M2 macrophages. J. Immunol., 2015, 194(5), 2330-2337.
[http://dx.doi.org/10.4049/jimmunol.1402166] [PMID: 25637017]

Skrzeczyńska-Moncznik, J.; Wawro, K.; Stefańska, A.; Oleszycka, E.; Kulig, P.; Zabel, B.A.; Sułkowski, M.; Kapińska-Mrowiecka, M.; Czubak-Macugowska, M.; Butcher, E.C.; Cichy, J. Potential role of chemerin in recruitment of plasmacytoid dendritic cells to diseased skin. Biochem. Biophys. Res. Commun., 2009, 380(2), 323-327.
[http://dx.doi.org/10.1016/j.bbrc.2009.01.071] [PMID: 19168032]

Graham, K.L.; Zabel, B.A.; Loghavi, S.; Zuniga, L.A.; Ho, P.P.; Sobel, R.A.; Butcher, E.C. Chemokine-like receptor-1 expression by cen-tral nervous system-infiltrating leukocytes and involvement in a model of autoimmune demyelinating disease. J. Immunol., 2009, 183(10), 6717-6723.
[http://dx.doi.org/10.4049/jimmunol.0803435] [PMID: 19864606]

Graham, K.L.; Zhang, J.V.; Lewén, S.; Burke, T.M.; Dang, T.; Zoudilova, M.; Sobel, R.A.; Butcher, E.C.; Zabel, B.A. A novel CMKLR1 small molecule antagonist suppresses CNS autoimmune inflammatory disease. PLoS One, 2014, 9(12), e112925.
[http://dx.doi.org/10.1371/journal.pone.0112925] [PMID: 25437209]

Parolini, S.; Santoro, A.; Marcenaro, E.; Luini, W.; Massardi, L.; Facchetti, F.; Communi, D.; Parmentier, M.; Majorana, A.; Sironi, M.; Tabellini, G.; Moretta, A.; Sozzani, S. The role of chemerin in the colocalization of NK and dendritic cell subsets into inflamed tissues. Blood, 2007, 109(9), 3625-3632.
[http://dx.doi.org/10.1182/blood-2006-08-038844] [PMID: 17202316]

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]

Aruna, B.; Islam, A.; Ghosh, S.; Singh, A.K.; Vijayalakshmi, M.; Ahmad, F.; Ehtesham, N.Z. Biophysical analyses of human resistin: Oligomer formation suggests novel biological function. Biochemistry, 2008, 47(47), 12457-12466.
[http://dx.doi.org/10.1021/bi801266k] [PMID: 18975914]

Lee, S.; Lee, H-C.; Kwon, Y-W.; Lee, S.E.; Cho, Y.; Kim, J.; Lee, S.; Kim, J-Y.; Lee, J.; Yang, H-M.; Mook-Jung, I.; Nam, K-Y.; Chung, J.; Lazar, M.A.; Kim, H-S. Adenylyl cyclase-associated protein 1 is a receptor for human resistin and mediates inflammatory actions of hu-man monocytes. Cell Metab., 2014, 19(3), 484-497.
[http://dx.doi.org/10.1016/j.cmet.2014.01.013] [PMID: 24606903]

Daquinag, A.C.; Zhang, Y.; Amaya-Manzanares, F.; Simmons, P.J.; Kolonin, M.G. An isoform of decorin is a resistin receptor on the surface of adipose progenitor cells. Cell Stem Cell, 2011, 9(1), 74-86.
[http://dx.doi.org/10.1016/j.stem.2011.05.017] [PMID: 21683670]

Tarkowski, A.; Bjersing, J.; Shestakov, A.; Bokarewa, M.I. Resistin competes with lipopolysaccharide for binding to toll-like receptor 4. J. Cell. Mol. Med., 2010, 14(6B), 1419-1431.
[http://dx.doi.org/10.1111/j.1582-4934.2009.00899.x] [PMID: 19754671]

Li, F-P.; He, J.; Li, Z-Z.; Luo, Z-F.; Yan, L.; Li, Y. Effects of resistin expression on glucose metabolism and hepatic insulin resistance. Endocrine, 2009, 35(2), 243-251.
[http://dx.doi.org/10.1007/s12020-009-9148-4] [PMID: 19184634]

Boström, E.A.; Tarkowski, A.; Bokarewa, M. Resistin is stored in neutrophil granules being released upon challenge with inflammatory stimuli. Biochim. Biophys. Acta, 2009, 1793(12), 1894-1900.
[http://dx.doi.org/10.1016/j.bbamcr.2009.09.008] [PMID: 19770005]

Silswal, N.; Singh, A.K.; Aruna, B.; Mukhopadhyay, S.; Ghosh, S.; Ehtesham, N.Z. Human resistin stimulates the pro-inflammatory cyto-kines TNF-alpha and IL-12 in macrophages by NF-kappaB-dependent pathway. Biochem. Biophys. Res. Commun., 2005, 334(4), 1092-1101.
[http://dx.doi.org/10.1016/j.bbrc.2005.06.202] [PMID: 16039994]

Berghoff, M.; Hochberg, A.; Schmid, A.; Schlegel, J.; Karrasch, T.; Kaps, M.; Schäffler, A. Quantification and regulation of the adipokines resistin and progranulin in human cerebrospinal fluid. Eur. J. Clin. Invest., 2016, 46(1), 15-26.
[http://dx.doi.org/10.1111/eci.12558] [PMID: 26509463]

Dong, X-Q.; Yang, S-B.; Zhu, F-L.; Lv, Q-W.; Zhang, G-H.; Huang, H-B. Resistin is associated with mortality in patients with traumatic brain injury. Crit. Care, 2010, 14(5), R190.
[http://dx.doi.org/10.1186/cc9307] [PMID: 21029428]

Demirci, S. Aynalı A.; Demirci, K.; Demirci, S.; Arıdoğan, B.C. The serum levels of resistin and its relationship with other proinflamma-tory cytokines in patients with Alzheimer’s disease. Clin. Psychopharmacol. Neurosci., 2017, 15(1), 59-63.
[http://dx.doi.org/10.9758/cpn.2017.15.1.59] [PMID: 28138112]

Wysocka, M.B.; Pietraszek-Gremplewicz, K.; Nowak, D. The Role of apelin in cardiovascular diseases, obesity and cancer. Front. Physiol., 2018, 9, 557.
[http://dx.doi.org/10.3389/fphys.2018.00557] [PMID: 29875677]

Chapman, N.A.; Dupré, D.J.; Rainey, J.K. The apelin receptor: Physiology, pathology, cell signalling, and ligand modulation of a peptide-activated class A GPCR. Biochem. Cell Biol., 2014, 92(6), 431-440.
[http://dx.doi.org/10.1139/bcb-2014-0072] [PMID: 25275559]

Yu, X-H.; Tang, Z-B.; Liu, L-J.; Qian, H.; Tang, S-L.; Zhang, D-W.; Tian, G-P.; Tang, C-K. Apelin and its receptor APJ in cardiovascular diseases. Clin. Chim. Acta, 2014, 428, 1-8.
[http://dx.doi.org/10.1016/j.cca.2013.09.001] [PMID: 24055369]

Duan, J.; Cui, J.; Yang, Z.; Guo, C.; Cao, J.; Xi, M.; Weng, Y.; Yin, Y.; Wang, Y.; Wei, G.; Qiao, B.; Wen, A. Neuroprotective effect of Apelin 13 on ischemic stroke by activating AMPK/GSK-3β/Nrf2 signaling. J. Neuroinflammation, 2019, 16(1), 24.
[http://dx.doi.org/10.1186/s12974-019-1406-7] [PMID: 30709405]

Izgüt-Uysal, V.N.; Gemici, B.; Birsen, I.; Acar, N.; Üstünel, I. The effect of apelin on the functions of peritoneal macrophages. Physiol. Res., 2017, 66(3), 489-496.
[http://dx.doi.org/10.33549/physiolres.933349] [PMID: 28248533]

Zhou, H.; Yang, R.; Wang, W.; Xu, F.; Xi, Y.; Brown, R.A.; Zhang, H.; Shi, L.; Zhu, D.; Gong, D-W. Fc-apelin fusion protein attenuates lipopolysaccharide-induced liver injury in mice. Sci. Rep., 2018, 8(1), e11428.
[http://dx.doi.org/10.1038/s41598-018-29491-7]

Akcılar, R.; Turgut, S.; Caner, V.; Akcılar, A.; Ayada, C.; Elmas, L.; Özcan, T.O. The effects of apelin treatment on a rat model of type 2 diabetes. Adv. Med. Sci., 2015, 60(1), 94-100.
[http://dx.doi.org/10.1016/j.advms.2014.11.001] [PMID: 25625368]

Leeper, N.J.; Tedesco, M.M.; Kojima, Y.; Schultz, G.M.; Kundu, R.K.; Ashley, E.A.; Tsao, P.S.; Dalman, R.L.; Quertermous, T. Apelin prevents aortic aneurysm formation by inhibiting macrophage inflammation. Am. J. Physiol. Heart Circ. Physiol., 2009, 296(5), H1329-H1335.
[http://dx.doi.org/10.1152/ajpheart.01341.2008] [PMID: 19304942]

Shao, Z-Q.; Dou, S-S.; Zhu, J-G.; Wang, H-Q.; Wang, C-M.; Cheng, B-H.; Bai, B. Apelin-13 inhibits apoptosis and excessive autophagy in cerebral ischemia/reperfusion injury. Neural Regen. Res., 2021, 16(6), 1044-1051.
[http://dx.doi.org/10.4103/1673-5374.300725] [PMID: 33269749]

Chu, H.; Yang, X.; Huang, C.; Gao, Z.; Tang, Y.; Dong, Q. Apelin-13 protects against ischemic blood-brain barrier damage through the effects of aquaporin-4. Cerebrovasc. Dis., 2017, 44(1-2), 10-25.
[http://dx.doi.org/10.1159/000460261] [PMID: 28402976]

Luo, H.; Xiang, Y.; Qu, X.; Liu, H.; Liu, C.; Li, G.; Han, L.; Qin, X. Apelin-13 suppresses neuroinflammation against cognitive deficit in a streptozotocin-induced rat model of Alzheimer’s disease through activation of BDNF-TrkB signaling pathway. Front. Pharmacol., 2019, 10, 395.
[http://dx.doi.org/10.3389/fphar.2019.00395] [PMID: 31040784]

Chen, P.; Wang, Y.; Chen, L.; Song, N.; Xie, J. Apelin-13 protects dopaminergic neurons against rotenone-induced neurotoxicity through the AMPK/mTOR/ULK-1 mediated autophagy activation. Int. J. Mol. Sci., 2020, 21(21), e8376.
[http://dx.doi.org/10.3390/ijms21218376] [PMID: 33171641]

Zhou, S.; Guo, X.; Chen, S.; Xu, Z.; Duan, W.; Zeng, B. Apelin-13 regulates LPS-induced N9 microglia polarization involving STAT3 signaling pathway. Neuropeptides, 2019, 76, 101938.
[http://dx.doi.org/10.1016/j.npep.2019.101938] [PMID: 31255353]

Ponath, G.; Ramanan, S.; Mubarak, M.; Housley, W.; Lee, S.; Sahinkaya, F.R.; Vortmeyer, A.; Raine, C.S.; Pitt, D. Myelin phagocytosis by astrocytes after myelin damage promotes lesion pathology. Brain, 2017, 140(2), 399-413.
[http://dx.doi.org/10.1093/brain/aww298] [PMID: 28007993]

Saddi-Rosa, P.; Oliveira, C.S.V.; Giuffrida, F.M.A.; Reis, A.F. Visfatin, glucose metabolism and vascular disease: A review of evidence. Diabetol. Metab. Syndr., 2010, 2(1), 21.
[http://dx.doi.org/10.1186/1758-5996-2-21] [PMID: 20346149]

Sun, Z.; Lei, H.; Zhang, Z. Pre-B cell colony enhancing factor (PBEF), a cytokine with multiple physiological functions. Cytokine Growth Factor Rev., 2013, 24(5), 433-442.
[http://dx.doi.org/10.1016/j.cytogfr.2013.05.006] [PMID: 23787158]

Garten, A.; Schuster, S.; Penke, M.; Gorski, T.; de Giorgis, T.; Kiess, W. Physiological and pathophysiological roles of NAMPT and NAD metabolism. Nat. Rev. Endocrinol., 2015, 11(9), 535-546.
[http://dx.doi.org/10.1038/nrendo.2015.117] [PMID: 26215259]

Galli, U.; Colombo, G.; Travelli, C.; Tron, G.C.; Genazzani, A.A.; Grolla, A.A. Recent advances in NAMPT inhibitors: A novel immuno-therapic strategy. Front. Pharmacol., 2020, 11, 656.
[http://dx.doi.org/10.3389/fphar.2020.00656] [PMID: 32477131]

Romacho, T.; Valencia, I.; Ramos-González, M.; Vallejo, S.; López-Esteban, M.; Lorenzo, O.; Cannata, P.; Romero, A.; San Hipólito-Luengo, A.; Gómez-Cerezo, J.F.; Peiró, C.; Sánchez-Ferrer, C.F. Visfatin/eNampt induces endothelial dysfunction in vivo: A role for Toll-Like Receptor 4 and NLRP3 inflammasome. Sci. Rep., 2020, 10(1), 5386.
[http://dx.doi.org/10.1038/s41598-020-62190-w] [PMID: 32214150]

Samara, A.; Pfister, M.; Marie, B.; Visvikis-Siest, S. Visfatin, low-grade inflammation and body mass index (BMI). Clin. Endocrinol. (Oxf.), 2008, 69(4), 568-574.
[http://dx.doi.org/10.1111/j.1365-2265.2008.03205.x] [PMID: 18248642]

Dakroub, A.; Nasser, S.A.; Kobeissy, F.; Yassine, H.M.; Orekhov, A.; Sharifi-Rad, J.; Iratni, R.; El-Yazbi, A.F.; Eid, A.H. Visfatin: An emerging adipocytokine bridging the gap in the evolution of cardiovascular diseases. J. Cell. Physiol., 2021, 236(9), 6282-6296.
[http://dx.doi.org/10.1002/jcp.30345] [PMID: 33634486]

Tu, T.H.; Nam-Goong, I.S.; Lee, J.; Yang, S.; Kim, J.G. Visfatin triggers anorexia and body weight loss through regulating the inflammato-ry response in the hypothalamic microglia. Mediators Inflamm., 2017, 2017, 1958947.
[http://dx.doi.org/10.1155/2017/1958947] [PMID: 29362519]

Chen, C-X.; Huang, J.; Tu, G-Q.; Lu, J-T.; Xie, X.; Zhao, B.; Wu, M.; Shi, Q-J.; Fang, S-H.; Wei, E-Q.; Zhang, W-P.; Lu, Y-B. NAMPT inhibitor protects ischemic neuronal injury in rat brain via anti-neuroinflammation. Neuroscience, 2017, 356, 193-206.
[http://dx.doi.org/10.1016/j.neuroscience.2017.05.022] [PMID: 28528966]

Mirzaei, K.; Hossein-Nezhad, A.; Mokhtari, F.; Najmafshar, A.; Nikoo, M.K. Visfatin/NAMPT/PBCEF and cytokine concentration in mul-tiple sclerosis patients compared to healthy subjects. Eur. J. Inflamm., 2011, 9(1), 31-37.
[http://dx.doi.org/10.1177/1721727X1100900105]

Baranowska-Bik, A.; Uchman, D.; Litwiniuk, A.; Kalisz, M. Martyńska, L.; Baranowska, B.; Bik, W.; Kochanowski, J. Peripheral levels of selected adipokines in patients with newly diagnosed multiple sclerosis. Endokrynol. Pol., 2020, 71(2), 109-115.
[http://dx.doi.org/10.5603/EP.a2020.0008] [PMID: 32154570]

Natarajan, R.; Hagman, S.; Hämälainen, M.; Leppänen, T.; Dastidar, P.; Moilanen, E.; Elovaara, I. Adipsin is associated with multiple scle-rosis: A follow-up study of adipokines. Mult. Scler. Int., 2015, 2015, 371734.
[http://dx.doi.org/10.1155/2015/371734] [PMID: 26634156]

Wu, X.; Hutson, I.; Akk, A.M.; Mascharak, S.; Pham, C.T.N.; Hourcade, D.E.; Brown, R.; Atkinson, J.P.; Harris, C.A. Contribution of adipose-derived factor d/adipsin to complement alternative pathway activation: Lessons from lipodystrophy. J. Immunol., 2018, 200(8), 2786-2797.
[http://dx.doi.org/10.4049/jimmunol.1701668] [PMID: 29531168]

Ohtsuki, T.; Satoh, K.; Shimizu, T.; Ikeda, S.; Kikuchi, N.; Satoh, T.; Kurosawa, R.; Nogi, M.; Sunamura, S.; Yaoita, N.; Omura, J.; Aoki, T.; Tatebe, S.; Sugimura, K.; Takahashi, J.; Miyata, S.; Shimokawa, H. Identification of adipsin as a novel prognostic biomarker in pa-tients with coronary artery disease. J. Am. Heart Assoc., 2019, 8(23), e013716.
[http://dx.doi.org/10.1161/JAHA.119.013716] [PMID: 31752640]

Gonzalez-Garza, M.T.; Martinez, H.R.; Cruz-Vega, D.E.; Hernandez-Torre, M.; Moreno-Cuevas, J.E. Adipsin, MIP-1b, and IL-8 as CSF biomarker panels for ALS diagnosis. Dis. Markers, 2018, 2018, 3023826.
[http://dx.doi.org/10.1155/2018/3023826] [PMID: 30405855]

Hietaharju, A.; Kuusisto, H.; Nieminen, R.; Vuolteenaho, K.; Elovaara, I.; Moilanen, E. Elevated cerebrospinal fluid adiponectin and adip-sin levels in patients with multiple sclerosis: A Finnish co-twin study. Eur. J. Neurol., 2010, 17(2), 332-334.
[http://dx.doi.org/10.1111/j.1468-1331.2009.02701.x] [PMID: 19538214]

Watkins, L.M.; Neal, J.W.; Loveless, S.; Michailidou, I.; Ramaglia, V.; Rees, M.I.; Reynolds, R.; Robertson, N.P.; Morgan, B.P.; Howell, O.W. Complement is activated in progressive multiple sclerosis cortical grey matter lesions. J. Neuroinflammation, 2016, 13(1), 161.
[http://dx.doi.org/10.1186/s12974-016-0611-x] [PMID: 27333900]

Goetzl, E.J.; Schwartz, J.B.; Abner, E.L.; Jicha, G.A.; Kapogiannis, D. High complement levels in astrocyte-derived exosomes of Alz-heimer disease. Ann. Neurol., 2018, 83(3), 544-552.
[http://dx.doi.org/10.1002/ana.25172] [PMID: 29406582]