Peptide Hormones and Adipose Tissue

Peptide Hormones and Adipose Tissue: Comparison

Please note this is a comparison between Version 2 by Conner Chen and Version 1 by Marek Skrzypski.

Peptide hormones play a prominent role in controlling energy homeostasis and metabolism. They have been implicated in controlling appetite, the function of the gastrointestinal and cardiovascular systems, energy expenditure, and reproduction. Furthermore, there is growing evidence indicating that peptide hormones and their receptors contribute to energy homeostasis regulation by interacting with white and brown adipose tissue.

adipocytes
fat tissue
peptide hormones

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References

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, 425–432.
Rocha, V.Z.; Libby, P. The Multiple Facets of the Fat Tissue. Thyroid 2008, 18, 175–183.
World Health Organization (WHO). Obesity: Preventing and managing the global epidemic. In Report of a WHO Consultation; Technical Report Series; World Health Organization: Geneva, Switzerland, 2000; Volume 894, pp. 1–253.
Tyagi, A.; Kapoor, P.; Kumar, R.; Chaudhary, K.; Gautam, A.; Raghava, G.P.S. In Silico Models for Designing and Discovering Novel Anticancer Peptides. Sci. Rep. 2013, 3, 2984.
Gao, S.; McMillan, R.P.; Zhu, Q.; Lopaschuk, G.D.; Hulver, M.W.; Butler, A.A. Therapeutic effects of adropin on glucose tolerance and substrate utilization in diet-induced obese mice with insulin resistance. Mol. Metab. 2015, 4, 310–324.
Kumar, K.G.; Trevaskis, J.L.; Lam, D.D.; Sutton, G.M.; Koza, R.A.; Chouljenko, V.N.; Kousoulas, K.G.; Rogers, P.M.; Kesterson, R.A.; Thearle, M.; et al. Identification of Adropin as a Secreted Factor Linking Dietary Macronutrient Intake with Energy Homeostasis and Lipid Metabolism. Cell Metab. 2008, 8, 468–481.
Gao, S.; Stevens, J.R.; Butler, A.A. Adropin—A circulating factor in metabolic control or a drop in the ocean? Expert Rev. Endocrinol. Metab. 2016, 11, 239–241.
Ghoshal, S.; Stevens, J.R.; Billon, C.; Girardet, C.; Sitaula, S.; Leon, A.S.; Rao, D.; Skinner, J.S.; Rankinen, T.; Bouchard, C.; et al. Adropin: An endocrine link between the biological clock and cholesterol homeostasis. Mol. Metab. 2018, 8, 51–64.
Lian, A.; Wu, K.; Liu, T.; Jiang, N.; Jiang, Q. Adropin induction of lipoprotein lipase expression in tilapia hepatocytes. J. Mol. Endocrinol. 2016, 56, 11–22.
Butler, A.A.; Zhang, J.; Price, C.A.; Stevens, J.R.; Graham, J.L.; Stanhope, K.L.; King, S.; Krauss, R.M.; Bremer, A.A.; Havel, P.J. Low plasma adropin concentrations increase risks of weight gain and metabolic dysregulation in response to a high-sugar diet in male nonhuman primates. J. Biol. Chem. 2019, 294, 9706–9719.
Aydin, S.; Kuloglu, T.; Aydin, S.; Eren, M.N.; Yilmaz, M.; Kalayci, M.; Sahin, I.; Kocaman, N.; Çitil, C.; Kendir, Y. Expression of adropin in rat brain, cerebellum, kidneys, heart, liver, and pancreas in streptozotocin-induced diabetes. Mol. Cell. Biochem. 2013, 380, 73–81.
Choi, H.-N.; Yim, J.-E. Plasma Adropin as a Potential Marker Predicting Obesity and Obesity-associated Cancer in Korean Patients with Type 2 Diabetes Mellitus. J. Cancer Prev. 2018, 23, 191–196.
Stein, L.M.; Yosten, G.L.C.; Samson, W.K. Adropin acts in brain to inhibit water drinking: Potential interaction with the orphan G protein-coupled receptor, GPR19. Am. J. Physiol. Integr. Comp. Physiol. 2016, 310, R476–R480.
Rao, A.; Herr, D.R. G protein-coupled receptor GPR19 regulates E-cadherin expression and invasion of breast cancer cells. Biochim. Biophys. Acta Bioenerg. 2017, 1864, 1318–1327.
O’Dowd, B.F.; Nguyen, T.; Lynch, K.R.; Kolakowski, L.F.; Thompson, M.; Cheng, R.; Marchese, A.; Ng, G.; Heng, H.H.; George, S.R. A novel gene codes for a putative G protein-coupled receptor with an abundant expression in brain. FEBS Lett. 1996, 394, 325–329.
Wong, C.-M.; Wang, Y.; Lee, J.T.H.; Huang, Z.; Wu, D.; Xu, A.; Lam, K.S.L. Adropin Is a Brain Membrane-bound Protein Regulating Physical Activity via the NB-3/Notch Signaling Pathway in Mice. J. Biol. Chem. 2014, 289, 25976–25986.
Butler, A.A.; Tam, C.S.; Stanhope, K.L.; Wolfe, B.M.; Ali, M.R.; O’Keeffe, M.; St-Onge, M.-P.; Ravussin, E.; Havel, P.J. Low Circulating Adropin Concentrations with Obesity and Aging Correlate with Risk Factors for Metabolic Disease and Increase after Gastric Bypass Surgery in Humans. J. Clin. Endocrinol. Metab. 2012, 97, 3783–3791.
Sayın, O.; Tokgöz, Y.; Arslan, N. Investigation of adropin and leptin levels in pediatric obesity-related nonalcoholic fatty liver disease. J. Pediatr. Endocrinol. Metab. 2014, 27, 479–484.
Yu, H.-Y.; Zhao, P.; Wu, M.-C.; Liu, J.; Yin, W. Serum adropin levels are decreased in patients with acute myocardial infarction. Regul. Pept. 2014, 190–191, 46–49.
Zang, H.; Jiang, F.; Cheng, X.; Xu, H.; Hu, X. Serum adropin levels are decreased in Chinese type 2 diabetic patients and negatively correlated with body mass index. Endocr. J. 2018, 65, 685–691.
Ganesh-Kumar, K.; Zhang, J.; Gao, S.; Rossi, J.; McGuinness, O.P.; Halem, H.H.; Culler, M.D.; Mynatt, R.L.; Butler, A.A. Adropin Deficiency Is Associated with Increased Adiposity and Insulin Resistance. Obesity 2012, 20, 1394–1402.
Jasaszwili, M.; Wojciechowicz, T.; Billert, M.; Strowski, M.Z.; Nowak, K.W.; Skrzypski, M. Effects of adropin on proliferation and differentiation of 3T3-L1 cells and rat primary preadipocytes. Mol. Cell. Endocrinol. 2019, 496, 110532.
Jasaszwili, M.; Wojciechowicz, T.; Strowski, M.Z.; Nowak, K.W.; Skrzypski, M. Adropin stimulates proliferation but suppresses differentiation in rat primary brown preadipocytes. Arch. Biochem. Biophys. 2020, 692, 108536.
Santos, L.C.; Arneson, D.; Krishnan, K.C.; Ahn, I.S.; Diamante, G.; Cely, I.; Butte, A.J.; Lusis, A.J.; Yang, X.; Rajbhandari, P. Cold-associated mammokines preserve adipocyte identity. bioRxiv 2020.
Nakagami, H. The Mechanism of White and Brown Adipocyte Differentiation. Diabetes Metab. J. 2013, 37, 85–90.
O’Dowd, B.F.; Heiber, M.; Chan, A.; Heng, H.H.; Tsui, L.-C.; Kennedy, J.L.; Shi, X.; Petronis, A.; George, S.R.; Nguyen, T. A human gene that shows identity with the gene encoding the angiotensin receptor is located on chromosome 11. Gene 1993, 136, 355–360.
Zhang, J.; Zhou, Y.; Wu, C.; Wan, Y.; Fang, C.; Li, J.; Fang, W.; Yi, R.; Zhu, G.; Li, J.; et al. Characterization of the Apelin/Elabela Receptors (APLNR) in Chickens, Turtles, and Zebrafish: Identification of a Novel Apelin-Specific Receptor in Teleosts. Front. Endocrinol. 2018, 9, 756.
Pope, G.R.; Roberts, E.M.; Lolait, S.J.; O’Carroll, A.-M. Central and peripheral apelin receptor distribution in the mouse: Species differences with rat. Peptides 2012, 33, 139–148.
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, 431–440.
Zhang, Y.; Wang, Y.; Lou, Y.; Luo, M.; Lu, Y.; Li, Z.; Wang, Y.; Miao, L. Elabela, a newly discovered APJ ligand: Similarities and differences with Apelin. Peptides 2018, 109, 23–32.
Tatemoto, K.; Hosoya, M.; Habata, Y.; Fujii, R.; Kakegawa, T.; Zou, M.-X.; Kawamata, Y.; Fukusumi, S.; Hinuma, S.; Kitada, C.; et al. Isolation and Characterization of a Novel Endogenous Peptide Ligand for the Human APJ Receptor. Biochem. Biophys. Res. Commun. 1998, 251, 471–476.
Chng, S.C.; Ho, L.; Tian, J.; Reversade, B. ELABELA: A Hormone Essential for Heart Development Signals via the Apelin Receptor. Dev. Cell 2013, 27, 672–680.
Lee, D.K.; Cheng, R.; Nguyen, T.; Fan, T.; Kariyawasam, A.P.; Liu, Y.; Osmond, D.H.; George, S.R.; O’Dowd, B.F. Characterization of Apelin, the Ligand for the APJ Receptor. J. Neurochem. 2001, 74, 34–41.
De Falco, M.; De Luca, L.; Onori, N.; Cavallotti, I.; Artigiano, F.; Esposito, V.; De Luca, B.; Laforgia, V.; Groeger, A.M.; De Luca, A. Apelin expression in normal human tissues. In Vivo 2002, 16, 333–336.
Boucher, J.; Masri, B.; Daviaud, D.; Gesta, S.; Guigné, C.; Mazzucotelli, A.; Castan-Laurell, I.; Tack, I.; Knibiehler, B.; Carpéné, C.; et al. Apelin, a Newly Identified Adipokine Up-Regulated by Insulin and Obesity. Endocrinology 2005, 146, 1764–1771.
De Mota, N.; Lenkei, Z.; Llorens-Cortès, C. Cloning, Pharmacological Characterization and Brain Distribution of the Rat Apelin Receptor. Neuroendocrinology 2000, 72, 400–407.
Medhurst, A.D.; Jennings, C.A.; Robbins, M.J.; Davis, R.P.; Ellis, C.; Winborn, K.Y.; Lawrie, K.W.M.; Hervieu, G.; Riley, G.; Bolaky, J.E.; et al. Pharmacological and immunohistochemical characterization of the APJ receptor and its endogenous ligand apelin. J. Neurochem. 2003, 84, 1162–1172.
Tatemoto, K.; Takayama, K.; Zou, M.-X.; Kumaki, I.; Zhang, W.; Kumano, K.; Fujimiya, M. The novel peptide apelin lowers blood pressure via a nitric oxide-dependent mechanism. Regul. Pept. 2001, 99, 87–92.
Sunter, D.; Hewson, A.K.; Dickson, S.L. Intracerebroventricular injection of apelin-13 reduces food intake in the rat. Neurosci. Lett. 2003, 353, 1–4.
O’Shea, M.; Hansen, M.J.; Tatemoto, K.; Morris, M.J. Inhibitory Effect of Apelin-12 on Nocturnal Food Intake in the Rat. Nutr. Neurosci. 2003, 6, 163–167.
Ferrante, C.; Orlando, G.; Recinella, L.; Leone, S.; Chiavaroli, A.; Di Nisio, C.; Shohreh, R.; Manippa, F.; Ricciuti, A.; Vacca, M.; et al. Central apelin-13 administration modulates hypothalamic control of feeding. J. Boil. Regul. Homeost. Agents 2016, 30, 883–888.
Valle, A.; Hoggard, N.; Adams, A.C.; Roca, P.; Speakman, J.R. Chronic central administration of apelin-13 over 10 days increases food intake, body weight, locomotor activity and body temperature in C57BL/6 mice. J. Neuroendocr. 2007, 20, 79–84.
Daviaud, D.; Boucher, J.; Gesta, S.; Dray, C.; Guigne, C.; Quilliot, D.; Ayav, A.; Ziegler, O.; Carpene, C.; Saulnier-Blache, J.-S.; et al. TNFα up-regulates apelin expression in human and mouse adipose tissue. FASEB J. 2006, 20, 1528–1530.
Wei, L.; Hou, X.; Tatemoto, K. Regulation of apelin mRNA expression by insulin and glucocorticoids in mouse 3T3-L1 adipocytes. Regul. Pept. 2005, 132, 27–32.
Geiger, K.; Muendlein, A.; Stark, N.; Saely, C.H.; Wabitsch, M.; Fraunberger, P.; Drexel, H. Hypoxia Induces Apelin Expression in Human Adipocytes. Horm. Metab. Res. 2011, 43, 380–385.
Lorente-Cebrián, S.; Bustos, M.; Marti, A.; Martinez, J.A.; Moreno-Aliaga, M.J. Eicosapentaenoic acid up-regulates apelin secretion and gene expression in 3T3-L1 adipocytes. Mol. Nutr. Food Res. 2010, 54, S104–S111.
Han, S.; Wang, G.; Qi, X.; Englander, E.W.; Greeley, G.H. Involvement of a Stat3 binding site in inflammation-induced enteric apelin expression. Am. J. Physiol. Gastrointest. Liver Physiol. 2008, 295, G1068–G1078.
Mazzucotelli, A.; Ribet, C.; Castan-Laurell, I.; Daviaud, D.; Guigné, C.; Langin, D.; Valet, P. The transcriptional co-activator PGC-1α up regulates apelin in human and mouse adipocytes. Regul. Pept. 2008, 150, 33–37.
Hung, W.-W.; Hsieh, T.-J.; Lin, T.; Chou, P.-C.; Hsiao, P.-J.; Lin, K.-D.; Shin, S.-J. Blockade of the Renin-Angiotensin System Ameliorates Apelin Production in 3T3-L1 Adipocytes. Cardiovasc. Drugs Ther. 2010, 25, 3–12.
Yue, P.; Jin, H.; Xu, S.; Aillaud, M.; Deng, A.C.; Azuma, J.; Kundu, R.K.; Reaven, G.M.; Quertermous, T.; Tsao, P.S. Apelin Decreases Lipolysis via Gq, Gi, and AMPK-Dependent Mechanisms. Endocrinology 2011, 152, 59–68.
Than, A.; Cheng, Y.; Foh, L.-C.; Leow, M.K.-S.; Lim, S.C.; Chuah, Y.J.; Kang, Y.; Chen, P. Apelin inhibits adipogenesis and lipolysis through distinct molecular pathways. Mol. Cell. Endocrinol. 2012, 362, 227–241.
Zhu, S.; Sun, F.; Li, W.; Cao, Y.; Wang, C.; Wang, Y.; Liang, N.; Zhang, R.; Zhang, S.; Wang, H.; et al. Apelin stimulates glucose uptake through the PI3K/Akt pathway and improves insulin resistance in 3T3-L1 adipocytes. Mol. Cell. Biochem. 2011, 353, 305–313.
Attane, C.; Daviaud, D.; Dray, C.; Dusaulcy, R.; Masseboeuf, M.; Prévot, D.; Carpéné, C.; Castan-Laurell, I.; Valet, P. Apelin stimulates glucose uptake but not lipolysis in human adipose tissue ex vivo. J. Mol. Endocrinol. 2010, 46, 21–28.
Than, A.; He, H.L.; Chua, S.H.; Xu, D.; Sun, L.; Leow, M.K.-S.; Chen, P. Apelin Enhances Brown Adipogenesis and Browning of White Adipocytes. J. Biol. Chem. 2015, 290, 14679–14691.
Li, C.; Miao, X.; Wang, S.; Liu, Y.; Sun, J.; Liu, Q.; Cai, L.; Wang, Y. Elabela may regulate SIRT3-mediated inhibition of oxidative stress through Foxo3a deacetylation preventing diabetic-induced myocardial injury. J. Cell. Mol. Med. 2021, 25, 323–332.
Onalan, E.; Doğan, Y.; Onalan, E.; Gozel, N.; Buran, I.; Donder, E. Elabela levels in patients with type 2 diabetes: Can it be a marker for diabetic nephropathy? Afr. Health Sci. 2020, 20, 833–840.
Zhang, H.; Gong, D.; Ni, L.; Shi, L.; Xu, W.; Shi, M.; Chen, J.; Ai, Y.; Zhang, X. Serum Elabela/Toddler Levels Are Associated with Albuminuria in Patients with Type 2 Diabetes. Cell. Physiol. Biochem. 2018, 48, 1347–1354.
Boström, P.; Wu, J.; Jedrychowski, M.P.; Korde, A.; Ye, L.; Lo, J.C.; Rasbach, K.A.; Boström, E.A.; Choi, J.H.; Long, J.Z.; et al. A PGC1-α-dependent myokine that drives brown-fat-like development of white fat and thermogenesis. Nature 2012, 481, 463–468.
Panati, K.; Narala, V.R.; Narasimha, V.R.; Derangula, M.; Tatireddigari, V.R.A.; Yeguvapalli, S. Expression, purification and biological characterisation of recombinant human irisin (12.5 kDa). J. Genet. Eng. Biotechnol. 2018, 16, 459–466.
Moreno-Navarrete, J.M.; Ortega, F.; Serrano, M.; Guerra, E.; Pardo, G.; Tinahones, F.; Ricart, W.; Fernández-Real, J.M. Irisin Is Expressed and Produced by Human Muscle and Adipose Tissue in Association with Obesity and Insulin Resistance. J. Clin. Endocrinol. Metab. 2013, 98, E769–E778.
Kim, H.; Wrann, C.D.; Jedrychowski, M.; Vidoni, S.; Kitase, Y.; Nagano, K.; Zhou, C.; Chou, J.; Parkman, V.-J.A.; Novick, S.J.; et al. Irisin Mediates Effects on Bone and Fat via αV Integrin Receptors. Cell 2018, 175, 1756–1768.e17.
Brenmoehl, J.; Albrecht, E.; Komolka, K.; Schering, L.; Langhammer, M.; Hoeflich, A.; Maak, S. Irisin Is Elevated in Skeletal Muscle and Serum of Mice Immediately after Acute Exercise. Int. J. Biol. Sci. 2014, 10, 338–349.
Norheim, F.; Langleite, T.M.; Hjorth, M.; Holen, T.; Kielland, A.; Stadheim, H.K.; Gulseth, H.L.; Birkeland, K.I.; Jensen, J.; Drevon, C.A. The effects of acute and chronic exercise on PGC-1α, irisin and browning of subcutaneous adipose tissue in humans. FEBS J. 2013, 281, 739–749.
Hofmann, T.; Elbelt, U.; Stengel, A. Irisin as a muscle-derived hormone stimulating thermogenesis—A critical update. Peptides 2014, 54, 89–100.
Li, H.; Zhang, Y.; Wang, F.; Donelan, W.; Zona, M.C.; Li, S.; Reeves, W.; Ding, Y.; Tang, D.; Yang, L. Effects of irisin on the differentiation and browning of human visceral white adipocytes. Am. J. Transl. Res. 2019, 11, 7410–7421.
Zhang, Y.; Li, R.; Meng, Y.; Li, S.; Donelan, W.; Zhao, Y.; Qi, L.; Zhang, M.; Wang, X.; Cui, T.; et al. Irisin Stimulates Browning of White Adipocytes through Mitogen-Activated Protein Kinase p38 MAP Kinase and ERK MAP Kinase Signaling. Diabetes 2014, 63, 514–525.
Zhang, Y.; Xie, C.; Wang, H.; Foss, R.M.; Clare, M.; George, E.V.; Li, S.; Katz, A.; Cheng, H.; Ding, Y.; et al. Irisin exerts dual effects on browning and adipogenesis of human white adipocytes. Am. J. Physiol. Endocrinol. Metab. 2016, 311, E530–E541.
Lee, P.; Linderman, J.D.; Smith, S.; Brychta, R.J.; Wang, J.; Idelson, C.; Perron, R.M.; Werner, C.D.; Phan, G.Q.; Kammula, U.S.; et al. Irisin and FGF21 Are Cold-Induced Endocrine Activators of Brown Fat Function in Humans. Cell Metab. 2014, 19, 302–309.
Huh, J.Y.; Dincer, F.; Mesfum, E.; Mantzoros, C.S. Irisin stimulates muscle growth-related genes and regulates adipocyte differentiation and metabolism in humans. Int. J. Obes. 2014, 38, 1538–1544.
Vaughan, R.A.; Gannon, N.P.; Barberena, M.A.; Garcia-Smith, R.; Bisoffi, M.; Mermier, C.M.; Conn, C.A.; Trujillo, K.A. Characterization of the metabolic effects of irisin on skeletal muscle in vitro. Diabetes Obes. Metab. 2014, 16, 711–718.
Xiong, X.-Q.; Chen, D.; Sun, H.-J.; Ding, L.; Wang, J.-J.; Chen, Q.; Li, Y.-H.; Zhou, Y.-B.; Han, Y.; Zhang, F.; et al. FNDC5 overexpression and irisin ameliorate glucose/lipid metabolic derangements and enhance lipolysis in obesity. Biochim. Biophys. Acta Mol. Basis Dis. 2015, 1852, 1867–1875.
Wang, C.; Wang, L.; Li, W.; Yan, F.; Tian, M.; Wu, C.; Qi, L.; Wang, X.; Song, J.; Hou, X.; et al. Irisin has no effect on lipolysis in 3T3-L1 adipocytes or fatty acid metabolism in HepG2 hepatocytes. Endocrine 2014, 49, 90–96.
Ma, E.B.; Sahar, N.E.; Jeong, M.; Huh, J.Y. Irisin Exerts Inhibitory Effect on Adipogenesis through Regulation of Wnt Signaling. Front. Physiol. 2019, 10, 1085.
Gao, S.; Li, F.; Li, H.; Huang, Y.; Liu, Y.; Chen, Y. Effects and Molecular Mechanism of GST-Irisin on Lipolysis and Autocrine Function in 3T3-L1 Adipocytes. PLoS ONE 2016, 11, e0147480.
Tang, H.; Yu, R.; Liu, S.; Huwatibieke, B.; Li, Z.; Zhang, W. Irisin Inhibits Hepatic Cholesterol Synthesis via AMPK-SREBP2 Signaling. EBioMedicine 2016, 6, 139–148.
Tekin, S.; Erden, Y.; Ozyalin, F.; Cigremis, Y.; Colak, C.; Sandal, S. The effects of intracerebroventricular infusion of irisin on feeding behaviour in rats. Neurosci. Lett. 2017, 645, 25–32.
Xin, C.; Liu, J.; Zhang, J.; Zhu, D.; Wang, H.; Xiong, L.; Lee, Y.; Ye, J.; Lian, K.; Xu, C.; et al. Irisin improves fatty acid oxidation and glucose utilization in type 2 diabetes by regulating the AMPK signaling pathway. Int. J. Obes. 2016, 40, 443–451.
Raschke, S.; Elsen, M.; Gassenhuber, H.; Sommerfeld, M.; Schwahn, U.; Brockmann, B.; Jung, R.; Wisløff, U.; Tjønna, A.E.; Raastad, T.; et al. Evidence against a Beneficial Effect of Irisin in Humans. PLoS ONE 2013, 8, e73680.
Kotani, M.; Detheux, M.; Vandenbogaerde, A.; Communi, D.; Vanderwinden, J.-M.; Le Poul, E.; Brézillon, S.; Tyldesley, R.; Suarez-Huerta, N.; Vandeput, F.; et al. The Metastasis Suppressor Gene KiSS-1 Encodes Kisspeptins, the Natural Ligands of the Orphan G Protein-coupled Receptor GPR54. J. Biol. Chem. 2001, 276, 34631–34636.
Michelle, L. Gottsch et al From KISS1 to Kisspeptins: An historical Perspective and Suggested Nomenclature. Peptides 2009, 30, 4–9.
Trevisan, C.M.; Montagna, E.; De Oliveira, R.; Christofolini, D.M.; Barbosa, C.P.; Crandall, K.A.; Bianco, B. Kisspeptin/GPR54 System: What Do We Know about Its Role in Human Reproduction? Cell. Physiol. Biochem. 2018, 49, 1259–1276.
Herbison, A.E.; De Tassigny, X.D.; Doran, J.; Colledge, W.H. Distribution and Postnatal Development of Gpr54 Gene Expression in Mouse Brain and Gonadotropin-Releasing Hormone Neurons. Endocrinology 2010, 151, 312–321.
Kauffman, A.S.; Park, J.H.; McPhie-Lalmansingh, A.A.; Gottsch, M.L.; Bodo, C.; Hohmann, J.G.; Pavlova, M.N.; Rohde, A.D.; Clifton, D.K.; Steiner, R.A.; et al. The Kisspeptin Receptor GPR54 Is Required for Sexual Differentiation of the Brain and Behavior. J. Neurosci. 2007, 27, 8826–8835.
Dudek, M.; Kołodziejski, P.; Pruszyńska-Oszmałek, E.; Sassek, M.; Ziarniak, K.; Nowak, K.; Sliwowska, J. Effects of high-fat diet-induced obesity and diabetes on Kiss1 and GPR54 expression in the hypothalamic–pituitary–gonadal (HPG) axis and peripheral organs (fat, pancreas and liver) in male rats. Neuropeptides 2016, 56, 41–49.
Wang, T.; Cui, X.; Xie, L.; Xing, R.; You, P.; Zhao, Y.; Yang, Y.; Xu, Y.; Zeng, L.; Chen, H.; et al. Kisspeptin Receptor GPR54 Promotes Adipocyte Differentiation and Fat Accumulation in Mice. Front. Physiol. 2018, 9, 1–13.
Pruszyńska-Oszmałek, E.; Kołodziejski, P.A.; Sassek, M.; Sliwowska, J.H. Kisspeptin-10 inhibits proliferation and regulates lipolysis and lipogenesis processes in 3T3-L1 cells and isolated rat adipocytes. Endocrinology 2017, 56, 54–64.
Song, W.J.; Mondal, P.; Wolfe, A.; Alonso, L.C.; Stamateris, R.; Ong, B.W.; Lim, O.C.; Yang, K.S.; Radovick, S.; Novaira, H.J.; et al. Glucagon regulates hepatic kisspeptin1 to impair insulin secretion. Cell Metab. 2014, 19, 667–681.
Fontana, R.; Della Torre, S. The Deep Correlation between Energy Metabolism and Reproduction: A View on the Effects of Nutrition for Women Fertility. Nutrients 2016, 8, 87.
Orlando, G.; Leone, S.; Ferrante, C.; Chiavaroli, A.; Mollica, A.; Stefanucci, A.; Macedonio, G.; Dimmito, M.P.; Leporini, L.; Menghini, L.; et al. Effects of Kisspeptin-10 on Hypothalamic Neuropeptides and Neurotransmitters Involved in Appetite Control. Molecules 2018, 23, 3071.
Brown, R.; Imran, S.; Ur, E.; Wilkinson, M. KiSS-1 mRNA in adipose tissue is regulated by sex hormones and food intake. Mol. Cell. Endocrinol. 2008, 281, 64–72.
Wahab, F.; Riaz, T.; Shahab, M. Study on the Effect of Peripheral Kisspeptin Administration on Basal and Glucose-induced Insulin Secretion under Fed and Fasting Conditions in the Adult Male Rhesus Monkey (Macaca mulatta). Horm. Metab. Res. 2010, 43, 37–42.
Tolson, K.P.; Marooki, N.; De Bond, J.P.; Walenta, E.; Stephens, S.B.; Liaw, R.B.; Savur, R.; Wolfe, A.; Oh, D.Y.; Smith, J.T.; et al. Conditional knockout of kisspeptin signaling in brown adipose tissue increases metabolic rate and body temperature and lowers body weight. FASEB J. 2020, 34, 107–121.
Halvorson, C.; De Bond, J.; Maloney, S.; Smith, J. Thermoneutral conditions correct the obese phenotype in female, but not male, Kiss1r knockout mice. J. Therm. Biol. 2020, 90, 102592.
Dong, T.S.; Vu, J.P.; Oh, S.; Sanford, D.; Pisegna, J.R.; Germano, P. Intraperitoneal Treatment of Kisspeptin Suppresses Appetite and Energy Expenditure and Alters Gastrointestinal Hormones in Mice. Dig. Dis. Sci. 2019, 65, 2254–2263.
Stengel, A.; Wang, L.; Goebel-Stengel, M.; Taché, Y. Centrally injected kisspeptin reduces food intake by increasing meal intervals in mice. NeuroReport 2011, 22, 253–257.
Sahin, Z.; Ozcan, M.; Ozkaya, A.; Canpolat, S.; Kutlu, S.; Kelestimur, H. Percentages of serum, liver and adipose tissue fatty acids and body weight are affected in female rats by long-term Central kisspeptin treatments. Arch. Physiol. Biochem. 2020, 1–9.
Zhai, L.; Zhao, J.; Zhu, Y.; Liu, Q.; Niu, W.; Liu, C.; Wang, Y. Downregulation of leptin receptor and kisspeptin/GPR54 in the murine hypothalamus contributes to male hypogonadism caused by high-fat diet-induced obesity. Endocrine 2018, 62, 195–206.
Zhou, Q.; Chen, H.; Yang, S.; Li, Y.; Wang, B.; Chen, Y.; Wu, X. High-fat diet decreases the expression of Kiss1 mRNA and kisspeptin in the ovary, and increases ovulatory dysfunction in postpubertal female rats. Reprod. Biol. Endocrinol. 2014, 12, 127.
Kołodziejski, P.A.; Pruszyńska-Oszmałek, E.; Korek, E.; Sassek, M.; Szczepankiewicz, D.; Kaczmarek, P.; Nogowski, L.; Maćkowiak, P.; Nowak, K.W.; Krauss, H.; et al. Serum Levels of Spexin and Kisspeptin Negatively Correlate with Obesity and Insulin Resistance in Women. Physiol. Res. 2018, 67, 45–56.
Lee, C.; Zeng, J.; Drew, B.G.; Sallam, T.; Martin-Montalvo, A.; Wan, J.; Kim, S.-J.; Mehta, H.; Hevener, A.L.; De Cabo, R.; et al. The Mitochondrial-Derived Peptide MOTS-c Promotes Metabolic Homeostasis and Reduces Obesity and Insulin Resistance. Cell Metab. 2015, 21, 443–454.
Kim, S.-J.; Mehta, H.H.; Wan, J.; Kuehnemann, C.; Chen, J.; Hu, J.-F.; Hoffman, A.R.; Cohen, P. Mitochondrial peptides modulate mitochondrial function during cellular senescence. Aging 2018, 10, 1239–1256.
Lu, H.; Tang, S.; Xue, C.; Liu, Y.; Wang, J.; Zhang, W.; Luo, W.; Chen, J. Mitochondrial-Derived Peptide MOTS-c Increases Adipose Thermogenic Activation to Promote Cold Adaptation. Int. J. Mol. Sci. 2019, 20, 2456.
Lu, H.; Wei, M.; Zhai, Y.; Li, Q.; Ye, Z.; Wang, L.; Luo, W.; Chen, J.; Lu, Z. MOTS-c peptide regulates adipose homeostasis to prevent ovariectomy-induced metabolic dysfunction. J. Mol. Med. 2019, 97, 473–485.
Li, Q.; Lu, H.; Hu, G.; Ye, Z.; Zhai, D.; Yan, Z.; Wang, L.; Xiang, A.; Lu, Z. Earlier changes in mice after D-galactose treatment were improved by mitochondria derived small peptide MOTS-c. Biochem. Biophys. Res. Commun. 2019, 513, 439–445.
Ramanjaneya, M.; Jerobin, J.; Bettahi, I.; Bensila, M.; Aye, M.; Siveen, K.S.; Sathyapalan, T.; Skarulis, M.; Abou-Samra, A.; Atkin, S.L. Lipids and insulin regulate mitochondrial-derived peptide (MOTS-c) in PCOS and healthy subjects. Clin. Endocrinol. 2019, 91, 278–287.
Fujii, R.; Yoshida, H.; Fukusumi, S.; Habata, Y.; Hosoya, M.; Kawamata, Y.; Yano, T.; Hinuma, S.; Kitada, C.; Asami, T.; et al. Identification of a Neuropeptide Modified with Bromine as an Endogenous Ligand for GPR7. J. Biol. Chem. 2002, 277, 34010–34016.
Brezillon, S.; Lannoy, V.; Franssen, J.-D.; Le Poul, E.; Dupriez, V.; Lucchetti, J.; Detheux, M.; Parmentier, M. Identification of Natural Ligands for the Orphan G Protein-coupled Receptors GPR7 and GPR8. J. Biol. Chem. 2003, 278, 776–783.
Tanaka, H.; Yoshida, T.; Miyamoto, N.; Motoike, T.; Kurosu, H.; Shibata, K.; Yamanaka, A.; Williams, S.C.; Richardson, J.A.; Tsujino, N.; et al. Characterization of a family of endogenous neuropeptide ligands for the G protein-coupled receptors GPR7 and GPR8. Proc. Natl. Acad. Sci. USA 2003, 100, 6251–6256.
Bu, G.; Lin, D.; Cui, L.; Huang, L.; Lv, C.; Huang, S.; Wan, Y.; Fang, C.; Li, J.; Wang, Y. Characterization of Neuropeptide B (NPB), Neuropeptide W (NPW), and Their Receptors in Chickens: Evidence for NPW Being a Novel Inhibitor of Pituitary GH and Prolactin Secretion. Endocrinology 2016, 157, 3562–3576.
Takenoya, F.; Kageyama, H.; Shiba, K.; Date, Y.; Nakazato, M.; Shioda, S. Neuropeptide W: A key player in the homeostatic regulation of feeding and energy metabolism? Ann. N. Y. Acad. Sci. 2010, 1200, 162–169.
Shimomura, Y.; Harada, M.; Goto, M.; Sugo, T.; Matsumoto, Y.; Abe, M.; Watanabe, T.; Asami, T.; Kitada, C.; Mori, M.; et al. Identification of Neuropeptide W as the Endogenous Ligand for Orphan G-protein-coupled Receptors GPR7 and GPR8. J. Biol. Chem. 2002, 277, 35826–35832.
Takenoya, F.; Kageyama, H.; Hirako, S.; Ota, E.; Wada, N.; Ryushi, T.; Shioda, S. Neuropeptide W. Front. Endocrinol. 2012, 3, 171.
Kitamura, Y.; Tanaka, H.; Motoike, T.; Ishii, M.; Williams, S.C.; Yanagisawa, M.; Sakurai, T. Distribution of neuropeptide W immunoreactivity and mRNA in adult rat brain. Brain Res. 2006, 1093, 123–134.
Fang, R.; Su, J.; Zheng, L.; Jin, M.; Hou, Y.; Ma, Z.; Guo, T.; Zhu, S.; Ma, X.; Ahmed, E.; et al. Cloning and distribution of neuropeptide W and its receptors in pigs. Res. Vet. Sci. 2015, 101, 106–116.
Singh, G.; Davenport, A.P. Neuropeptide B and W: Neurotransmitters in an emerging G-protein-coupled receptor system. Br. J. Pharmacol. 2006, 148, 1033–1041.
Price, C.J.; Samson, W.K.; Ferguson, A.V. Neuropeptide W has cell phenotype-specific effects on the excitability of different subpopulations of paraventricular nucleus neurones. J. Neuroendocr. 2009, 21, 850–857.
Mazzocchi, G.; Rebuffat, P.; Ziolkowska, A.; Rossi, G.P.; Malendowicz, L.K.; Nussdorfer, G.G. G Protein Receptors 7 and 8 Are Expressed in Human Adrenocortical Cells, and Their Endogenous Ligands Neuropeptides B and W Enhance Cortisol Secretion by Activating Adenylate Cyclase- and Phospholipase C-Dependent Signaling Cascades. J. Clin. Endocrinol. Metab. 2005, 90, 3466–3471.
Billert, M.; Sassek, M.; Wojciechowicz, T.; Jasaszwili, M.; Strowski, M.Z.; Nowak, K.W.; Skrzypski, M. Neuropeptide B stimulates insulin secretion and expression but not proliferation in rat insulin-producing INS-1E cells. Mol. Med. Rep. 2019, 20, 2030–2038.
Wojciechowicz, T.; Billert, M.; Dhandapani, P.; Szczepankiewicz, D.; Wasielewski, O.; Strowski, M.Z.; Nowak, K.W.; Skrzypski, M. Neuropeptide B promotes proliferation and differentiation of rat brown primary preadipocytes. FEBS Open Bio 2021, 11, 1153–1164.
Dun, S.L.; Brailoiu, G.C.; Mizuo, K.; Yang, J.; Chang, J.K.; Dun, N.J. Neuropeptide B immunoreactivity in the central nervous system of the rat. Brain Res. 2005, 1045, 157–163.
Dvorakova, M.C. Distribution and Function of Neuropeptides W/B Signaling System. Front. Physiol. 2018, 9, 981.
Hochol, A.; Belloni, A.S.; Rucinski, M.; Ziolkowska, A.; Di Liddo, R.; Nussdorfer, G.G.; Malendowicz, L.K. Expression of neuropeptides B and W and their receptors in endocrine glands of the rat. Int. J. Mol. Med. 2006, 18, 1101–1106.
Pandey, S.; Tuma, Z.; Peroni, E.; Monasson, O.; Papini, A.M.; Dvorakova, M.C. Identification of NPB, NPW and Their Receptor in the Rat Heart. Int. J. Mol. Sci. 2020, 21, 7827.
Kelly, M.A.; Beuckmann, C.T.; Williams, S.C.; Sinton, C.M.; Motoike, T.; Richardson, J.A.; Hammer, R.E.; Garry, M.G.; Yanagisawa, M. Neuropeptide B-deficient mice demonstrate hyperalgesia in response to inflammatory pain. Proc. Natl. Acad. Sci. USA 2005, 102, 9942–9947.
Samson, W.K.; Baker, J.R.; Samson, H.W.; Taylor, M.M. Central Neuropeptide B Administration Activates Stress Hormone Secretion and Stimulates Feeding in Male Rats. J. Neuroendocr. 2004, 16, 842–849.
Hochol, A.; Albertin, G.; Nussdorfer, G.G.; Spinazzi, R.; Ziolkowska, A.; Rucinski, M.; Malendowicz, L.K. Effects of neuropeptides B and W on the secretion and growth of rat adrenocortical cells. Int. J. Mol. Med. 2004, 14, 843–847.
Yang, S.; Ma, Z.; Suo, C.; Cheng, L.; Su, J.; Lei, Z.; Zhihai, L. Cloning and mRNA expression of NPB and its effect on hormone secretion of the reproductive cells in the pig. Gen. Comp. Endocrinol. 2018, 261, 97–103.
Dun, S.L.; Brailoiu, G.; Yang, J.; Chang, J.K.; Dun, N.J. Neuropeptide W-immunoreactivity in the hypothalamus and pituitary of the rat. Neurosci. Lett. 2003, 349, 71–74.
Takenoya, F.; Yagi, M.; Kageyama, H.; Shiba, K.; Endo, K.; Nonaka, N.; Date, Y.; Nakazato, M.; Shioda, S. Distribution of neuropeptide W in the rat brain. Neuropeptides 2010, 44, 99–106.
Skrzypski, M.; Pruszyńska-Oszmałek, E.; Rucinski, M.; Szczepankiewicz, D.; Sassek, M.; Wojciechowicz, T.; Kaczmarek, P.; Kołodziejski, P.A.; Strowski, M.Z.; Malendowicz, L.K.; et al. Neuropeptide B and W regulate leptin and resistin secretion, and stimulate lipolysis in isolated rat adipocytes. Regul. Pept. 2012, 176, 51–56.
Rucinski, M.; Nowak, K.W.; Chmielewska, J.; Ziolkowska, A.; Malendowicz, L.K. Neuropeptide W exerts a potent suppressive effect on blood leptin and insulin concentrations in the rat. Int. J. Mol. Med. 2007, 19, 401–405.
Mondal, M.S.; Yamaguchi, H.; Date, Y.; Shimbara, T.; Toshinai, K.; Shimomura, Y.; Mori, M.; Nakazato, M. A Role for Neuropeptide W in the Regulation of Feeding Behavior. Endocrinology 2003, 144, 4729–4733.
Watanabe, N.; Wada, M.; Irukayama-Tomobe, Y.; Ogata, Y.; Tsujino, N.; Suzuki, M.; Furutani, N.; Sakurai, T.; Yamamoto, M. A Single Nucleotide Polymorphism of the Neuropeptide B/W Receptor-1 Gene Influences the Evaluation of Facial Expressions. PLoS ONE 2012, 7, e35390.
Ishii, M.; Fei, H.; Friedman, J.M. Targeted disruption of GPR7, the endogenous receptor for neuropeptides B and W, leads to metabolic defects and adult-onset obesity. Proc. Natl. Acad. Sci. USA 2003, 100, 10540–10545.
Jamaluddin, S.; Weakley, S.M.; Yao, Q.; Chen, C. Resistin: Functional roles and therapeutic considerations for cardiovascular disease. Br. J. Pharmacol. 2012, 165, 622–632.
Enriori, P.J.; Evans, A.E.; Sinnayah, P.; Cowley, M.A. Leptin Resistance and Obesity. Obesity 2006, 14, 254S–258S.
Yosten, G.L.C.; Lyu, R.-M.; Hsueh, A.J.; Avsian-Kretchmer, O.; Chang, J.-K.; Tullock, C.W.; Dun, S.L.; Dun, N.; Samson, W.K. A Novel Reproductive Peptide, Phoenixin. J. Neuroendocr. 2012, 25, 206–215.
Cowan, A.; Lyu, R.-M.; Chen, Y.-H.; Dun, S.L.; Chang, J.-K.; Dun, N.J. Phoenixin: A candidate pruritogen in the mouse. Neuroscience 2015, 310, 541–548.
Stein, L.M.; Haddock, C.J.; Samson, W.K.; Kolar, G.R.; Yosten, G.L. The phoenixins: From discovery of the hormone to identification of the receptor and potential physiologic actions. Peptides 2018, 106, 45–48.
McIlwraith, E.K.; Belsham, D.D. Phoenixin: Uncovering its receptor, signaling and functions. Acta Pharmacol. Sin. 2018, 39, 774–778.
Stein, L.M.; Tullock, C.W.; Mathews, S.K.; Garcia-Galiano, D.; Elias, C.F.; Samson, W.K.; Yosten, G.L.C. Hypothalamic action of phoenixin to control reproductive hormone secretion in females: Importance of the orphan G protein-coupled receptor Gpr173. Am. J. Physiol. Integr. Comp. Physiol. 2016, 311, R489–R496.
Yosten, G.L.C.; Kolar, G.R.; Redlinger, L.J.; Samson, W.K. Evidence for an interaction between proinsulin C-peptide and GPR146. J. Endocrinol. 2013, 218, B1–B8.
Treen, A.K.; Luo, V.; Belsham, D.D. Phoenixin Activates Immortalized GnRH and Kisspeptin Neurons through the Novel Receptor GPR173. Mol. Endocrinol. 2016, 30, 872–888.
Nguyen, X.P.; Nakamura, T.; Osuka, S.; Bayasula, B.; Nakanishi, N.; Kasahara, Y.; Muraoka, A.; Hayashi, S.; Nagai, T.; Murase, T.; et al. Effect of the neuropeptide phoenixin and its receptor GPR173 during folliculogenesis. Reproduction 2019, 158, 25–34.
Ullah, K.; Rahman, T.U.; Wu, D.-D.; Lin, X.-H.; Liu, Y.; Guo, X.-Y.; Leung, P.C.; Zhang, R.-J.; Huang, H.-F.; Sheng, J.-Z. Phoenixin-14 concentrations are increased in association with luteinizing hormone and nesfatin-1 concentrations in women with polycystic ovary syndrome. Clin. Chim. Acta 2017, 471, 243–247.
Yuruyen, M.; Gultekin, G.; Batun, G.C.; Yavuzer, H.; Akcan, F.E.; Doventas, A.; Emul, M. Does plasma phoenixin level associate with cognition? Comparison between subjective memory complaint, mild cognitive impairment, and mild Alzheimer’s disease. Int. Psychogeriatr. 2017, 29, 1543–1550.
Billert, M.; Wojciechowicz, T.; Jasaszwili, M.; Szczepankiewicz, D.; Waśko, J.; Kaźmierczak, S.; Strowski, M.Z.; Nowak, K.W.; Skrzypski, M. Phoenixin-14 stimulates differentiation of 3T3-L1 preadipocytes via cAMP/Epac-dependent mechanism. Biochim. Biophys. Acta Mol. Cell Biol. Lipids 2018, 1863, 1449–1457.
Kalamon, N.; Błaszczyk, K.; Szlaga, A.; Billert, M.; Skrzypski, M.; Pawlicki, P.; Górowska–Wójtowicz, E.; Kotula–Balak, M.; Błasiak, A.; Rak, A. Levels of the neuropeptide phoenixin-14 and its receptor GRP173 in the hypothalamus, ovary and periovarian adipose tissue in rat model of polycystic ovary syndrome. Biochem. Biophys. Res. Commun. 2020, 528, 628–635.
Delitala, A.P.; Capobianco, G.; Delitala, G.; Cherchi, P.L.; Dessole, S. Polycystic ovary syndrome, adipose tissue and metabolic syndrome. Arch. Gynecol. Obstet. 2017, 296, 405–419.
Mirabeau, O.; Perlas, E.; Severini, C.; Audero, E.; Gascuel, O.; Possenti, R.; Birney, E.; Rosenthal, N.; Gross, C. Identification of novel peptide hormones in the human proteome by hidden Markov model screening. Genome Res. 2007, 17, 320–327.
Kim, D.-K.; Yun, S.; Son, G.H.; Hwang, J.-I.; Park, C.R.; Kim, J.I.; Kim, K.; Vaudry, H.; Seong, J.Y. Coevolution of the Spexin/Galanin/Kisspeptin Family: Spexin Activates Galanin Receptor Type II and III. Endocrinology 2014, 155, 1864–1873.
Porzionato, A.; Rucinski, M.; Macchi, V.; Stecco, C.; Malendowicz, L.K.; De Caro, R. Spexin Expression in Normal Rat Tissues. J. Histochem. Cytochem. 2010, 58, 825–837.
Kołodziejski, P.; Pruszyńska-Oszmałek, E.; Hejdysz, M.; Sassek, M.; Leciejewska, N.; Ziarniak, K.; Bień, J.; Ślósarz, P.; Kubiś, M.; Kaczmarek, S. Effects of Fasting on the Spexin System in Broiler Chickens. Animals 2021, 11, 518.
Kolodziejski, P.A.; Pruszynska-Oszmalek, E.; Micker, M.; Skrzypski, M.; Wojciechowicz, T.; Szwarckopf, P.; Skieresz-Szewczyk, K.; Nowak, K.W.; Strowski, M.Z. Spexin: A novel regulator of adipogenesis and fat tissue metabolism. Biochim. Biophys. Acta Mol. Cell Biol. Lipids 2018, 1863, 1228–1236.
Zheng, B.; Li, S.; Liu, Y.; Li, Y.; Chen, H.; Tang, H.; Liu, X.; Lin, H.; Zhang, Y.; Cheng, C.H.K. Spexin Suppress Food Intake in Zebrafish: Evidence from Gene Knockout Study. Sci. Rep. 2017, 7, 14643.
Gu, L.; Ma, Y.; Gu, M.; Zhang, Y.; Yan, S.; Li, N.; Wang, Y.; Ding, X.; Yin, J.; Fan, N.; et al. Spexin peptide is expressed in human endocrine and epithelial tissues and reduced after glucose load in type 2 diabetes. Peptides 2015, 71, 232–239.
Lv, S.-Y.; Zhou, Y.-C.; Zhang, X.-M.; Chen, W.-D.; Wang, Y.-D. Emerging Roles of NPQ/Spexin in Physiology and Pathology. Front. Pharmacol. 2019, 10, 457.
Wong, M.K.H.; Sze, K.H.; Chen, T.; Cho, C.K.; Law, H.C.H.; Chu, I.K.; Wong, A.O.L. Goldfish spexin: Solution structure and novel function as a satiety factor in feeding control. Am. J. Physiol. Endocrinol. Metab. 2013, 305, E348–E366.
Walewski, J.L.; Ge, F.; Iv, H.L.; Levin, N.; Schwartz, G.J.; Vasselli, J.R.; Pomp, A.; Dakin, G.; Berk, P.D. Spexin is a novel human peptide that reduces adipocyte uptake of long chain fatty acids and causes weight loss in rodents with diet-induced obesity. Obesity 2014, 22, 1643–1652.
Karaca, A.; Bakar-Ates, F.; Ersoz-Gulcelik, N. Decreased Spexin Levels in Patients with Type 1 and Type 2 Diabetes. Med. Princ. Pract. 2018, 27, 549–554.
Behrooz, M.; Vaghef-Mehrabany, E.; Ostadrahimi, A. Different spexin level in obese vs normal weight children and its relationship with obesity related risk factors. Nutr. Metab. Cardiovasc. Dis. 2020, 30, 674–682.
Behrooz, M.; Vaghef-Mehrabany, E.; Moludi, J.; Ostadrahimi, A. Are spexin levels associated with metabolic syndrome, dietary intakes and body composition in children? Diabetes Res. Clin. Pract. 2021, 172, 108634.
Pruszynska-Oszmalek, E.; Sassek, M.; Szczepankiewicz, D.; Nowak, K.W.; Kolodziejski, P.A. Short-term administration of spexin in rats reduces obesity by affecting lipolysis and lipogenesis: An in vivo and in vitro study. Gen. Comp. Endocrinol. 2020, 299, 113615.
Ge, J.F.; Walewski, J.L.; Anglade, D.; Berk, P.D. Regulation of Hepatocellular Fatty Acid Uptake in Mouse Models of Fatty Liver Disease with and without Functional Leptin Signaling: Roles of NfKB and SREBP-1C and the Effects of Spexin. Semin. Liver Dis. 2016, 36, 360–372.
Gambaro, S.E.; Zubiría, M.G.; Giordano, A.P.; Portales, A.E.; Alzamendi, A.; Rumbo, M.; Giovambattista, A. Spexin improves adipose tissue inflammation and macrophage recruitment in obese mice. Biochim. Biophys. Acta Mol. Cell Biol. Lipids 2020, 1865, 158700.
Said, M.A.; Nafeh, N.Y.; Abdallah, H.A. Spexin alleviates hypertension, hyperuricaemia, dyslipidemia and insulin resistance in high fructose diet induced metabolic syndrome in rats via enhancing PPAR-ɣ and AMPK and inhibiting IL-6 and TNF-α. Arch. Physiol. Biochem. 2021, 1–6.