{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,12]],"date-time":"2026-02-12T12:09:51Z","timestamp":1770898191347,"version":"3.50.1"},"reference-count":119,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2020,2,17]],"date-time":"2020-02-17T00:00:00Z","timestamp":1581897600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001807","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de S\u00e3o Paulo","doi-asserted-by":"publisher","award":["2016\/04000-3; 2004\/04933-2; 2015\/20657-0"],"award-info":[{"award-number":["2016\/04000-3; 2004\/04933-2; 2015\/20657-0"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["445363\/2014-2; 400944\/2014-6; 400944\/2014-6; 302809\/2016-3"],"award-info":[{"award-number":["445363\/2014-2; 400944\/2014-6; 400944\/2014-6; 302809\/2016-3"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>Thimet oligopeptidase (EC 3.4.24.15; EP24.15; THOP1) is a potential therapeutic target, as it plays key biological functions in processing biologically functional peptides. The structural conformation of THOP1 provides a unique restriction regarding substrate size, in that it only hydrolyzes peptides (optimally, those ranging from eight to 12 amino acids) and not proteins. The proteasome activity of hydrolyzing proteins releases a large number of intracellular peptides, providing THOP1 substrates within cells. The present study aimed to investigate the possible function of THOP1 in the development of diet-induced obesity (DIO) and insulin resistance by utilizing a murine model of hyperlipidic DIO with both C57BL6 wild-type (WT) and THOP1 null (THOP1\u2212\/\u2212) mice. After 24 weeks of being fed a hyperlipidic diet (HD), THOP1\u2212\/\u2212 and WT mice ingested similar chow and calories; however, the THOP1\u2212\/\u2212 mice gained 75% less body weight and showed neither insulin resistance nor non-alcoholic fatty liver steatosis when compared to WT mice. THOP1\u2212\/\u2212 mice had increased adrenergic-stimulated adipose tissue lipolysis as well as a balanced level of expression of genes and microRNAs associated with energy metabolism, adipogenesis, or inflammation. Altogether, these differences converge to a healthy phenotype of THOP1\u2212\/\u2212 fed a HD. The molecular mechanism that links THOP1 to energy metabolism is suggested herein to involve intracellular peptides, of which the relative levels were identified to change in the adipose tissue of WT and THOP1\u2212\/\u2212 mice. Intracellular peptides were observed by molecular modeling to interact with both pre-miR-143 and pre-miR-222, suggesting a possible novel regulatory mechanism for gene expression. Therefore, we successfully demonstrated the previously anticipated relevance of THOP1 in energy metabolism regulation. It was suggested that intracellular peptides were responsible for mediating the phenotypic differences that are described herein by a yet unknown mechanism of action.<\/jats:p>","DOI":"10.3390\/biom10020321","type":"journal-article","created":{"date-parts":[[2020,2,21]],"date-time":"2020-02-21T10:49:16Z","timestamp":1582282156000},"page":"321","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":17,"title":["The Relevance of Thimet Oligopeptidase in the Regulation of Energy Metabolism and Diet-Induced Obesity"],"prefix":"10.3390","volume":"10","author":[{"given":"Mayara C. F.","family":"Gewehr","sequence":"first","affiliation":[{"name":"Department of Pharmacology, Biomedical Sciences Institute, University of S\u00e3o Paulo, 05508-900 S\u00e3o Paulo, SP, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3099-7070","authenticated-orcid":false,"given":"Alexandre A. 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C.","family":"Santos","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, Biomedical Sciences Institute, University of S\u00e3o Paulo, 05508-900 S\u00e3o Paulo, SP, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7506-6667","authenticated-orcid":false,"given":"Luana A.","family":"Biondo","sequence":"additional","affiliation":[{"name":"Department of Cell Biology and Development, Biomedical Sciences Institute, University of S\u00e3o Paulo, 05508-900 S\u00e3o Paulo, SP, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"F\u00e1bio C.","family":"Gozzo","sequence":"additional","affiliation":[{"name":"Institute of Chemistry, State University of Campinas, 13083-862 Campinas, SP, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Amanda M.","family":"Cordibello","sequence":"additional","affiliation":[{"name":"Institute of Chemistry, State University of Campinas, 13083-862 Campinas, SP, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rosangela A. S.","family":"Eichler","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, Biomedical Sciences Institute, University of S\u00e3o Paulo, 05508-900 S\u00e3o Paulo, SP, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Patr\u00edcia","family":"Reckziegel","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, Federal University of S\u00e3o Paulo, 04023-062 S\u00e3o Paulo, SP, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ren\u00e9e N. O.","family":"Da Silva","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, Biomedical Sciences Institute, University of S\u00e3o Paulo, 05508-900 S\u00e3o Paulo, SP, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2258-9349","authenticated-orcid":false,"given":"Nilton B.","family":"Dos Santos","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, Biomedical Sciences Institute, University of S\u00e3o Paulo, 05508-900 S\u00e3o Paulo, SP, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Niels O. S.","family":"Camara","sequence":"additional","affiliation":[{"name":"Department of Immunology, Biomedical Sciences Institute, University of S\u00e3o Paulo, 05508-900 S\u00e3o Paulo, SP, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Angela","family":"Castoldi","sequence":"additional","affiliation":[{"name":"Department of Immunology, Biomedical Sciences Institute, University of S\u00e3o Paulo, 05508-900 S\u00e3o Paulo, SP, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Maria L. M.","family":"Barreto-Chaves","sequence":"additional","affiliation":[{"name":"Department of Anatomy, Biomedical Sciences Institute, University of S\u00e3o Paulo, 05508-900 S\u00e3o Paulo, SP, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Camila S.","family":"Dale","sequence":"additional","affiliation":[{"name":"Department of Anatomy, Biomedical Sciences Institute, University of S\u00e3o Paulo, 05508-900 S\u00e3o Paulo, SP, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nathalia","family":"Senger","sequence":"additional","affiliation":[{"name":"Department of Anatomy, Biomedical Sciences Institute, University of S\u00e3o Paulo, 05508-900 S\u00e3o Paulo, SP, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Joanna D. C. 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Rev. Biochem."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/S0161-5890(02)00098-6","article-title":"The importance of the proteasome and subsequent proteolytic steps in the generation of antigenic peptides","volume":"39","author":"Goldberg","year":"2002","journal-title":"Mol. Immunol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"945","DOI":"10.1086\/285643","article-title":"Evolutionary Genetics of the Major Histocompatibility Complex","volume":"143","author":"Hedrick","year":"1994","journal-title":"Am. Nat."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"2160","DOI":"10.1002\/eji.1830230917","article-title":"The evolutionary origin of the major histocompatibility complex: Polymorphism of class II alpha chain genes in the cartilaginous fish","volume":"23","author":"Kasahara","year":"1993","journal-title":"Eur. J. Immunol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1007\/BF00216798","article-title":"Evolutionary relationships of the classes of major histocompatibility complex genes","volume":"37","author":"Hughes","year":"1993","journal-title":"Immunogenetics"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1437","DOI":"10.1016\/S0022-2836(02)01470-5","article-title":"A comprehensive view on proteasomal sequences: Implications for the evolution of the proteasome","volume":"326","author":"Gille","year":"2003","journal-title":"J. Mol. Biol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1016\/0006-3002(57)90184-1","article-title":"Intracellular peptides of Pseudomonas hydrophila","volume":"24","author":"Connell","year":"1957","journal-title":"Biochim. Biophys Acta"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1016\/S0021-9258(18)70441-9","article-title":"Synthesis of intracellular peptides in Torula utilis","volume":"231","author":"Mc","year":"1958","journal-title":"J. Biol. Chem."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"8547","DOI":"10.1074\/jbc.M212030200","article-title":"Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme","volume":"278","author":"Rioli","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1152\/physiolgenomics.00145.2004","article-title":"ACE gene titration in mice uncovers a new mechanism for ACE on the control of body weight","volume":"20","author":"Heimann","year":"2005","journal-title":"Physiol. Genom."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1583","DOI":"10.1021\/pr100952f","article-title":"Peptidomic analysis of human cell lines","volume":"10","author":"Gelman","year":"2011","journal-title":"J. Proteome Res."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"14105","DOI":"10.1074\/jbc.M807916200","article-title":"Analysis of intracellular substrates and products of thimet oligopeptidase in human embryonic kidney 293 cells","volume":"284","author":"Berti","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"7104","DOI":"10.1002\/jcp.27465","article-title":"Identification of intracellular peptides associated with thermogenesis in human brown adipocytes","volume":"234","author":"Li","year":"2019","journal-title":"J. Cell Physiol"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/j.jprot.2016.05.025","article-title":"Peptidomic analysis of the anterior temporal lobe and corpus callosum from schizophrenia patients","volume":"151","author":"Ferro","year":"2017","journal-title":"J. Proteom."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"2408","DOI":"10.1016\/j.bbapap.2013.01.043","article-title":"Analysis of peptides secreted from cultured mouse brain tissue","volume":"1834","author":"Gelman","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1111\/j.1471-4159.2010.06653.x","article-title":"Hemopressins and other hemoglobin-derived peptides in mouse brain: Comparison between brain, blood, and heart peptidome and regulation in Cpefat\/fat mice","volume":"113","author":"Gelman","year":"2010","journal-title":"J. Neurochem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1089\/zeb.2018.1718","article-title":"Characterization of Intracellular Peptides from Zebrafish (Danio rerio) Brain","volume":"16","author":"Teixeira","year":"2019","journal-title":"Zebrafish"},{"key":"ref_18","doi-asserted-by":"crossref","unstructured":"Dasgupta, S., Yang, C., Castro, L.M., Tashima, A.K., Ferro, E.S., Moir, R.D., Willis, I.M., and Fricker, L.D. (2016). Analysis of the Yeast Peptidome and Comparison with the Human Peptidome. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0163312"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1007\/978-1-4939-7537-2_27","article-title":"Analysis of Endogenous Peptide Pools of Physcomitrella patens Moss","volume":"1719","author":"Fesenko","year":"2018","journal-title":"Methods Mol. Biol."},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Fesenko, I.A., Arapidi, G.P., Skripnikov, A.Y., Alexeev, D.G., Kostryukova, E.S., Manolov, A.I., Altukhov, I.A., Khazigaleeva, R.A., Seredina, A.V., and Kovalchuk, S.I. (2015). Specific pools of endogenous peptides are present in gametophore, protonema, and protoplast cells of the moss Physcomitrella patens. Bmc Plant. Biol., 15.","DOI":"10.1186\/s12870-015-0468-7"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1042\/bj2940451","article-title":"Human thimet oligopeptidase","volume":"294","author":"Dando","year":"1993","journal-title":"Biochem J."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1042\/bj3240517","article-title":"Structural features that make oligopeptides susceptible substrates for hydrolysis by recombinant thimet oligopeptidase","volume":"324","author":"Camargo","year":"1997","journal-title":"Biochem. J."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"4417","DOI":"10.1021\/bi002715k","article-title":"Substrate specificity characterization of recombinant metallo oligo-peptidases thimet oligopeptidase and neurolysin","volume":"40","author":"Oliveira","year":"2001","journal-title":"Biochemistry"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"20480","DOI":"10.1074\/jbc.M400795200","article-title":"Crystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation, and localization","volume":"279","author":"Ray","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1016\/j.jmb.2017.11.011","article-title":"Mechanism of Peptide Binding and Cleavage by the Human Mitochondrial Peptidase Neurolysin","volume":"430","author":"Teixeira","year":"2018","journal-title":"J. Mol. Biol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1038\/ni.1974","article-title":"Antigen processing by nardilysin and thimet oligopeptidase generates cytotoxic T cell epitopes","volume":"12","author":"Kessler","year":"2011","journal-title":"Nat. Immunol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1006\/bbrc.1999.0250","article-title":"Thimet oligopeptidase (EC 3.4.24.15), a novel protein on the route of MHC class I antigen presentation","volume":"255","author":"Silva","year":"1999","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/0006-8993(92)90517-D","article-title":"Immunocytochemical localization of endopeptidase 24.15 in rat brain","volume":"571","author":"Healy","year":"1992","journal-title":"Brain Res."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1002\/cne.1323","article-title":"Comparative fine structural distribution of endopeptidase 24.15 (EC3.4.24.15) and 24.16 (EC3.4.24.16) in rat brain","volume":"438","author":"Massarelli","year":"2001","journal-title":"J. Comp. Neurol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/S0006-8993(99)02135-6","article-title":"Differential subcellular distribution of neurolysin (EC 3.4.24.16) and thimet oligopeptidase (EC 3.4.24.15) in the rat brain","volume":"851","author":"Massarelli","year":"1999","journal-title":"Brain Res."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"eaal3321","DOI":"10.1126\/science.aal3321","article-title":"A subcellular map of the human proteome","volume":"356","author":"Thul","year":"2017","journal-title":"Science"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1260419","DOI":"10.1126\/science.1260419","article-title":"Proteomics. Tissue-based map of the human proteome","volume":"347","author":"Fagerberg","year":"2015","journal-title":"Science"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"4358","DOI":"10.1111\/j.1742-4658.2009.07144.x","article-title":"Interaction with calmodulin is important for the secretion of thimet oligopeptidase following stimulation","volume":"276","author":"Russo","year":"2009","journal-title":"FEBS J."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1111\/j.1471-4159.2004.02967.x","article-title":"14-3-3 epsilon modulates the stimulated secretion of endopeptidase 24.15","volume":"93","author":"Carreno","year":"2005","journal-title":"J. Neurochem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"2978","DOI":"10.1111\/j.1742-4658.2005.04692.x","article-title":"Calcium modulates endopeptidase 24.15 (EC 3.4.24.15) membrane association, secondary structure and substrate specificity","volume":"272","author":"Oliveira","year":"2005","journal-title":"FEBS J."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"415","DOI":"10.2174\/0929866043406706","article-title":"The intracellular distribution and secretion of endopeptidases 24.15 (EC 3.4.24.15) and 24.16 (EC 3.4.24.16)","volume":"11","author":"Ferro","year":"2004","journal-title":"Protein Pept. Lett."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1089\/104454999315385","article-title":"Confocal microscopy reveals thimet oligopeptidase (EC 3.4.24.15) and neurolysin (EC 3.4.24.16) in the classical secretory pathway","volume":"18","author":"Garrido","year":"1999","journal-title":"Dna Cell Biol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1089\/104454999314926","article-title":"Secretion of metalloendopeptidase 24.15 (EC 3.4.24.15)","volume":"18","author":"Ferro","year":"1999","journal-title":"DNA Cell Biol"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1006\/bbrc.1993.1213","article-title":"Secretion of a neuropeptide-metabolizing enzyme similar to endopeptidase 22.19 by glioma C6 cells","volume":"191","author":"Ferro","year":"1993","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1111\/j.1471-4159.2006.03706.x","article-title":"Modulation of bradykinin signaling by EP24.15 and EP24.16 in cultured trigeminal ganglia","volume":"97","author":"Jeske","year":"2006","journal-title":"J. Neurochem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1002\/jnr.10779","article-title":"Novel roles of neuropeptide processing enzymes: EC3.4.24.15 in the neurome","volume":"74","author":"Kim","year":"2003","journal-title":"J. Neurosci. Res."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"36514","DOI":"10.1074\/jbc.M001843200","article-title":"The neuropeptide processing enzyme EC 3.4.24.15 is modulated by protein kinase A phosphorylation","volume":"275","author":"Tullai","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/S0006-8993(99)01494-8","article-title":"The association of metalloendopeptidase EC 3.4.24.15 at the extracellular surface of the AtT-20 cell plasma membrane","volume":"835","author":"Crack","year":"1999","journal-title":"Brain Res."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"487","DOI":"10.4149\/neo_2018_181029N805","article-title":"Prognosis related miRNAs, DNA methylation, and epigenetic interactions in lung adenocarcinoma","volume":"66","author":"Liu","year":"2019","journal-title":"Neoplasma"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1016\/S1074-7613(03)00058-X","article-title":"The cytosolic endopeptidase, thimet oligopeptidase, destroys antigenic peptides and limits the extent of MHC class I antigen presentation","volume":"18","author":"York","year":"2003","journal-title":"Immunity"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1042\/bj20030490","article-title":"Regulation of cell-surface major histocompatibility complex class I expression by the endopeptidase EC3.4.24.15 (thimet oligopeptidase)","volume":"375","author":"Kim","year":"2003","journal-title":"Biochem. J."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1006\/bbrc.1999.0251","article-title":"Thimet oligopeptidase and the stability of MHC class I epitopes in macrophage cytosol","volume":"255","author":"Portaro","year":"1999","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"17395","DOI":"10.1074\/jbc.272.28.17395","article-title":"Thiol activation of endopeptidase EC 3.4.24.15. A novel mechanism for the regulation of catalytic activity","volume":"272","author":"Shrimpton","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1006\/bbrc.1998.8941","article-title":"Neuropeptide specificity and inhibition of recombinant isoforms of the endopeptidase 3.4.24.16 family: Comparison with the related recombinant endopeptidase 3.4.24.15","volume":"250","author":"Rioli","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"813","DOI":"10.1046\/j.1365-2826.1997.00637.x","article-title":"Endopeptidase EC 3.4.24.15 presence in the rat median eminence and hypophysial portal blood and its modulation of the luteinizing hormone surge","volume":"9","author":"Wu","year":"1997","journal-title":"J. Neuroendocrinol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1016\/0300-9084(94)90160-0","article-title":"The role of EC 3.4.24.15 in the post-secretory regulation of peptide signals","volume":"76","author":"Smith","year":"1994","journal-title":"Biochimie"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"12626","DOI":"10.1016\/S0021-9258(18)99922-9","article-title":"Evidence for a two-step mechanism of gonadotropin-releasing hormone metabolism by prolyl endopeptidase and metalloendopeptidase EC 3.4.24.15 in ovine hypothalamic extracts","volume":"269","author":"Lew","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"10323","DOI":"10.1021\/bi00497a006","article-title":"Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15","volume":"29","author":"Pierotti","year":"1990","journal-title":"Biochemistry"},{"key":"ref_54","doi-asserted-by":"crossref","unstructured":"Santos, N.B.D., Franco, R.D., Camarini, R., Munhoz, C.D., Eichler, R.A.S., Gewehr, M.C.F., Reckziegel, P., Llanos, R.P., Dale, C.S., and Silva, V. (2019). Thimet Oligopeptidase (EC 3.4.24.15) Key Functions Suggested by Knockout Mice Phenotype Characterization. Biomolecules, 9.","DOI":"10.3390\/biom9080382"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"2264","DOI":"10.1167\/iovs.17-23678","article-title":"Proteomic Analysis of Early Diabetic Retinopathy Reveals Mediators of Neurodegenerative Brain Diseases","volume":"59","author":"Sundstrom","year":"2018","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1186\/s13075-017-1220-5","article-title":"Discovery of new candidate genes for rheumatoid arthritis through integration of genetic association data with expression pathway analysis","volume":"19","author":"Shchetynsky","year":"2017","journal-title":"Arthritis Res."},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Qi, L., Li, S.H., Si, L.B., Lu, M., and Tian, H. (2014). Expression of THOP1 and its relationship to prognosis in non-small cell lung cancer. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0106665"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"S443","DOI":"10.1245\/s10434-014-3581-1","article-title":"Expression analysis of THOP1 in background liver, a prognostic predictive factor in hepatocellular carcinoma, extracted by multiarray analysis","volume":"21","author":"Nomoto","year":"2014","journal-title":"Ann. Surg. Oncol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/j.nbd.2008.04.004","article-title":"Increased expression of the oligopeptidase THOP1 is a neuroprotective response to Abeta toxicity","volume":"31","author":"Pollio","year":"2008","journal-title":"Neurobiol. Dis."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"5823","DOI":"10.1113\/JP275422","article-title":"Primate fetal hepatic responses to maternal obesity: Epigenetic signalling pathways and lipid accumulation","volume":"596","author":"Puppala","year":"2018","journal-title":"J. Physiol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"2237","DOI":"10.1110\/ps.0216302","article-title":"Mapping sequence differences between thimet oligopeptidase and neurolysin implicates key residues in substrate recognition","volume":"11","author":"Ray","year":"2002","journal-title":"Protein. Sci."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1006\/abio.2001.5083","article-title":"Selective neurotensin-derived internally quenched fluorogenic substrates for neurolysin (EC 3.4.24.16): Comparison with thimet oligopeptidase (EC 3.4.24.15) and neprilysin (EC 3.4.24.11)","volume":"292","author":"Oliveira","year":"2001","journal-title":"Anal. Biochem."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/j.jprot.2014.03.043","article-title":"Peptidomic analysis of the neurolysin-knockout mouse brain","volume":"111","author":"Castro","year":"2014","journal-title":"J. Proteom."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"15426","DOI":"10.1074\/jbc.M113.539148","article-title":"Neurolysin knockout mice generation and initial phenotype characterization","volume":"289","author":"Cavalcanti","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"de Araujo, C.B., Heimann, A.S., Remer, R.A., Russo, L.C., Colquhoun, A., Forti, F.L., and Ferro, E.S. (2019). Intracellular Peptides in Cell Biology and Pharmacology. Biomolecules, 9.","DOI":"10.3390\/biom9040150"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"2668","DOI":"10.1002\/pmic.201200051","article-title":"Identification of intracellular peptides in rat adipose tissue: Insights into insulin resistance","volume":"12","author":"Berti","year":"2012","journal-title":"Proteomics"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"14781","DOI":"10.1038\/s41598-017-13690-9","article-title":"A novel peptide that improves metabolic parameters without adverse central nervous system effects","volume":"7","author":"Reckziegel","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1172\/JCI92035","article-title":"Inflammatory mechanisms linking obesity and metabolic disease","volume":"127","author":"Saltiel","year":"2017","journal-title":"J. Clin. Investig."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1016\/j.bbrc.2010.03.045","article-title":"Catalytic properties of thimet oligopeptidase H600A mutant","volume":"394","author":"Machado","year":"2010","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1016\/j.bbrc.2005.11.041","article-title":"Substrate phosphorylation affects degradation and interaction to endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme","volume":"339","author":"Machado","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1677\/joe.0.0400527","article-title":"Correlation between \u2018Lee index\u2019 and carcass fat content in weanling and adult female rats with hypothalamic lesions","volume":"40","author":"Bernardis","year":"1968","journal-title":"J. Endocrinol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1038\/s41588-018-0064-5","article-title":"A large electronic-health-record-based genome-wide study of serum lipids","volume":"50","author":"Hoffmann","year":"2018","journal-title":"Nat. Genet."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"1514","DOI":"10.1038\/s41588-018-0222-9","article-title":"Genetics of blood lipids among ~300,000 multi-ethnic participants of the Million Veteran Program","volume":"50","author":"Klarin","year":"2018","journal-title":"Nat. Genet."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"965","DOI":"10.1016\/0024-3205(93)90532-8","article-title":"Circadian rhythms of plasma corticosterone at different times after induction of diabetes. Responses to corticoadrenal stimulation in light and dark phases","volume":"52","author":"Velasco","year":"1993","journal-title":"Life Sci."},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"(2006). Langin, D, Adipose tissue lipolysis as a metabolic pathway to define pharmacological strategies against obesity and the metabolic syndrome. Pharmacol. Res., 53, 482\u2013491.","DOI":"10.1016\/j.phrs.2006.03.009"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"3540","DOI":"10.3748\/wjg.v13.i26.3540","article-title":"Metabolic liver disease of obesity and role of adipose tissue in the pathogenesis of nonalcoholic fatty liver disease","volume":"13","author":"Qureshi","year":"2007","journal-title":"World J. Gastroenterol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/j.freeradbiomed.2019.05.029","article-title":"Lipidomic biomarkers and mechanisms of lipotoxicity in non-alcoholic fatty liver disease","volume":"144","author":"Pierantonelli","year":"2019","journal-title":"Free Radic. Biol. Med."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"1489","DOI":"10.1002\/hep.25880","article-title":"Analysis of the role of hepatic PPAR\u03b3 expression during mouse liver regeneration","volume":"56","author":"Gazit","year":"2012","journal-title":"Hepatology"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"2331","DOI":"10.1172\/JCI2961","article-title":"Activation of cholesterol synthesis in preference to fatty acid synthesis in liver and adipose tissue of transgenic mice overproducing sterol regulatory element-binding protein-2","volume":"101","author":"Horton","year":"1998","journal-title":"J. Clin. Investig."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"866","DOI":"10.1007\/s13361-017-1852-3","article-title":"Quantitative Peptidomics with Five-plex Reductive Methylation labels","volume":"29","author":"Tashima","year":"2018","journal-title":"J. Am. Soc. Mass Spectrom."},{"key":"ref_81","doi-asserted-by":"crossref","unstructured":"Dasgupta, S., Fishman, M.A., Castro, L.M., Tashima, A.K., Ferro, E.S., and Fricker, L.D. (2019). Effect of Protein Denaturation and Enzyme Inhibitors on Proteasomal-Mediated Production of Peptides in Human Embryonic Kidney Cells. Biomolecules, 9.","DOI":"10.3390\/biom9060207"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"608","DOI":"10.1208\/s12248-010-9224-y","article-title":"Similar intracellular peptide profile of TAP1\/beta2 microglobulin double-knockout mice and C57BL\/6 wild-type mice as revealed by peptidomic analysis","volume":"12","author":"Castro","year":"2010","journal-title":"Aaps J."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"24448","DOI":"10.1074\/jbc.M801252200","article-title":"Intracellular peptides as natural regulators of cell signaling","volume":"283","author":"Cunha","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"3287","DOI":"10.1016\/j.febslet.2012.07.002","article-title":"Inhibition of thimet oligopeptidase by siRNA alters specific intracellular peptides and potentiates isoproterenol signal transduction","volume":"586","author":"Russo","year":"2012","journal-title":"Febs. Lett."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"25324","DOI":"10.1074\/jbc.M100560200","article-title":"Sterol carrier protein-2 expression modulates protein and lipid composition of lipid droplets","volume":"276","author":"Atshaves","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.diabres.2007.02.021","article-title":"Glycated albumin is low in obese, type 2 diabetic patients","volume":"78","author":"Miyashita","year":"2007","journal-title":"Diabetes Res. Clin Pr."},{"key":"ref_87","first-page":"529","article-title":"Does Glycated Albumin Increase with Body Weight Reduction in Obese Non-Diabetic Subjects?","volume":"49","author":"Koga","year":"2019","journal-title":"Ann. Clin. Lab. Sci."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1111\/brv.12116","article-title":"Intracellular role of exchangeable apolipoproteins in energy homeostasis, obesity and non-alcoholic fatty liver disease","volume":"90","author":"Wu","year":"2015","journal-title":"Biol. Rev. Camb. Philos. Soc."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"e161","DOI":"10.1038\/emm.2015.26","article-title":"The macrophage migration inhibitory factor protein superfamily in obesity and wound repair","volume":"47","author":"Kim","year":"2015","journal-title":"Exp. Mol. Med."},{"key":"ref_90","doi-asserted-by":"crossref","unstructured":"Kim, B.S., Rongisch, R., Hager, S., Grieb, G., Nourbakhsh, M., Rennekampff, H.O., Bucala, R., Bernhagen, J., and Pallua, N. (2015). Macrophage Migration Inhibitory Factor in Acute Adipose Tissue Inflammation. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0137366"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"308","DOI":"10.3389\/fimmu.2015.00308","article-title":"Role of Macrophage Migration Inhibitory Factor in Obesity, Insulin Resistance, Type 2 Diabetes, and Associated Hepatic Co-Morbidities: A Comprehensive Review of Human and Rodent Studies","volume":"6","author":"Morrison","year":"2015","journal-title":"Front. Immunol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"1324","DOI":"10.1074\/mcp.M117.067553","article-title":"The Landscape of Histone Modifications in a High-Fat Diet-Induced Obese (DIO) Mouse Model","volume":"16","author":"Nie","year":"2017","journal-title":"Mol. Cell Proteom."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"11","DOI":"10.3389\/fnut.2019.00011","article-title":"Peptides and Peptidomimetics as Potential Antiobesity Agents: Overview of Current Status","volume":"6","author":"Kumar","year":"2019","journal-title":"Front. Nutr."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1016\/j.cmet.2019.07.010","article-title":"Acyl-CoA-Binding Protein Is a Lipogenic Factor that Triggers Food Intake and Obesity","volume":"30","author":"Sica","year":"2019","journal-title":"Cell Metab."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1111\/j.1471-4159.2004.02757.x","article-title":"Intracellullar peptides as putative natural regulators of protein interactions","volume":"91","author":"Ferro","year":"2004","journal-title":"J. Neurochem."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"e34872","DOI":"10.1371\/journal.pone.0034872","article-title":"Differential expression of microRNAs in adipose tissue after long-term high-fat diet-induced obesity in mice","volume":"7","author":"Chartoumpekis","year":"2012","journal-title":"PLoS ONE"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"e38389","DOI":"10.7554\/eLife.38389","article-title":"Importance of miRNA stability and alternative primary miRNA isoforms in gene regulation during Drosophila development","volume":"7","author":"Zhou","year":"2018","journal-title":"eLife"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"107167","DOI":"10.18632\/oncotarget.22363","article-title":"About miRNAs, miRNA seeds, target genes and target pathways","volume":"8","author":"Kehl","year":"2017","journal-title":"Oncotarget"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"1551","DOI":"10.1002\/hep.28000","article-title":"Stimulation of nuclear receptor peroxisome proliferator-activated receptor-\u03b3 limits NF-\u03baB-dependent inflammation in mouse cystic fibrosis biliary epithelium","volume":"62","author":"Scirpo","year":"2015","journal-title":"Hepatol. (Baltim. Md.)"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"243","DOI":"10.3109\/07420529209064533","article-title":"Circadian rhythm of the endopeptidase 22.19 (EC 3.4.22.19) in the rat brain","volume":"9","author":"Ferro","year":"1992","journal-title":"Chronobiol. Int."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"550","DOI":"10.1038\/nature12710","article-title":"A diurnal serum lipid integrates hepatic lipogenesis and peripheral fatty acid use","volume":"502","author":"Liu","year":"2013","journal-title":"Nature"},{"key":"ref_102","doi-asserted-by":"crossref","unstructured":"Oike, H., Nagai, K., Fukushima, T., Ishida, N., and Kobori, M. (2011). Feeding cues and injected nutrients induce acute expression of multiple clock genes in the mouse liver. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0023709"},{"key":"ref_103","doi-asserted-by":"crossref","unstructured":"Shimizu, H., Hanzawa, F., Kim, D., Sun, S., Laurent, T., Umeki, M., Ikeda, S., Mochizuki, S., and Oda, H. (2018). Delayed first active-phase meal, a breakfast-skipping model, led to increased body weight and shifted the circadian oscillation of the hepatic clock and lipid metabolism-related genes in rats fed a high-fat diet. PLoS ONE, 13.","DOI":"10.1371\/journal.pone.0206669"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"989","DOI":"10.1038\/ijo.2010.12","article-title":"A microarray analysis of sexual dimorphism of adipose tissues in high-fat-diet-induced obese mice","volume":"34","author":"Grove","year":"2010","journal-title":"Int. J. Obes."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"2124","DOI":"10.1172\/JCI106179","article-title":"Effects of weight changes produced by exercise, food restriction, or overeating on body composition","volume":"48","author":"Oscai","year":"1969","journal-title":"J. Clin. Investig."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1016\/S0021-9258(18)64849-5","article-title":"A simple method for the isolation and purification of total lipides from animal tissues","volume":"226","author":"Folch","year":"1957","journal-title":"J. Biol. Chem."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1007\/s00395-010-0089-0","article-title":"Blockage of Angiotensin II type 2 receptor prevents thyroxine-mediated cardiac hypertrophy by blocking Akt activation","volume":"105","author":"Diniz","year":"2010","journal-title":"Basic Res. Cardiol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1045","DOI":"10.1002\/jcsm.12441","article-title":"Tumour-derived transforming growth factor-\u03b2 signalling contributes to fibrosis in patients with cancer cachexia","volume":"10","author":"Lima","year":"2019","journal-title":"J. Cachexiasarcopenia Muscle"},{"key":"ref_109","doi-asserted-by":"crossref","unstructured":"Nie, Y., Gavin, T.P., and Kuang, S. (2015, September 20). Measurement of Resting Energy Metabolism in Mice Using Oxymax Open Circuit Indirect Calorimeter. Available online: https:\/\/bio-protocol.org\/pdf\/bio-protocol1602.pdf.","DOI":"10.21769\/BioProtoc.1602"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"e45","DOI":"10.1093\/nar\/29.9.e45","article-title":"A new mathematical model for relative quantification in real-time RT-PCR","volume":"29","author":"Pfaffl","year":"2001","journal-title":"Nucleic Acids Res."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"e179","DOI":"10.1093\/nar\/gni178","article-title":"Real-time quantification of microRNAs by stem-loop RT-PCR","volume":"33","author":"Chen","year":"2005","journal-title":"Nucleic Acids Res."},{"key":"ref_112","doi-asserted-by":"crossref","unstructured":"Dasgupta, S., Castro, L.M., Dulman, R., Yang, C., Schmidt, M., Ferro, E.S., and Fricker, L.D. (2014). Proteasome inhibitors alter levels of intracellular peptides in HEK293T and SH-SY5Y cells. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0103604"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"D442","DOI":"10.1093\/nar\/gky1106","article-title":"The PRIDE database and related tools and resources in 2019: Improving support for quantification data","volume":"47","author":"Csordas","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"857","DOI":"10.1021\/jacs.5b09216","article-title":"Screening of Pre-miRNA-155 Binding Peptides for Apoptosis Inducing Activity Using Peptide Microarrays","volume":"138","author":"Pai","year":"2016","journal-title":"J. Am. Chem. Soc."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"1701","DOI":"10.1002\/jcc.20291","article-title":"GROMACS: Fast, flexible, and free","volume":"26","author":"Lindahl","year":"2005","journal-title":"J. Comput. Chem."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1400","DOI":"10.1002\/jcc.21726","article-title":"Combination of the CHARMM27 force field with united-atom lipid force fields","volume":"32","author":"Sapay","year":"2011","journal-title":"J. Comput. Chem."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"1545","DOI":"10.1002\/jcc.21287","article-title":"CHARMM: The biomolecular simulation program","volume":"30","author":"Brooks","year":"2009","journal-title":"J. Comput. Chem."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1038\/nature06684","article-title":"The MC-Fold and MC-Sym pipeline infers RNA structure from sequence data","volume":"452","author":"Parisien","year":"2008","journal-title":"Nature"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"1771","DOI":"10.1093\/bioinformatics\/btu097","article-title":"ZDOCK server: Interactive docking prediction of protein-protein complexes and symmetric multimers","volume":"30","author":"Pierce","year":"2014","journal-title":"Bioinformatics"}],"container-title":["Biomolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2218-273X\/10\/2\/321\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T08:58:34Z","timestamp":1760173114000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2218-273X\/10\/2\/321"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,2,17]]},"references-count":119,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2020,2]]}},"alternative-id":["biom10020321"],"URL":"https:\/\/doi.org\/10.3390\/biom10020321","relation":{},"ISSN":["2218-273X"],"issn-type":[{"value":"2218-273X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,2,17]]}}}