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Zhang"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Melatonin","Non-alcoholic steatotic liver disease","Lipid metabolism"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD071550"],"tissue":["Liver","Cell Culture"],"sample_protocol":["CETSA (Cellular Thermal Shift Assay) is an experimental method that leverages the principle that “drug binding to a target protein enhances its thermal stability, delaying denaturation and precipitation to higher temperatures.” It enables direct assessment of drug-target interactions under near-physiological conditions, effectively addressing the limitation of traditional in vitro binding assays that struggle to reflect true in vivo binding scenarios. The target proteins of melatonin were identified using CETSA-MS, carried out following established protocols [36,37]. Differentiated 3T3 cells were harvested, and cell pellet were lysed using a mild lysis buffer (containing 1× protein inhibitors, 50 mmol/L HEPES, 0.1 mmol/L activated Na₃VO₄, 5 mmol/L β-glycerophosphate, 1 mmol/L tris(2-hydroxypropyl)amine (TCEP), and 20 mmol/L MgCl₂) and a mild lysis method (subjecting the resulting pellet to three rapid freeze-thaw cycles between liquid nitrogen and room-temperature water) was employed to preserve the activity of most proteins. Then the resulting cell lysates were treated with different concentrations of melatonin (9 concentration gradients of 0.001, 0.025, 0.01, 0.1, 0.5, 1, 2.5, 5, and 10 mM) as well as a DMSO control to serve as a negative control. The cell lysates underwent thermal cycling at 52℃ for 3 min each, followed by a cooling period at 4℃ for an additional 3 min on a PCR instrument. The lysates were then centrifuged at 4℃ for 10 min at 20,000 g. The supernatants subsequently underwent dithiothreitol (DTT) reduction, alkylation with iodoacetamide (IAA), and overnight trypsin digestion. Following enzymatic digestion, the samples were desalted and dried. The peptide samples were reconstituted and labeled with TMT reagent. To enhance the analytical separation, the peptides were subjected to high-performance liquid chromatography (HPLC)-based fractionation, spun-dried, and then reconstituted in a solution containing 0.1% formic acid and 1% acetonitrile. These samples were analyzed by a high-resolution Orbitrap LC-MS/MS mass spectrometer, with resultant data processed through the Proteome Discoverer software. Based on the protein quantification results, isothermal dose-response (ITDR) curves were plotted using the mineCETSA program package. Liver tissue samples (n=3) from the chow, HFD, mel-low, and mel-high were separately added to RIPA solution and protease inhibitor. Tissue homogenizers were used for homogenization. After thorough mixing, samples were centrifuged at 4°C at 22,000 g for 15 min. The supernatant was collected, and protein concentration was measured. From each sample, 100 µg of protein was taken and mixed with a final concentration of 40 mM DTT. After treatment at 37°C for 30 min, a final concentration of 50 mM IAA was added and incubated in the dark for 30 min. The mixture was precipitated with acetone at -40°C for 30 min, centrifuge at 22,000 g for 15 min. Add 100 mM TEAB to the pellet, sonicate, then digest with trypsin for 16 h. Pass through a desalting column (WAT094225, Waters, USA) and dry the sample. Then reconstituted in a solution containing 0.1% formic acid and 1% acetonitrile. These samples were analyzed by a high-resolution Orbitrap LC-MS/MS mass spectrometer."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Data were processed using Proteome Discovery software (Thermo Fisher Scientific, version 2.4), Mascot (v2.6.1), and the SEQUEST® HT search engine. All mass spectrometry data were aligned against the UniProtKB mouse FASTA database (Mus_musculus_uniprot_reviewed_202205.fasta). Identification search parameters were set as follows: MS1 tolerance 10 ppm; MS/MS tolerance 0.02 Da; trypsin as the specific digestion enzyme with 2 uncut sites allowed. Fixed modifications: carbamoylation of cysteine; variable modifications: methionine oxidation and phosphorylation of serine, threonine, and tyrosine. For protein identification, the false discovery rate (FDR) for PSMs was set to 1%. Following protein identification, the proteomics dataset was visualized using statistical software R (version 4.1.1). Differentially Expressed Proteins (DEPs) Identification: The limma package (version 3.54.2) was used to calculate expression difference P-values and fold change values. Proteins with P < 0.05 and Fold Change > 1.5 were selected as differentially expressed proteins (DEPs). Enrichment analysis of DEPs was performed using GO and KEGG resources."],"omics_type":["Proteomics"],"labhead":["Yongping Zhu"],"instrument_platform":[""],"labhead_affiliation":["State Key Laboratory for Quality Ensurance and Sustainable Use of Dao-di Herbs, Artemisinin Research Center, and Institute of Chinese Materia Medica, China Academy of Chinese Medical Sciences"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["jzzhang@icmm.ac.cn"],"publication":["42118212 Zhu Y, Liu Y, Liu R, Zhang J, Meng Y, Liu L, Liu X, Liu D, Gu L, Zhong L, Xu X, Li Y, Xu J, Dai L, Shen S, Wang J. Melatonin targets mitochondrial trifunctional enzyme HADHA to improve lipid metabolism in metabolic dysfunction-associated steatotic liver disease. Mol Biomed. 2026 7(1):68 10.1186/s43556-026-00461-0"],"submitter_affiliation":["Institute of Chinese Materia Medica, China Academy of Chinese Medical Sciences"],"submitter_country":["China"],"pubmed_abstract":["Metabolic dysfunction-associated steatotic liver disease (MASLD) is a clinicopathological syndrome characterized by abnormal accumulation of fat within hepatocytes, and there is currently no standardized clinical treatment available. Consequently, there is an urgent need to discover new pharmacological interventions and to investigate novel therapeutic targets for MASLD. Melatonin, known for its multifaceted biological functions, has shown therapeutic potential for the treatment of MASLD. However, the underlying mechanisms remain unclear, particularly since the direct targets of melatonin remain poorly understood. In our study, we found that melatonin significantly improved various indicators in a mouse MASLD model and protected palmitic acid-induced mouse hepatocytes from lipid accumulation. We successfully identified and validated the mitochondrial trifunctional enzyme α-subunit HADHA as a binding target for melatonin using the cellular thermal shift assay (CETSA). This interaction enhanced the expression of peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1α), which subsequently promotes mitochondrial biogenesis and accelerates lipid metabolism. In addition, melatonin reduced lipid accumulation and ameliorated MASLD through its regulatory effect on key proteins involved in fatty acid metabolism, including acyl coenzyme A oxidase 1 (ACOX1), cluster of differentiation 36 (CD36), and fatty acid synthase (FASN). Importantly, these beneficial effects were diminished when HADHA was knocked down. In conclusion, our study suggests that melatonin ameliorates MASLD through HADHA-mediated regulation of mitochondrial biogenesis and lipid oxidation, highlighting its potential as a promising therapeutic agent for MASLD. These results offer novel insights into the role of melatonin in the treatment of MASLD."],"pubmed_title":["Melatonin targets mitochondrial trifunctional enzyme HADHA to improve lipid metabolism in metabolic dysfunction-associated steatotic liver disease."],"pubmed_authors":["Zhu Yongping Y, Liu Yanqing Y, Liu Rui R, Zhang Junzhe J, Meng Yuqing Y, Liu Li L, Liu Xin X, Liu Dandan D, Gu Liwei L, Zhong Linying L, Xu Xianyu X, Li Ying Y, Xu Jinyan J, Dai Lingyun L, Shen Shengnan S, Wang Jigang J"],"additional_accession":[]},"is_claimable":false,"name":"Melatonin targets mitochondrial trifunctional enzyme HADHA to improve lipid metabolism in metabolic dysfunction-associated steatotic liver disease","description":"Metabolic dysfunction-associated steatotic liver disease (MASLD) is a clinicopathological syndrome characterized by abnormal accumulation of fat within hepatocytes, and there is currently no standardized clinical treatment available. Consequently, there is an urgent need to discover new pharmacological interventions and to investigate novel therapeutic targets for MASLD. Melatonin, known for its multifaceted biological functions, has shown therapeutic potential for the treatment of MASLD. However, the underlying mechanisms remain unclear, particularly since the direct targets of melatonin have not yet been discovered. In our study, we found that melatonin significantly improved various indicators in a mouse MASLD model and protected palmitic acid induced mouse hepatocytes from lipid accumulation. We successfully identified and validated the mitochondrial trifunctional enzyme α-subunit HADHA as a binding target for melatonin using the cellular thermal shift assay (CETSA). This interaction enhances the expression of PGC-1α, which subsequently promotes mitochondrial biogenesis and accelerates lipid metabolism. In addition, melatonin reduces lipid accumulation and ameliorates MASLD through its regulatory effect on key proteins involved in fatty acid metabolism, including Acyl coenzyme A oxidase 1, CD36, and Fatty acid synthase. Importantly, these beneficial effects are diminished when HADHA is knocked down. In conclusion, our study suggests that melatonin ameliorates MASLD through HADHA-mediated regulation of mitochondrial biogenesis and lipid oxidation, highlighting its potential as a promising therapeutic agent for MASLD. These results lay a theoretical foundation and offer novel insights and strategies into the role of melatonin in the treatment of MASLD.","dates":{"publication":"2026-06-08","submission":"2025-12-04"},"accession":"PXD071550","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2737160","NEWT:2042546","NEWT:2042545","NEWT:148942","NEWT:193528","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:57577","NEWT:156563","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:44270","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:93217","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:10031","NEWT:82569","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:109376","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:1190602","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:1176302","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:77151","NEWT:317447","NEWT:698761","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:1177","NEWT:11308","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:143292","NEWT:2767842","NEWT:314345","NEWT:224308","NEWT:3134131","NEWT:49928","NEWT:160621","NEWT:110368","NCBITaxon:5204","NEWT:1916073","NEWT:1303873","NEWT:305400","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:160620","NCBITaxon:77643","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:32224","NEWT:11320","NEWT:1410384","NEWT:1310173","NEWT:1072569","NEWT:1072568","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:135666","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1336794","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3710","NEWT:393133","NEWT:65125","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3716","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:118221","NEWT:32201","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:284811","NEWT:2902907","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:10882","NEWT:1431297","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:1423687","NEWT:657322","NEWT:10886","NEWT:3707","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:1301262","NEWT:319224","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:292415","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:223074","NEWT:2499525","NEWT:467144","NEWT:142786","NEWT:28196","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:387344","NEWT:657318","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:367737","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:272831","NEWT:987059","NEWT:491","NEWT:422203","NEWT:460523","NEWT:2422","NEWT:2423","NEWT:3755","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:1195466","NEWT:2483192","NEWT:85698","NEWT:291146","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:34839","NEWT:476","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NEWT:106299","NCBITaxon:50557","NEWT:63363","NEWT:3735","NEWT:1002697","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:427924","NEWT:2003758","NEWT:29486","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:1120755","NEWT:1862567","NEWT:591090","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:29471","NEWT:108931","NEWT:219799","NEWT:1325292","NEWT:219798","NEWT:548","NEWT:150475","NEWT:546","NEWT:1431340","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:630390","NEWT:550","NEWT:10804","NEWT:52694","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:40686","NEWT:1225786","NEWT:366497","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:771875","NEWT:377142","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10835","NEWT:10832","NEWT:311339","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:536","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:480020","NEWT:51315","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353154","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:6055","NEWT:13037","NEWT:5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