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Pandey"],"technology_type":["SRM/MRM","Mass Spectrometry"],"disease":["Disease Free","Alpha Thalassemia"],"software":[""],"submitter_keywords":["Hemoglobinopathy","Translation","thalassemia","Hematopoiesis","Protein"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD064022"],"tissue":["Blood Cell","Blood"],"sample_protocol":["Sample collection  Umbilical cord blood samples were collected from newborns at birth, while peripheral venous blood samples were obtained from pediatric subjects at the specified ages. Both cord and peripheral blood samples were sourced from unaffected individuals who provided deidentified residual samples. Adult whole blood samples were collected from deidentified volunteer donors.  Protein extraction and digestion  Dried blood spots (DBS) were prepared from whole blood by spotting 20 μl onto Cytiva Whatman 903 Protein Saver Cards. Proteins were extracted using 8 M urea buffer, followed by centrifugation to collect the extract. Protein concentration was measured, and equal amounts were processed for in-solution digestion. Disulfide bonds were reduced, cysteines alkylated, and samples diluted to reduce urea concentration before trypsin digestion overnight at 37°C. The digested peptides were acidified, desalted using C18 columns, and spiked with stable isotope-labeled peptides for further analysis.  Peptide selection and LC-MRM analysis  Synthetic peptides for globin quantitation were selected based on criteria such as unique sequence, appropriate length, absence of cysteine, and no missed cleavage sites. Multiple surrogate peptides were chosen for each globin chain, synthesized in-house using FMOC chemistry, and purified by reversed-phase chromatography. Peptide purity and integrity were verified using LC/MS. Prior to LC-MRM analysis, 500 fmol of the synthetic peptide mix was spiked into 5 µg of each sample digest. Discovery analysis of umbilical cord blood samples and synthetic peptide mixtures was performed using a 3000 RSLCnano system coupled to an Orbitrap Eclipse Tribrid Mass Spectrometer in data-dependent acquisition (DDA) mode. For synthetic peptides, the most intense MS/MS fragments were selected as transitions, optimized using default collision energy values in Skyline, and applied to a TSQ Altis Triple Quadrupole Mass Spectrometer. The LC-MRM method was developed on a TSQ Altis coupled with a Vanquish Horizon UHPLC system, using a 0.25 mL/min flow rate and an Accucore Vanquish C18+ UHPLC column at 60°C. Samples were run for 35 minutes with a gradient of 0.1% formic acid in water and acetonitrile, starting at 3% solvent B and increasing to 20% at 29 minutes. The TSQ Altis was operated in SRM mode with Q1 and Q3 resolutions set at 0.7 and 1.2, respectively, a collision gas pressure of 2 mTorr, and a cycle time of 0.833 seconds."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Data analysis and absolute quantitation  For discovery data, protein database searching was conducted using Sequest HT within Proteome Discoverer 2.5. The UniProt Human Reviewed database (20,432 entries) was used as the protein sequence reference in FASTA format. Search parameters included fully tryptic cleavage specificity with up to four missed cleavages, a precursor mass tolerance of 10 ppm, and a fragment mass tolerance of 0.02 Da. Carbamidomethylation of cysteines was specified as a fixed modification, while methionine oxidation and N-terminal protein acetylation were included as variable modifications. Calibration curves for surrogate synthetic peptides were created by diluting peptide stocks from 50 attomoles to 1 picomole on-column, spiked into pooled sample digests (5 µg per injection) as the background matrix, and acquired in triplicate. Peptide amounts were plotted against MS signal areas, with correlation coefficients of 0.99 or higher. Hemoglobin mu-globin quantitation was calculated relative to spiked-in internal standards. Results were expressed as the percentage contribution of each globin chain to the total or as the concentration (pg/µg of blood)."],"omics_type":["Proteomics"],"labhead":["Akhilesh Pandey, M.D., Ph.D."],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Department of Laboratory Medicine and Pathology, Mayo Clinic, Rochester, Minnesota 55905, United States"],"species":["Homo Sapiens (human)"],"publication":["42004318 Garapati K, Chavan S, Bellad A, Venkataraman S, Oglesbee D, Chakraborty R, Wick MJ, Girard S, Pandey A. Hemoglobin alpha-like subunit mu is expressed during ontogeny and is elevated in alpha thalassemia. Blood Red Cells Iron. 2026 2(1):100043 10.1016/j.brci.2025.100043"],"submitter_mail":["pandey.akhilesh@mayo.edu"],"submitter_affiliation":["Department of Laboratory Medicine and Pathology, Mayo Clinic, Rochester, MN 55905"],"submitter_country":["United States"],"pubmed_abstract":["The alpha globin gene cluster on chromosome 16 encodes alpha-like globins whose expression changes during development. <i>HBM</i> located in this cluster was considered a pseudogene until its transcript was discovered in 2005, but without a detectable protein product. Here, we provide the first detailed description of <i>HBM</i>-encoded globin at the protein level (hemoglobin mu chain [HBM]) across different age groups using liquid chromatography coupled with tandem mass spectrometry. Using targeted analysis, we demonstrate that HBM protein is readily detectable in circulation with its levels falling with increasing gestational age. We also report HBM levels in relation to other hemoglobin chains in neonatal, pediatric, and adult blood. Furthermore, analysis of alpha thalassemia patient samples revealed that HBM levels were elevated 3- to 17-fold, indicating a compensatory role, which could be explored for its therapeutic potential. This study enhances our understanding of erythropoiesis and globin chain production through ontogeny."],"pubmed_title":["Hemoglobin alpha-like subunit mu is expressed during ontogeny and is elevated in alpha thalassemia."],"pubmed_authors":["Garapati Kishore K, Chavan Sandip S, Bellad Anikha A, Venkataraman Shilpa S, Oglesbee Devin D, Chakraborty Rana R, Wick Myra J MJ, Girard Sylvie S, Pandey Akhilesh A"],"additional_accession":[]},"is_claimable":false,"name":"Hemoglobin alpha-like chain subunit mu (HBM) is expressed during ontogeny and is elevated in alpha thalassemias","description":"Background: Alpha and beta-like globin chains are encoded by gene clusters on chromosomes 16 and 11, respectively, with controlled expression patterns through development and childhood into adulthood. The alpha gene cluster contains genes such as HBA1, HBA2, HBZ and HBM. HBM was initially thought to be a pseudogene. Subsequently, although a transcript was reported in cord blood, the encoded protein was not detected by early mass spectrometry-based analyses.  Methods: Dried blood spots (DBS) were obtained from umbilical cord blood of neonates born at term as well as preterm neonates born at different gestational age. DBS were also prepared from peripheral venous blood from other pediatric subjects up to 5 years of age. We developed a targeted mass spectrometry assay for all alpha- and beta-like globin chains using heavy synthetic peptide standards which were unique to each chain. Proteins were extracted from DBS samples and digested. The resulting samples were cleaned-up and spiked-in with heavy synthetic peptide standards prior to analysis in liquid chromatography – multiple reaction monitoring (LC-MRM) mode. Additionally, samples from patients with alpha thalassemia and from unaffected adult donors were also analyzed.   Results: Analysis of dried blood spots (DBS) from neonates by LC-MS/MS using discovery proteomics pipelines resulted in detection of HBM protein along with other globin chains with multiple unique peptides each. Targeted selected reaction monitoring (SRM) assays resulted in the detection of HBM in samples from preterm newborns at higher levels compared to all other samples. As the gestational age at collection increased from 32 weeks to term, the levels of HBM decreased, continuing to do so with postnatal age. Importantly, HBM levels fell precipitously between one week and two years after birth. Interestingly, HBM protein was detected at quantifiable levels in all tested samples including adult blood samples. The levels of HBM were elevated in certain types of alpha thalassemia in comparison with unaffected adult donors.  Conclusions: Our data reveal that HBM gene encodes a protein that is expressed at low levels in adults but is more abundant during development, suggesting that it could play a role in ontogeny, which is likely taken over by other globin chains post-birth. Further experimental studies are required to fully understand the functional role of HBM and its potential beta-like globin binding partner. The elevated levels of HBM observed in patients with alpha thalassemia are likely a compensatory mechanism to offset the deficiency of alpha-like chains.","dates":{"publication":"2026-04-27","submission":"2025-05-18"},"accession":"PXD064022","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2042546","NEWT:148942","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1310173","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:550537","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:215451","NEWT:460519","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2499525","NEWT:142786","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:272831","NEWT:987059","NEWT:491","NEWT:460523","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","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:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:445","NEWT:2003758","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:219798","NEWT:548","NEWT:150475","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:1225786","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","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:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:941638","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:300641","NEWT:39655","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:6039","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:280406","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:762903","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:266940","NEWT:287889","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:315750","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:1479235","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:105812","NEWT:11298","NEWT:4233","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:1170227","NEWT:2666255","NEWT:999810","NEWT:28995","NEWT:1392998","NEWT:1150621","NEWT:1085791","NEWT:745531","NEWT:226900","NEWT:231490","NEWT:590651","NEWT:449239","NEWT:244704","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:36599","NEWT:41949","NEWT:9900","NEWT:326423","NEWT:326424","NEWT:13013","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:431947","NEWT:142809","NEWT:1095183","NEWT:302409","N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