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Kim"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"software":[""],"submitter_keywords":["Alzheimer’s disease","Mild cognitive impairment","Proteomics","Liquid chromatography-tandem mass spectrometry; biomarker","Liquid chromatography-tandem mass spectrometry","Amyloid","biomarker","Platelets"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067460"],"tissue":["Blood Platelet"],"sample_protocol":["Blood samples were collected from all participants and platelets were isolated from them according to the procedures as described previously [32]. Platelets were lysyzed in a RIPA Buffer (150 mM NaCl, 50 mM triethylammonium bicarbonate, 1% SDS, 0.5% dichloroacetic acid, pH 8) for 20 min on ice to extract total protein. Protein concentration was measured by Pierce™ BCA Protein Assay Kit (Thermo Fisher Scientific, Waltham, MA, USA). Protein extracts (200 ug) were dissolved in a buffer (300 ul) containing 4% SDS, 100 mM dithiothreitol, 100 mM Tris-HCI (pH 7.6). Samples were added to the Microcon-30 kDa Centrifugal Filter Unit with Ultracel-30 membrane (Merck, Rahway, NJ, USA) and centrifuged (14,000 × g, 60 min, room temperature). The filter was washed with 180 ul of 8 M urea in 0.1 M Tris-HCl (pH 8.5) with 3 rounds by centrifugation (14,000 × g, 40 min), followed by alkylation with 50 mM iodoacetamide for 30 min at 37°C. The filter membrane was centrifuged equally and then washed with 180 ul of 8 M urea in 0.1 M Tris-HCl (pH 8.5) twice and then with 180 ul of 100 mM triethylammonium bicarbonate (TEAB) three times. Trypsin (Thermo Fisher Scientific) in 50 mM TEAB was added to filter at a ratio of 1:50 (enzyme/protein, wt/wt) and incubated at 37°C overnight. The tryptic peptides were eluted by centrifugation with 75 ul of 100 mM TEAB three times (14,000 × g, 20 min). The eluted peptides were vacuum-dried and desalted using Macro SpinColumns™ (Harvard Apparatus, Holliston, MA, United States). The peptides were labeled with TMT 10 plex (Thermo Fisher Scientific) according to the manufacturer’s instructions. Add 41 ul of anhydrous acetonitrile (ACN) to each tube, vortex sufficiently, and centrifuge. In brief, each sample in 0.1 M TEAB was labeled by mixing with different TMT labeling reagents in ACN and incubating for 1 h at room temperature. Hydroxylamine (5%) was added to the sample and incubated for 15 min. Two TMT 10-plex sets were employed, with each patient contributing platelet samples to nine of the channels. The remaining channel served as the reference and contained pooled samples from all patients. In order to increase the number of identified proteins in the data-dependent acquisition method, samples were separated into 96 fractions using 1100 series high performance liquid chromatography (HPLC) system (Agilent Technologies, Wilmington, DE, USA) equipped with XBridge BEH C18 column (130 Å, 5 um, 4.6 mm × 250 mm; Waters, Milford, MA, USA). Solvent A (4.5 mM ammonium formate in 2% ACN, pH 10-11) and solvent B (4.5 mM ammonium formate in 90% ACN, pH 10-11) were applied to the HPLC system with following gradients: 0 to 7 min, 0% B; 7 to 12 min, 12% B; 12 to 35 min 25% B; 35 to 85 min 40% B; 85 to 95 min 70% B; 95 to 101 min 70% B; 101 to 105 min 0% B; 105 to 115 min 0% B. The 96 fractions were combined into 12 fractions. The fractionated peptides were vacuum-dried and then desalted using Macro SpinColumns™. The desalted peptide samples were dissolved in 0.1% formic acid and analyzed using a nanoACQUITY UPLC System (Waters, Milford, MA, USA) connected to a Q Exactive Orbitrap Mass Spectrometer (Thermo Fisher Scientific, Waltham, MA, USA). The samples were analyzed by 180 min gradient of solvent A (3% ACN/0.1% formic acid in water) and solvent B (90% ACN/0.1% formic acid). The gradient was as follows: 0 to 5 min, 2% B; 5 to 10 min, 10% B; 10 to 140 min 25% B; 140 to 160 min 40% B; 160 to 161 min 90% B; 161 to 165 min 90% B; 165 to 166 min 2% B; 166 to 180 min 2% B. A constant flow rate was set at 0.300 ul/min. The peptides were loaded onto a C18 trap column (75 um × 2 cm, 3 um particle size, 100 Å pore size, Thermo Fisher Scientific) and then ionized on an EASY-spray column (75 um × 500 mm, 2 um particle size, 100 Å, Thermo Fisher Scientific). For the proteome profiling analysis in data-dependent acquisition mode, full MS spectra were acquired using positive polarity, scan rage of 350–1800 m/z, resolution of 70,000, and automatic gain control target value of 3e6. Maximum ion-injection time of 100 ms. MS/MS scan was set to resolution of 35,000, automatic gain control target value of 1e6 and maximum ion-injection time of 120 ms. The dynamic exclusion time was set to 30 s, and the high collisional dissociation collision energy was set to 32. The isolation window was set to 1.6 m/z."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The MS/MS spectra were analyzed using the SEQUEST HT search on Proteome Discoverer 2.1 software (Thermo Fisher Scientific) to search the UniProtKB human protein database (UniProtKB/SwissProt with 20,324 entries). Protein Discoverer 2.1 parameters set up cleavage at arginine and lysine residues using trypsin. A maximum of 2 missed cleavages were allowed. The carbamidomethylation of cysteine, TMT on lysine, and the N-terminus were set as static modification. In dynamic modification, oxidation of methionine was set. The tolerance was set to 10 ppm for the precursor masses and 0.02 Da for the fragment masses. The target peptide spectrum match and protein level analyses applied to a 1% false discovery rate (FDR) threshold. The threshold score for peptide identification was equivalent to 1% FDR. Proteins were quantified only if they have at least two unique peptides. The reporter ion quantification was based on intensity. The two TMT sets were normalized to reference channel and each channel was corrected for the ratio of the sum of protein abundances for all proteins identified in all channels."],"omics_type":["Proteomics"],"labhead":["Kwang Pyo Kim"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Department of Applied Chemistry, Institute of Natural Science, Kyung Hee University, Yongin 17104, Republic of Korea"],"species":["Homo Sapiens (human)"],"publication":["41904574 Cho YE, Kim A, Lee HM, Oh JW, Son SJ, Roh HW, Jung YS, Hong CH, Lee SY, Kim KP. Platelet proteomic signatures of amyloid β-positive mild cognitive impairment and Alzheimer's disease. Mol Brain. 2026 19(1):33 10.1186/s13041-026-01294-2"],"submitter_mail":["kkim39@snu.ac.kr"],"submitter_affiliation":["Seoul National University"],"submitter_country":["South Korea"],"pubmed_abstract":["Early detection of Alzheimer's disease (AD) is critical for preventing disease progression. Blood platelets have emerged as a useful peripheral source for AD diagnosis. However, the identification of proteomics-based platelet biomarkers of mild cognitive impairment (MCI) and AD in relation to amyloid β (Aβ) deposition remains largely unexplored. In this study, we compared four groups from 18 participants: subjective memory impairment (SMI, n = 4) as cognitive normal controls, MCI without Aβ deposition (MCI-A(+), n = 5), MCI with Aβ deposition (MCI-A(-), n = 5), and AD (n = 4). We conducted in-depth platelet protein profiling using high-throughput LC-MS/MS with tandem mass tag labeling. Among the total 4,524 proteins detected, we identified both unique and overlapping differentially expressed proteins in MCI-A(+), MCI-A(-), and AD compared with SMI. Hierarchical clustering analysis revealed seven distinct patterns of proteomic alterations across groups. Functional network and gene ontology enrichment analyses indicated that each cluster was associated with specific processes, including platelet activation, AD, and apoptotic signaling pathways. Notably, upregulated proteins in MCI-A(-) and AD were linked to endomembrane system organization. Furthermore, we quantified the relative abundance of multiple protein candidates that were significantly altered in MCI-A(-) and AD compared with SMI and MCI-A(+). Our findings highlight several platelet proteins-ATP6V0C, AP4B1, RAB2B, PSMD9, FKBP1B, and mTOR-as potential molecular targets for predicting AD at the stage of MCI with Aβ deposition, providing new insights into amyloid-related neurodegeneration."],"pubmed_title":["Platelet proteomic signatures of amyloid β-positive mild cognitive impairment and Alzheimer's disease."],"pubmed_authors":["Cho Yeong Eun YE, Kim Andrew A, Lee Hyeong Min HM, Oh Jae Won JW, Son Sang Joon SJ, Roh Hyun Woong HW, Jung Yi-Sook YS, Hong Chang Hyung CH, Lee Sang Yoon SY, Kim Kwang Pyo KP"],"additional_accession":[]},"is_claimable":false,"name":"In-Depth Platelet Proteomic Analysis in Various Dementia Stages: Unveiling Biomarkers for Alzheimer's Disease","description":"Early detection of Alzheimer’s disease (AD) can provide an effective scheme to prevent the disease progression. Studies have shown that blood platelets are a useful peripheral source for AD diagnosis. Identifying proteomics-based platelet biomarkers of mild cognitive impairment (MCI) and AD related to amyloid  peptide (A) deposition, which remains largely unexplored, is valuable. This study compared four groups from 18 human participants. subjective memory impairment (SMI, n = 4) as cognitive normal control, MCI without A deposition (MCI-A(), n = 5), MCI with A deposition (MCI-A(), n = 5), and AD (n = 4). We performed in-depth platelet protein profiling using high-throughput LC–MS/MS with tandem mass tag (TMT) labeling.MCI-A(), MCI-A(), and AD in comparison to SMI. Hierarchical clustering analysis revealed seven different patterns of proteomic alterations among functional network and gene ontology (GO) enrichment showed a distinct feature of each cluster specific processes such as platelet activation, AD, and apoptotic signaling pathways. In particular, our data indicated that upregulated proteins in MCI-A() and AD are associated with endomembrane system organization. Moreover, we determined the relative abundance of multiple protein candidates that significantly changed in MCI-A() and AD compared to SMI and MCI-A(). Our data demonstrated that several platelet proteins, including ATP6V0C, AP4B1, RAB2B, PSMD9, FKBP1B, and mTOR, can be key molecular targets for predicting AD at the stage of MCI with A deposition and provide insights into amyloid-related neurodegeneration.","dates":{"publication":"2026-05-25","submission":"2025-08-18"},"accession":"PXD067460","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:1584","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:7719","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:237610","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:906914","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:49012","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:1613","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:443906","NEWT:13037","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:28550","NEWT:80863","NEWT:90675","NEWT:52639","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEW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