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Neely"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Kemp’s ridley sea turtle","Plasma","Lc-ms/ms"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD079061"],"tissue":["Blood Plasma"],"sample_protocol":["Previous blood sample collection from Kemp’s ridley sea turtles was conducted during 2010 under appropriate authorizations associated with the Deepwater Horizon Oil Spill response, including Marine Turtle Permit #021. Following their capture, oiled juvenile Kemp’s ridleys were assigned to one of four oiling categories (OC) before being transported to the Audubon Nature Institute rehabilitation facility, New Orleans, LA, USA. Blood samples were taken from the external jugular vein after their arrival to the rehabilitation facility but prior to any bathing or intervention. These samples are considered the “Admission” samples for each turtle. Additionally, “Rehabilitation” samples were taken from the external jugular vein following successful rehabilitation (30-59 d) and prior to release back into the Gulf of Mexico. Once collected, blood samples were immediately transferred into a lithium-heparin anticoagulant and centrifuged at 5000 x g for 10 minutes to harvest plasma. Samples were stored in a -20˚ C freezer for approximately 5 months following collection and then transferred to a -80˚ C freezer. Plasma samples were thawed on ice and vortexed for 10 seconds prior to determination of protein concentration using the Bradford method (acidified Coomassie Brilliant Blue G-250, Bio-Rad Catalog #500-0006) with phosphate buffered saline. Plasma samples were thawed on ice and vortexed for 10 seconds prior to in-solution digestion. Using the protein concentration determined by the Bradford assay, 150 µg of protein were combined with approximately 95.5 µl (range: 92.5 – 97.0 µl) of 50 mM Ammonium Bicarbonate (AmmBic) in 1.5 mL Lo-Bind microcentrifuge tubes (Eppendorf) and vortexed for 10 seconds to mix. Samples were then reduced with 11.1 µL of 10 mM Dithiothreitol (DTT; prepared by dissolving 20 mg of 90 mM DTT in 2 mL of water) to a final DTT concentration of approximately 0.1 mM to break disulfide bonds. Samples were vortexed and centrifuged prior to being incubated at 60˚ C on a heat block for 30 minutes. After cooling to room temperature (22˚ C), samples were alkalized by adding 11.1 µL of 20 mM chloroacetamide (CAA; prepared by dissolving 37.4 mg of 200 mM CAA in 2 mL of water) to a final CAA concentration of approximately 0.16 mM and incubating at room temperature (22˚ C) in the dark for 30 minutes. Following the second incubation, 100 µL of 50 mM AmmBic was added to all samples and lightly vortexed to mix. Proteins were then digested with 7.5 µL of 1 µg/µL Pierce™ trypsin protease (100 µg powder reconstituted with 100µL 50mM acetic acid) in 1:20 enzyme to protein ratio. Following the addition of the proteolytic enzyme, samples were incubated at 37˚ C for 4 hours in an Isotemp incubator (model 203FS, ThermoFisher Scientific, Dubuque, IA, USA). In order to stop the digestion process, 45.9 µL of 1% formic acid was added to all samples and vortexed to mix. Samples were then stored frozen at -80˚ C before preparing peptides for solid-phase extraction. Solid-phase cartridges (Affinisep, AttractSPE® Disks Spin C18-cartridges, Catalog # Spin-C18.T1.96) were activated using 200 µL acetonitrile (Honeywell B&J Brand™ Catalog #75-05-8) and washed with 200 µL 50% acetonitrile in 0.2% formic acid (v/v), followed by 200 µL 0.2% formic acid (v/v). Digested plasma samples containing tryptic peptides were added to the C18 cartridges and centrifuged at 1,200 rcf for one minute at 4˚ C. Columns were then washed with 200 µL 0.2% formic acid and centrifuged. Prior to elution, C18 cartridges were placed into 2.0 mL Lo-Bind microcentrifuge tubes (Eppendorf). Samples were then eluted with 200 µL 50% acetonitrile in 0.2% formic acid. The elution process was repeated and the eluate from both collections were combined into a new 1.5 mL Lo-Bind microcentrifuge tube and briefly frozen at -80˚ C. Frozen eluates were dried by SpeedVac until dry. Samples were stored at -80˚ C prior to resuspension and quantification. Peptides were resuspended in 150 µL 0.1% formic acid and quantified using the Pierce Quantitative Colorimetric Peptide Assay (ThermoFisher Scientific)."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Tryptic peptides were brought to a final concentration of 0.1 µg/µL in 0.1% formic acid (volume fraction) and were analyzed using a trap elute scheme on the UltiMate 3000 Nano LC coupled to a Fusion Lumos Orbitrap mass spectrometer (ThermoFisher Scientific). A volume equivalent to 500 ng of peptide was loaded onto a PepMap 100 C18 trap column (75 µm i.d. × 2 cm length; Thermo Fisher Scientific) at 3 µL/min for 10 min with 2% acetonitrile (volume fraction) and 0.05% trifluoroacetic acid (volume fraction). Peptides were subsequently separated on an Acclaim PepMap RSLC 2 µm C18 analytical column (75 µm i.d. × 25 cm length; Thermo Fisher Scientific) at 40 °C. As described in the attached methods files, peptides were separated along a 65 min two-step gradient of 5 to 30% mobile phase B [80% acetonitrile (volume fraction), 0.08% formic acid (volume fraction)] over 50 min followed by a ramp to 45% mobile phase B over 10 min and last to 95% mobile phase B over 5 min and held at 95% mobile phase B for 5 min, all at a flow rate of 300 nL/min. The Fusion Lumos was operated with a dynamic exclusion time of 60 s (10 ppm error) in positive ion mode with a 30% RF lens using data-dependent acquisition (topN, 3 s cycle time). Full MS scans were acquired over a mass range of m/z 375–1500 at a resolution of 60,000. The full scan ion target value was approximately 4.0 × 10⁵ with a maximum injection time of 50 ms. An intensity threshold of 2.5 × 10⁴ was used for precursor selection, including charge states 2–6 for monoisotopic peak determination. Data-dependent fragmentation was performed using higher-energy collisional dissociation (HCD) with a normalized collision energy of 32 and quadrupole isolation at a 1.3 m/z window. Fragment ions were analyzed in the Orbitrap at a resolution of 15,000 with an ion target value of 2.0 × 10⁵ and a maximum injection time of 30 ms. For comprehensive functional annotations of the Kemp’s ridley sea turtle proteome (rLepKem1.hap1, NCBI Refseq Assembly: GCF_965140285.1, 57,471 proteins) unique protein identities were aligned with their human equivalents using the HUGO Gene Nomenclature Committee (HGNC) gene symbols. This mapping process was facilitated by a Python script available at GitHub (https://github.com/neely/ChatGPT/tree/main/addGeneSymbol2RefSeq). In instances where a gene symbol and protein name was unavailable for significant protein identities UniProt’s BLAST (Basic Local Alignment Search Tool) was utilized for Testudinata (Uniprot ID 2841271) sequence similarity searches to assign appropriate gene symbols. Assignments were based on top similarity results showing at least 80% identity. Protein names for matching similarities were then aligned with their respective gene symbols using the HUGO Gene Nomenclature Committee (HGNC). In the two instances where a gene symbol was not available, the previously assigned “LOC” gene symbol remained. Raw files obtained from the mass spectrometer for eight randomized Kemp’s ridley plasma samples (two samples selected per group) were converted into peak lists as a .mgf file using the MSConvert software (v3.0.18205; available at https://github.com/phnmnl/container-pwiz). The databases used for the search were L. kempii; NCBI RefSeq rLepKem1.hap2; GCF_965140265.1-RS_2025_04, containing 59,884 sequences and the common Repository of Adventitious Proteins database (cRAP; v2012.01.01; Global Proteome Machine), containing 107 sequences. Using Mascot (v2.8.2), an error tolerance search was conducted on the merged .mgf files from the eight randomized plasma samples to implicate non-traditionally included peptide search modifications. The search parameters in Mascot were utilized as follows as seen in the included .par file: semiTrypsin was specified as the enzyme, allowing for up to two mis-cleavages. Carbamidomethylation on cysteine residues (C) was set as a fixed modification, while deamidation of asparagine and glutamine residues (NQ), cyclization of glutamine to form pyroglutamate (N-term Q), and oxidation on methionine residues (M) were set as variable modifications. The precursor mass tolerance (MS₁) was set to 10 ppm, and the product mass tolerance (MS₂) was set to 20 ppm, as calculated as four times the interquartile range generated in MetaMorpheus (v1.0.5; available at https://github.com/smith-chem-wisc/MetaMorpheus). The instrument type was specified as ESI-FTICR, and the decoy setting in Mascot was utilized to estimate the local false discovery rate (FDR). Peptide results were scored using the Scaffold 5 (v5.1.1, Proteome Software, Portland, OR, USA) local FDR algorithm. Protein and peptide FDR thresholds were set to 1% for positive identification with a minimum of one peptide."],"omics_type":["Proteomics"],"labhead":["Camille Berardone, Benjamin A. Neely, Michael G. Janech"],"instrument_platform":[""],"labhead_affiliation":["National Institute of Standards and Technology, NIST - Charleston"],"submission_type":["COMPLETE"],"species":["Lepidochelys Kempii"],"submitter_mail":["benjamin.neely@nist.gov"],"publication":["Not available"],"submitter_affiliation":["National Institute of Standards and Technology"],"submitter_country":["United States"],"doi":["10.6019/PXD079061"],"additional_accession":[]},"is_claimable":false,"name":"Proteomic analysis of plasma from rescued Kemp’s ridley sea turtles (Lepidochelys kempii) exposed to light and heavy degrees of oiling from the Deepwater Horizon oil spill","description":"In 2010, the Deepwater Horizon oil spill resulted in an estimated loss of 61,000–174,000 sea turtles in the Gulf of Mexico. Rescued Kemp’s ridley sea turtle exhibited adverse effects, including physiological stress and severe derangements. While prior studies evaluated health impacts of oil exposure, effects on plasma proteins remained largely unexplored. This study compared the plasma proteome of turtles from two oiling categories (OC) before and after rehabilitation. Plasma samples were collected from lightly oiled (n=9) and heavily oiled (n=15) turtles at admission and post-rehabilitation. Proteins were analyzed using label-free tandem mass spectrometry. At admission, few differences were observed between groups, with 17 proteins reduced in heavily oiled turtles relative to lightly oiled turtles. After rehabilitation, no significant differences were detected, suggesting normalization of the plasma proteome. Osteocalcin, a bone mineralization and metabolic hormone, displayed a large increase after recovery implicating a mechanistic role for this hormone in the recovery of sea turtles. Unexpectedly, alpha-fetoprotein was the most abundant plasma protein in 41 of 48 samples representing 20.2 ± 3.1% of the molar protein fraction surpassing albumin which is routinely measured for diagnostic evaluation. These findings demonstrate that plasma proteomics can distinguish oiling status and support future biomarker development.","dates":{"publication":"2026-05-29","submission":"2026-05-29"},"accession":"PXD079061","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","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:475174","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:383379","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","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: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: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:1182590","NEWT:3712","NEWT:3711","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:460523","NEWT:235443","NEWT:1757312","NEWT:85694","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:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","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:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","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:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:40674","NEWT:1194669","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","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:80863","NEWT:90675","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:90690","NEWT:1436183","NEWT:300273","NEWT:4232","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:7742","NEWT:196627","NEWT:200308","NEWT:200302","NEWT:870435","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NCBITaxon:5693","NEWT:28995","NEWT:1392998","NEWT:380394","NEWT:226900","NEWT:1266738","NEWT:231490","NEWT:244704","NEWT:7725","NEWT:9909","NEWT:99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