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In total, eight groups were selected for proteomic analysis (Supplementary file). The donor Lewis normal (DLN) and Brown Norway normal (DBNN) were selected as control groups and used for normalization of the respective implanted scaffolds. The samples were homogenized in the lysis buffer (50 mM triethylammonium bicarbonate (TEAB), 2% sodium dodecyl sulfate (SDS)), centrifuged, and supernatants transferred into new vials. Protein concentration was determined using Pierce™ BCA Protein Assay (Thermo Scientific). As reference samples, the controls DLN and DBNN were chosen to be analysed in both TMT sets. Aliquots containing 30 μg of each sample and the references were digested with trypsin using the filter-aided sample preparation (FASP) method (Wiśniewski, Zougman et al. 2009). Peptides were collected by centrifugation. Digested peptides were labelled using TMT 11-plex isobaric mass tagging reagents (Thermo Scientific) according to the manufacturer instructions. The combined samples of each of the two TMT sets were pre-fractionated with basic reversed-phase chromatography (bRP-LC) using a Dionex Ultimate 3000 UPLC system (Thermo Fischer Scientific). Peptide separations were performed using a reversed-phase XBridge BEH C18 column (3.5 μm, 3.0x150 mm, Waters Corporation) and a linear gradient from 3% to 40% solvent B over 17 min followed by an increase to 100% B over 5 min. Solvent A was 10 mM ammonium formate buffer at pH 10.00 and solvent B was 90% acetonitrile, 10% 10 mM ammonium formate at pH 10.00. The 40 fractions were concatenated into 20 fractions, dried and reconstituted in 3% acetonitrile, 0.2% formic acid. Liquid Chromatography-Tandem Mass Spectrometry Analysis The fractions were analyzed on an QExactive HF mass spectrometer interfaced with Easy-nLC1200 liquid chromatography system (Thermo Fisher Scientific). Peptides were trapped on an Acclaim Pepmap 100 C18 trap column (100 μm x 2 cm, particle size 5 μm, Thermo Fischer Scientific) and separated on an in-house packed analytical column (75 μm x 300 mm, particle size 3 μm, Reprosil-Pur C18, Dr. Maisch) using a gradient from 7% to 35% B over 76 min followed by an increase to 100% B for 8 min at a flow of 300 nL/min. The instrument operated in data-dependent mode where the precursor ion mass spectra were acquired at a resolution of 60 000, the 10 most intense ions were isolated in a 0.7 Da isolation window and fragmented using collision energy HCD settings at either 28 or 50. MS2 spectra were recorded at a resolution of 60 000, charge states 2 to 4 were selected for fragmentation and dynamic exclusion was set to 15 s with 10 ppm tolerance."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The data files for each TMT set were merged for identification and relative quantification using Proteome Discoverer version 2.2 (Thermo Fisher Scientific). The database search was performed using the Swissprot rat Database (Oct 2018) using Mascot 2.5.1 (Matrix Science) as a search engine with precursor mass tolerance of 5ppm and fragment mass tolerance of 200 mmu. Tryptic peptides were accepted with zero missed cleavage, variable modifications of methionine oxidation and fixed cysteine alkylation, TMT-label modifications of N-terminal and lysine were selected. Percolator was used for the validation of identified proteins and the quantified proteins were filtered at 1% FDR and grouped by sharing the same sequences to minimize redundancy. Reporter ion intensities were quantified in MS2 spectra using the S/N values as abundances and normalized on the total protein abundance within the Proteome Discoverer 2.2 workflow. Only peptides unique for a given protein were considered for quantification of the protein and ratios were calculated by dividing the samples with the reference samples DLN or DBNN. Only proteins quantified in all samples and relative standard deviation less than 25 percent in either syngeneic (LNSC, LNO, LDCSC, and LDCO) or allogeneic (BNNSC, BNNO, BNDCSC, and BNDCO) dataset were considered for comparisons among different sample groups. Proteins with two-fold expression changes were selected as up- or down- regulated."],"omics_type":["Proteomics"],"labhead":["Carina Sihlbom"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Proteomics Core Facility, University of Gothenburg"],"species":["Rattus Norvegicus (rat)","Rattus Rattus (black Rat)"],"submitter_mail":["carina.sihlbom@gu.se"],"publication":["34963315 Banerjee D, Nayakawde NB, Antony D, Deshmukh M, Ghosh S, Sihlbom C, Berger E, Ul Haq U, Olausson M. Characterization of Decellularized Implants for Extracellular Matrix Integrity and Immune Response Elicitation. Tissue Eng Part A. 2022 28(13-14):621-639 10.1089/ten.tea.2021.0146"],"submitter_affiliation":["Proteomics Core Facility / University of Gothenburg"],"submitter_country":["Sweden"],"pubmed_abstract":["Biological scaffold is a popular choice for the preparation of tissue-engineered organs and has the potential to address donor shortages in clinics. However, biological scaffolds prepared by physical or chemical agents cause damage to the extracellular matrix (ECM) by potentially inducing immune responses after implantation. The current study explores the fate of the decellularized (DC) scaffolds using a cocktail of chemicals following implantation without using immunosuppressants. Using the syngeneic (Lewis male-Lewis female) and allogeneic (Brown Norway male-Lewis female) models and different tissue routes (subcutaneous <i>vs.</i> omentum) for implantation, we applied in-depth quantitative proteomics, genomics along with histology and quantitative image analysis tools to comprehensively describe and compare the proteins following DC and postimplantation. Our data helped to identify any alteration postdecullarization as well implantation. We could also monitor route-specific modulation of the ECM and regulation of the immune responses (macrophage and T cells) following implantation. The current approach opens up the possibility to monitor the fate of biological scaffolds in terms of the ECM and immune response against the implants. In addition, the identification of different routes helped us to identify differential immune responses against the implants. This study opens up the potential to identify the changes associated with chemical DC both pre- and postimplantation, which could further help to promote research in this direction. Impact Statement The development of a biological scaffold helps in the preparation of a functional organ in the clinics. In the current study, we develop a strategy for chemical decellularization and explored two different routes to understand the differential responses elicited postimplantation. The use of sensitive protein and genomic tools to study the changes creates a favorable environment for similar efforts to develop and characterize biological scaffolds before further trials in the clinics. The current study, which was carried out without any immunosuppressive agents, could help to establish (a) appropriate chemical strategies for preparing biological scaffolds as well as (b) identify putative implantable routes to circumvent any adverse immune reactions, which will ultimately decide the outcome for acceptance or rejection of the scaffold/implant."],"pubmed_title":["Characterization of Decellularized Implants for Extracellular Matrix Integrity and Immune Response Elicitation."],"pubmed_authors":["Banerjee Debashish D, Nayakawde Nikhil B NB, Antony Deepti D, Deshmukh Meghshree M, Ghosh Sudip S, Sihlbom Carina C, Berger Evelin E, Ul Haq Uzair U, Olausson Michael M"],"additional_accession":[]},"is_claimable":false,"name":"Title- Modulation of implanted aortic scaffold- involvement of ECM and immune proteins","description":"Development of a suitable biological scaffold is an essential pre-requisite for functional development of organ including blood vessel. Biological scaffold prepared by conventional means using physical or chemical agent have been shown to cause damage to the extracellular matrix architecture as well as produce immune response subsequent to scaffold implantation/engraftment. During the current study, taking advantage of different host tissue environment (subcutaneous vs omentum), acellular scaffold was prepared using a syngeneic vs allogeneic model of scaffold implantation (in vivo decellularization) and compared with a chemically decellularized scaffold. By means of molecular, proteomics and histologic techniques, we confirmed that site specific advantages exist in modulating the ECM as well as regulating the immune response (macrophage and T-cells) to produce an acellular scaffold without the need for immunosuppressants. The current approach opens up the possibility for creation of tailor made scaffold for further use in the clinics with a possibility for long term acceptability without adverse reactions in the host and a further possibility to build functional organs following cell engraftment.","dates":{"publication":"2026-07-06","submission":"2020-08-28"},"accession":"PXD021179","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","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:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:112509","NEWT:475174","NEWT:111205","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NEWT:1748418","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:1907535","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:2086595","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","NEWT:111225","NEWT:7719","NEWT:29073","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:2020713","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:55350","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:37919","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:329854","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","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:3715","NEWT:1538","NEWT:2065263","NEWT:199225","NEWT:177437","NEWT:717966","NEWT:10891","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:9006","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:2714896","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2499525","NEWT:1122981","NEWT:2853422","NEWT:1122984","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:31345","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:299467","NEWT:9541","NEWT:51350","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:20734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