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Protein G-sepharose 4FF beads were then added and the SD-supts were incubated another 30 min at 4°C on a rotating wheel, prior to centrifugation in a microfuge (10 min, 4°C, maximum speed). The resulting, pre-cleared SD-supts were incubated with 1 µg/ml of antibody raised against a protein of interest (overnight, 4°C, on a rotating wheel), prior to further incubation with protein G-sepharose beads (60 min, 4°C, on a rotating wheel) and centrifugation in a microfuge (10 min, 4°C, maximum speed). The resulting immunoprecipitates were washed once, aliquoted, snap-frozen in liquid nitrogen, and kept at -20°C until mass spectrometry analysis; whereas the resulting supernatants were aliquoted, snap-frozen in liquid nitrogen, and kept at -20°C until later use as NET stimulus.  Reduction, alkylation and digestion of proteins All buffers used from this stage were prepared with MS grade water. The protein reduction step was carried out by incubating the beads in 100 μl of 20 mM ammonium bicarbonate buffer containing 10 mM DTT (Thermo Fisher Scientific, Waltham, USA) with stirring (1250 rpm) for 30 minutes at 60 °C. The alkylation of the proteins was carried out by adding another volume of 100 μl of 20 mM ammonium bicarbonate buffer, and then supplementing to 15 mM IAA (Sigma-Aldrich, Saint-Louis, United States) final before stirring for 1 hour at room temperature away from light. The IAA was then neutralized by completing 15mM DTT and stirring for 10 minutes at 37 ° C. The proteins were digested by adding 1 μg Pierce MS-grade trypsin (Thermo Fisher Scientific, Waltham, USA) and incubated overnight at 37 ° C with shaking. Purification and desalting of the peptides on C18 columns Digestion was stopped by adding 1% formic acid (FA) (Thermo Fisher Scientific, Waltham, USA) to a total volume of 200 μl, followed by stirring for 5 minutes at room temperature. The beads were spun at 6000 x g for 3 minutes before harvesting the supernatant and transferring to a new low binding microtube. The beads were resuspended in 200 .mu.l of buffer containing 60% acetonitrile (ACN) (Sigma-Aldrich, St. Louis, USA) and 0.1% FA, and then stirred for 5 minutes at room temperature. The supernatant was harvested and combined with that obtained previously. These samples were concentrated by a centrifugal evaporator at 65 ° C until complete drying (approximately 2 hours), and resuspended in 30 μl of 0.1% trifluoroacetic acid (TFA) buffer (Sigma-Aldrich, St. Louis, USA). United). The peptides were purified with ZipTip micropipette tips of 10 μl format containing a C18 column (EMD Millipore, Burlington, USA). The ZipTip was first moistened by suctioning 10 μl of 100% ACN solution three times, then equilibrated by suctioning 10 μl of 0.1% TFA buffer three times. Each sample of peptides was passed on the balanced ZipTip by succeeding up-and-downs of 10 μl of the sample 10 times. This step was performed three times in order to pass the entire sample on the column. The ZipTip was then washed with 10 μl of 0.1% TFA buffer three times. The elution of the peptides was made in a new low-binding microtube, 10 times with a volume of 10 μl of buffer 50% ACN and 0.1% FA. This step was carried out three times to obtain a final volume of 30 μl. The peptides were concentrated by centrifugal evaporator at 65 ° C. until complete drying (approximately 30 minutes) and then resuspended in 25 μl of 1% FA buffer. Peptides were assayed using a NanoDrop spectrophotometer (Thermo Fisher Scientific, Waltham, USA) reading the absorbance at 205 nm. The peptides were then transferred to a glass vial (Thermo Fisher Scientific, Waltham, USA) and stored at -20 ° C until analyzed by mass spectrometry."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["LC-MS/MS analysis Trypsin digested peptides were separated using a Dionex Ultimate 3000 nanoHPLC system. 10 μl of sample (a total of 2 μg) in 1% (vol/vol) formic acid was loaded with a constant flow of 4 μl/min onto an Acclaim PepMap100 C18 column (0.3 mm id x 5 mm, Dionex Corporation). After trap enrichment peptides were eluted off onto an EasySpray PepMap C18 nano column (75 μm x 50 cm, Dionex Corporation) with a linear gradient of 5-35% solvent B (90% acetonitrile with 0.1% formic acid) over 240 minutes with a constant flow of 200 nl/min. The HPLC system was coupled to an OrbiTrap QExactive mass spectrometer (Thermo Fisher Scientific Inc) via an EasySpray source. The spray voltage was set to 2.0 kV and the temperature of the column was set to 40 oC. Full scan MS survey spectra (m/z 350-1600) in profile mode were acquired in the Orbitrap with a resolution of 70,000 after accumulation of 1,000,000 ions. The ten most intense peptide ions from the preview scan in the Orbitrap were fragmented by collision induced dissociation (normalised collision energy 35% and resolution of 17,500) after the accumulation of 50,000 ions. Maximal filling times were 250 ms for the full scans and 60 ms for the MS/MS scans. Precursor ion charge state screening was enabled and all unassigned charge states as well as singly, 7 and 8 charged species were rejected. The dynamic exclusion list was restricted to a maximum of 500 entries with a maximum retention period of 40 seconds and a relative mass window of 10 ppm. The lock mass option was enabled for survey scans to improve mass accuracy. Data were acquired using the Xcalibur software. Protein identification by MaxQuant analysis The raw files were analyzed using the MaxQuant version 1.6.2.2 software (Cox and Mann, 2008) and the Uniprot human database (16/07/2013). Analyzes were initially performed separately for each isoform to obtain enrichment ratios for the complete sequence of each. A common analysis was then performed to integrate all raw MS / MS analysis files. The MaxQuant software default settings were used, except for the following parameters: multiplicity of 3 SILAC media (R0K0, R6K4 and R10K8), identification values \"PSM FDR\", \"Protein FDR\" and \"Site decoy fraction\" 0.05, minimum ratio count of 1 and selection of the \"Re-quantify\" option. Following the analysis, the results were sorted according to several parameters. Proteins positive for at least one of the Reverse, Only identified by site and Potential contaminants categories were eliminated, as well as proteins identified from a single peptide. The ratios identified in only one of the three replicas for each experiment were eliminated. The ratios identified in two of the three replicas were eliminated when they were considered to be too divergent, ie when the standard deviation was greater than the average of the two enrichment ratios. Outliers for the ratios measured in the three replicas were detected using the Grubbs test at a value of α = 0.05 and then eliminated. Following this sorting, proteins for which no ratio was calculated in at least one experiment were removed."],"omics_type":["Proteomics"],"labhead":["Patrick McDonald"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Pulmonary Division, CRCHUS, Universite de Sherbrooke, Sherbrooke, QC, Canada."],"species":["Homo Sapiens (human)"],"publication":["42305534 de Carvalho Oliveira V, Mazur M, McDonald PP. A feedback loop sustaining neutrophil extracellular trap formation involves S100 proteins, histones, TLR2 and RAGE, and is restrained by albumin. Front Immunol. 2026 17:1774475 10.3389/fimmu.2026.1774475"],"submitter_mail":["vanessa.oliveira@usherbrooke.ca"],"submitter_affiliation":["Université de Sherbrooke"],"submitter_country":["Canada"],"pubmed_abstract":["Neutrophil extracellular trap (NET) generation must be tightly controlled as this essential antimicrobial response can also cause tissue damage and contribute to various pathologies. We previously described that neutrophils undergoing NET formation release endogenous mediators that feedback on the cells via the RAGE receptor to drive the response. We now identify S100 proteins and histones as prominent endogenous NET inducers. Mass spectrometry analyses of culture supernatant from NETing neutrophils revealed the presence of seven species of S100 proteins and ten histone variants, all of which could bind to RAGE. In addition, endogenous NET inducers were found to act via TLR2 since antagonism of the receptor for up to 3 h post-stimulation hindered NET formation elicited by various classes of physiological stimuli. By comparison, antagonism of TLR4 did not inhibit NET generation. Conversely, we show that serum or equivalent albumin concentrations restrain NET formation by sequestering endogenous NET inducers. Serum depleted of albumin indeed loses its ability to prevent NET formation; likewise, the belated addition of HSA to culture medium blocks NET generation. Prior exposure to serum or albumin renders endogenous NET inducers unable to trigger the response; mass spectrometry analyses confirmed that albumin captures S100 proteins. Collectively, our data unveil a feedback loop of NET formation involving endogenous S100 proteins and histones, acting through RAGE and/or TLR2, that can be physiologically counteracted by albumin."],"pubmed_title":["A feedback loop sustaining neutrophil extracellular trap formation involves S100 proteins, histones, TLR2 and RAGE, and is restrained by albumin."],"pubmed_authors":["de Carvalho Oliveira Vanessa V, Mazur Matthew M, McDonald Patrick P PP"],"additional_accession":[]},"is_claimable":false,"name":"A feedback loop sustaining neutrophil extracellular trap formation involves S100 proteins, histones, TLR2 and RAGE, and is restrained by albumin","description":"Neutrophil extracellular trap (NET) generation must be tightly controlled as this essential antimicrobial response can also cause tissue damage and contribute to various pathologies. We previously described that neutrophils undergoing NET formation release endogenous mediators that feed back on the cells via the RAGE receptor to drive the response. We now identify S100 proteins and histones as prominent endogenous NET inducers. Mass spectrometry analyses of culture supernatant from NETing neutrophils revealed the presence of seven species of S100 proteins and 10 histone variants, all of which could bind to RAGE. In addition, endogenous NET inducers were found to act via TLR2 since antagonism of the receptor for up to 3 h post-stimulation hindered NET formation elicited by various classes of physiological stimuli. By comparison, antagonism of TLR4 did not affect NET generation. Conversely, we show that serum or equivalent albumin concentrations restrain NET formation by sequestering endogenous NET inducers. Serum depleted of albumin indeed loses its ability to prevent NET formation; likewise, the belated addition of HSA to culture medium blocks NET generation. Prior exposure to serum or albumin renders endogenous NET inducers unable to trigger the response; mass spectrometry analysis confirmed that albumin captures S100 proteins. Collectively, our data unveil a feedback loop of NET formation involving endogenous S100 proteins and histones, acting through RAGE and/or TLR2, that can be physiologically counteracted by albumin.","dates":{"publication":"2026-06-29","submission":"2026-05-21"},"accession":"PXD078688","cross_references":{"TAXONOMY":["NEWT:68239","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:2492962","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:156587","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:118221","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","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:2709072","NEWT:2499525","NEWT:467144","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:2423","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:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","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:1325292","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:595495","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:38323","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:510516","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:483179","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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