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Extraction and culturing protocols were identical to previously reported protocols (Porro et al, 2023).  4.2 Cell-membrane protein capture Endothelial cell-membrane proteins were labelled with biotin through conjugation with the cell-membrane impermeable reagent sulfo-biotin-NHS (ThermoFisher, A39257). Following incubation (in appropriate cell-culture medium, 37oC) for specific time-points, biotinylated proteins remaining on the cell-membrane were captured by conjugation to streptavidin-coated agarose microbeads. Following blocking of remaining available streptavidin sites on the bound microbeads with excess free biotin, cells were lysed (lysis buffer with 10% protease inhibitors). Lysates were collected into centrifugation filter tubes and microbead-captured biotinylated proteins separated from free proteins by through centrifugation according to the manufacturer protocol (ThermoFisher, biotinylated protein interaction pull-down kit, cat no. 2115). Following washing of separated microbeads with acetate wash buffer (pH 5) and 0.5M NaCl, microbeads were recovered in ammonium bicarbonate buffer (50mM, pH 8) and frozen (-80oC) until mass spectrometry analysis.  4.3 On-bead tryptic protein digestion Biotinylated proteins on thawed agarose microbeads were digested with trypsin and separated by centrifugation. Supernatant containing protein fragments was acidified (formic acid, 1%) and samples cleaned with C18 desalting spin columns (MonoSpin S type, GL Sciences) and subsequently with SCX tips following manufacturer protocols. Peptides were eluted with 5% ammonium hydroxide in 30% methanol, dried (Speed Vac) and stored at -20oC. For Liquid Chromatography-Mass Spectrometry (LC-MS) injection, dried eluates were reconstituted in 3% ACN/1% FA and loaded onto Evotips with an internal peptide standard mix (iRT kit, Biognosys) for MS quantification.  4.4 LC-MS/MS procedure Mass spectrometry was performed on an Orbitrap Eclipse Tribrid mass spectrometer (ThermoFisher Scientific, San Jose, CA) connected to an EVOSEP One (EVOSEP, Odense, Denmark) via a nanoEasy Spray Source interface with a stainless-steel emitter (EV-1086 EVOSEP). Tryptic peptides were loaded onto the EVOTIP (EV-2013 EVOSEP) following the manufacturer's instructions. The analytical column was a 15cm x 150µm ID, with Dr Maisch C18 AQ. 1.5 µm beads (EV-1137 EVOSEP), placed into a column oven at 40ºC. The eluents were 0.1% formic acid in water and 0.1% formic acid in acetonitrile. The Evosep One method was 15 SPD (88 min gradient), and the flow rate 0.22 µl/min. The mass spectrometer was operated in data independent acquisition mode (DIA). Full MS1 scans were acquired in the Orbitrap with a scan range of 350 - 1200 m/z and a resolution of 120,000 (at 200 m/z). Automatic gain control (AGC) was set to a target of 1 x 106 and a maximum injection time of 56 ms. MS2 spectra were acquired in DIA using 33 m/z variable windows with 0.5 m/z overlap. MS2 spectra were analyzed in the Orbitrap with a resolution of 30,000 (at 200 m/z). A higher energy collision induced dissociation (HCD) method (28% NCE) was applied with an AGC target of 5x104 and a maximum injection time of 55 ms. Orbitrap Eclipse Tune Application 3.5.3890 and Xcalibur version 4.5.445.18 were used to operate the instrument and to acquire data, respectively."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["4.5 LC-MS Data analysis Spectrum files were analyzed using DIA by Neural Networks software (DIA-NN, v1.9.2) (Demichev et al, 2020), searching against UniProt reference proteome of Rattus Norvegicus (retrieved on June, 2024) and common contaminants (Frankenfield et al, 2022). An independent DIA-NN search was carried out for each tissue-specific data subset, with constant search parameters throughout. Protein N-terminal acetylation, methionine oxidation and methionine excision at protein N-terminal were accepted as variable modifications. The maximum number of tryptic missed cleavages and number of variable modifications allowed were 2 and 1, respectively. The m/z range for the precursors and the fragment ions were set to 350 - 1200 and 200 - 2000, respectively. The match between runs option and the heuristic algorithm for the protein inference were also enabled. The remaining DIA-NN parameters were kept at their default values. The R package ‘diann-rpackage’ was used to generate protein group MaxLFQ (Cox et al, 2014) quantifications prior to filtering by q-value below or equal to 0.01, and the resulting datasets were further pre-processed, analysed and visualized with the R. In particular, contaminant protein groups were filtered out and the resulting protein group quantification values were log2-transformed, normalized using the cyclic LOESS algorithm implementation included in the ‘limma’ R package, and filtered requiring at least two peptides per protein group. Protein abundance was quantified and plotted for each time-point (0, 1, 2, 4, 8, 24 hr) and ETOR calculated from the inverse of the slope. All results comparing ‘Abundance’ and ‘ETOR’ employed the abundance of the 0h time-point."],"omics_type":["Proteomics"],"labhead":["Marta Vilaseca"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Mass Spectrometry & Proteomics Core Facility (MSPCF) Institute for Research in Biomedicine (IRB Barcelona) Barcelona Institute of Science and Technology (BIST) C/ Baldiri Reixac, 10-12 08028 Barcelona - Spain."],"species":["Rattus Norvegicus (rat)"],"publication":["Not available"],"submitter_mail":["masspe@irbbarcelona.org"],"submitter_affiliation":["Mass Spectrometry & Proteomics Core Facility (MSPCF)\nInstitute for Research in Biomedicine (IRB Barcelona)\nBarcelona Institute of Science and Technology (BIST)\nC/ Baldiri Reixac, 10-12\n08028 Barcelona - Spain"],"submitter_country":["Spain"],"additional_accession":[]},"is_claimable":false,"name":"Endocytic Turnover of Endothelial Cell-Membrane Proteins as a Driver of Blood Brain Barrier Specialization and Dysfunction","description":"The blood-brain barrier (BBB), formed primarily by specialized brain endothelial cells (BEC), exerts essential functions for proper brain activity, including nutrient transport, signal transduction, immune cell transmigration and pathogen restriction. While these functions are known to be regulated by the identity and abundance (i.e. composition) of cell-membrane proteins, a parameter which remains underexplored is how protein endocytic turnover rate (ETOR)—the rate of protein internalization from the cell membrane— governs BBB physiology. Employing high-throughput in vitro proteomics, we quantify the ETOR of large protein arrays (c. 1000 individual proteins) across endothelial phenotypes and pathological states to examine the mechanisms driving BBB specialization and the changes underlying BBB dysfunction. We find that BEC possess a specialized ETOR profile which differentiates them from peripheral endothelial cells beyond their cell-membrane protein composition. In addition, we demonstrate that inflammatory conditions disrupt the endocytic rates of BEC to a greater degree than disruptions in protein abundance, shifting the specialized ETOR profile of BEC towards a peripheral phenotype. Furthermore, we demonstrate that, while inflammation-induced changes in protein abundance identify proteins strongly involved in immune response, inflammation-induced changes in ETOR identifies proteins strongly involved in vasculature remodelling. Together, our results indicate that the ETOR of cell-membrane proteins is an important parameter driving the specialization of the BBB which becomes disrupted during pathological conditions independently of cell-membrane protein composition. Furthermore, it highlights that ETOR changes identify pathological mechanisms underlying BBB dysfunction not identified by changes in protein abundance.","dates":{"publication":"2026-05-15","submission":"2025-08-08"},"accession":"PXD067112","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:3765","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","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:28174","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:55784","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:491","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","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:906914","NEWT:9031","NEWT:27292","NEWT:1050722","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: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:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:443906","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: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:48106","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",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