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Wilmarth"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"disease":["Glaucoma"],"software":["Not available"],"submitter_keywords":["Human","Glaucoma","Cell culture","Quantitative proteomics","Trabecular meshwork","Extracellular matrix","Isobaric labeling","Mass spectrometry"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD066598"],"tissue":["Eye","Trabecular Meshwork Cell"],"sample_protocol":["A total of 18 primary trabecular meshwork cell strains were used in this study (biological replicates). Nine cell strains were from non-glaucomatous human donor eyes, while 9 cell strains were from those with an ocular history of glaucoma. For TMT mass spectrometry experiments, we used n=5 non-glaucomatous (NTM) and n=5 glaucomatous (GTM) cell strains.  Primary TM cells were cultured from donor eyes that were age and sex matched. All studies followed the principles outlined in the Declaration of Helsinki. All cell strains have been characterized by their ability to up-regulate myocilin expression in response to dexamethasone treatment. For proteomics experiments, non-glaucomatous (NTM) and glaucomatous (GTM) cells were used at passage number 3  Pelleted cell samples were prepared by adding 200 microliters of 5% sodium dodecyl sulfate (SDS) and 40-50 mg of acid-washed glass beads, which were previously rinsed in dH2O. Cells were homogenized by bead-beating at 4C in a Bertin Precellys Evolution Bead Beater (6 cycles of 15 sec at 6800 rpm with a 30 sec pause between cycles). Samples were then heated to 70C for 10 min, centrifuged for 5 min at 8000xg, and sonicated in a Diagenode Bioruptor Pico with the following conditions (30 sec on, 30 sec off, 10 cycles). After centrifugation at 12,000xg for 10 min, the protein concentration in each sample was measured by BCA assay (ThermoFisher).  SDS protein extraction buffer (5% SDS, 50 mM TEAB (pH7.5) and 22 mM DTT was then added to each sample and incubated for 10 min at 95C. Samples were alkylated by adding 40 mM IAA (final concentration) and incubated at room temp in the dark for 30 min. Phosphoric acid (1.2% final concentration) and 6x volume of S-Trap protein binding buffer (90% aqueous methanol containing 100 mM TEAB, pH7.5) was added to each sample. The mixture was then loaded into the S-Trap micro column and centrifuged for 3 min at 4,000xg. Captured protein was washed 5 times with S-Trap protein binding buffer and then 40 µl of digestion buffer (80 ng/µL trypsin in 50 mM TEAB at a 1:16 enzyme: substrate ratio) was loaded into the top of the micro column, which was loosely capped and incubated overnight at 37 oC. The next day, 100 µl HPLC-grade H2O was added, the columns were shaken for 10 min, and the column spun at 12,000xg for 5 min to elute the digested peptides. Concentration was determined with a Pierce peptide assay kit and samples were dried by vacuum centrifugation.  A tandem mass tag (TMTpro) 18-plex reagent kit (ThermoFisher Scientific) was used to label the digested peptide samples. Each TMTpro 18-plex reagent (200 microgram) dissolved in 12 microliters of anhydrous acetonitrile was added to 15 micrograms of peptide sample in 20 microliters of 100mM TEAB, and labeling performed by shaking at room temp for 1h. After the incubation, 2 microliters of each labeled peptide digest were combined; 2 microliters of 5% hydroxylamine added, and samples incubated at room temp for 15 min, then dried by vacuum centrifugation. The remaining volume of each labeled sample was frozen at −80 °C without hydroxylamine addition (in case relabeling was required).  The 2 microliters of each combined TMTpro labeled sample was then dissolved in 20 microliters of 5% formic acid and 2 micrograms of peptides analyzed using a 140 min LC-MS/MS method on an Orbitrap Fusion Mass Spectrometer to determine the volume of each sample to provide equal total reporter ion intensities in the combined sample for the 2D-LC/MS analysis. The TMTpro labeled samples were thawed and calculated aliquots removed that would produce 50 micrograms of total peptides from all 18 samples. To quench the labeling reaction, 5% hydroxylamine was added to bring the total hydroxylamine concentration to 0.5% followed by incubation for 15 min at room temperature.  The multiplexed samples were dissolved in 10 mM ammonium formate, pH9 buffer and injected onto a NanoEase 5-micron XBridge BEH130 C18 300 micron × 50 mm column (Waters Corporation, Milford, MA) at 3 microliters/min in a mobile phase containing 10 mM ammonium formate (pH 9). Peptides were eluted by sequential injection of 20 microliter volumes of 17, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 40, 50, 90% ACN (20 fractions). Eluted peptides were diluted at a 3-way union with mobile phase containing 0.1% formic acid at a 24 microliters/min flow rate and delivered to an Acclaim PepMap 100 micron × 2 cm NanoViper C18, 5-micron trap (Thermo Fisher Scientific) on a switching valve. After 10 min of loading, the trap column was switched on-line to a PepMap RSLC C18, 2-micron, 75 micron × 25 cm EasySpray column (ThermoFisher Scientific). TMTpro 18-plex labeled peptides were then separated at low pH in the second dimension using a 5–25% ACN gradient over 140 min in the mobile phase containing 0.1% formic acid at a 300 nL/min flow rate."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Tandem mass spectrometry data was collected using an Orbitrap Fusion Tribrid instrument configured with an EasySpray NanoSource (Thermo Scientific, San Jose, CA). Survey scans were performed in the Orbitrap mass analyzer at resolution = 120,000, with internal mass calibration enabled, and data-dependent MS2 scans using dynamic exclusion performed in the linear ion trap using collision-induced dissociation. Reporter ion detection was performed in the Orbitrap mass analyzer (resolution = 50,000) with higher-energy collisional dissociation in the ion-routing multipole using MS3 scans after synchronous precursor isolation of the top 10 fragment ions in the linear ion trap.   The 20 binary instrument files were processed with the PAW pipeline (https://github.com/pwilmart/PAW_pipeline). Binary files were converted to text files using MSConvert. Python scripts extracted TMT reporter ion peak heights and fragment ion spectra in MS2 format. The Comet search engine (version 2016.03) was used: 1.25 Da monoisotopic peptide mass tolerance, 1.0005 Da monoisotopic fragment ion tolerance, tryptic cleavage with up to three missed cleavages, variable oxidation of methionine residues (+15.9949 Da), static alkylation of cysteines (+57.0215 Da), and static modifications for TMTpro labels (+304.2071 Da at peptide N-termini and at lysine residues). Searches used UniProt proteome UP000005640 (Homo sapiens, taxon ID 9606) canonical FASTA sequences (20,593 proteins, downloaded June 2023). Common contaminants (175 sequences excluding any albumins) were added, and sequence-reversed entries were concatenated for a final protein FASTA file of 41,536 sequences. Top-scoring peptide spectrum matches (PSMs) were filtered to a 1% false discovery rate (FDR) using interactive delta-mass and conditional Peptide-prophet-like linear discriminant function scores. Incorrect delta-mass and score histogram distributions were estimated using the target/decoy method. The filtered PSMs (129,424 scans) were assembled into protein lists using basic and extended parsimony principles and required two distinct peptides per protein. The final list of identified proteins, protein groups, and protein families (5,518 total) were used to define unique and shared peptides for quantitative use. Total (summed) reporter ion intensities were computed from the PSMs associated with all unique peptides for each protein.   The protein intensity values for each biological sample in each biological condition were compared for differential protein expression using the Bioconductor package edgeR and the Trimmed Mean of M-values (TMM) biological normalization function. Benjamini-Hochberg corrected p-values (FDR) of less than 0.1 were considered as candidates for differential relative abundance."],"omics_type":["Proteomics"],"labhead":["Kate E. Keller, Ph.D."],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Department of Ophthalmology School of Medicine Oregon Health & Science University Portland, OR 97239 USA"],"species":["Homo Sapiens (human)"],"publication":["41851243 Holden P, Sun YY, Zientek K, Wilmarth PA, Reddy AP, Keller KE. Isobaric quantitative proteomics reveals altered extracellular matrix, cytoskeletal, and degradation pathways in glaucomatous trabecular meshwork cells. Sci Rep. 2026 10.1038/s41598-026-44561-x"],"submitter_mail":["wilmarth@ohsu.edu"],"submitter_affiliation":["OHSU"],"submitter_country":["United States"],"pubmed_title":["Isobaric quantitative proteomics reveals altered extracellular matrix, cytoskeletal, and degradation pathways in glaucomatous trabecular meshwork cells."],"pubmed_authors":["Holden Paul P, Sun Ying Ying YY, Zientek Keith K, Wilmarth Phillip A PA, Reddy Ashok P AP, Keller Kate E KE"],"additional_accession":[]},"is_claimable":false,"name":"Identification of differentially abundant proteins in glaucomatous and non-glaucomatous trabecular meshwork cell cultures using isobaric multiplexed quantitative proteomics","description":"Glaucoma trabecular meshwork (GTM) cells cultured in vitro retain many characteristics of their in situ phenotype. We used isobaric labeling quantitative proteomics to identify proteins that were differentially regulated between glaucomatous and age-matched non-glaucomatous TM (NTM) cells. NTM (n=5) and GTM cells (n=5) were grown to confluence, placed in serum-free media for 3 days, and scraped cells then were lysed by bead beating in 5% SDS. Equal amounts of protein were reduced, alkylated, and digested with trypsin and peptides were labeled with 18-plex tandem mass tags (TMTpro). After combining samples, they were fractionated on an Orbitrap Fusion mass spectrometer. Data was processed using the PAW/Comet pipeline and EdgeR with Benjami-Hochberg multiple correction testing (p<0.05). Pathway enrichment analysis was done. Western immunoblotting and immunofluorescence validations were performed. Analysis of the NTM and GTM biological replicates identified 206 proteins that were significantly up-regulated in GTM cells, 42 proteins that were down-regulated, with 5270 non-candidates. Interestingly, there were 18 proteins that were not detected in any of the NTM cell strains but produced abundant reporter ion intensities in GTM cells. Significant regulated pathways included the Wnt and TGFb pathways, protein degradation, actin cytoskeletal regulation, and nuclear proteins. Western immunoblotting studies agreed with the TMT 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