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Per sample each 10 µg of purified mouse tail collagen were reduced by addition of dithiothreitol to a final concentration of 2 mM and incubation at 60 °C for 10 min. After equilibration to room temperature, iodoacetamide was added to a final concentration of 6 mM and incubated for 30 min at RT in the dark, followed by tryptic digest (Promega) at 1:20 ratio at 37 °C for overnight (18 h). Samples were acidified with trifluoroacetic acid and stored at −20 °C before mass spectrometry analyses. LC-MS/MS analysis was performed as described previously on a Q-Exactive HF mass spectrometer online coupled to an Ultimate 3000 nano-RSLC (Thermo Scientific) (Merl-Pham et al. 2019). Briefly, approximately 0.3 μg of purified collagen sample was loaded onto the trap column and after 5 min eluted and separated on the C18 analytical column (nanoEase M/Z HSS T3 Column, 100Å pore size, 1.8 µm particles, 75 µm I.D. X 250 mm length, Waters) by a 90 min non-linear acetonitrile gradient. MS and MSMS spectra were recorded as described."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The acquired spectra were analyzed in the MaxQuant software (version 2.3.0.1, MPI Biochemistry Martinsried) applying default settings. Searches were performed within the MaxQuant software using the Andromeda search engine against the Swissprot mouse protein database (Release 2020_02, 17061 sequences) additionally allowing for oxidation of proline and lysine as variable modifications. LFQ (ratio count 1, iBAQ and TOP3 quantification based on unique peptides were included. Identifications were filtered for a peptide-spectrum-match and protein false discovery rate of each 1%. The resulting list of protein groups including intensities, LFQ intensities, iBAQ and TOP3 values were used for calculation of sample purity and chain stoichiometries. The MyriMatch (Tabb et al. 2007) database search engine was utilized for the identification of site-specific collagen PTMs (hydroxylation of proline and lysine, O-glycosylation of hydroxylysine)."],"omics_type":["Proteomics"],"labhead":["Claudia A."],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Institute of Lung Health and Immunity (LHI), Helmholtz Munich, Comprehensive Pneumology Center (CPC-M), Germany, Member of the German Center for Lung Research (DZL); Department of Pediatrics, University of Colorado Anschutz Medical Campus, Aurora, CO, USA"],"species":["Mus Musculus (mouse)"],"publication":["10.1016/J.JBC.2026.111422"],"submitter_mail":["claudia.staab-weijnitz@cuanschutz.edu"],"submitter_affiliation":["University of Colorado, Anschutz Medical Campus"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Site-specific quantification of collagen post-translational modifications reveals profound disruption of the collagen biosynthetic network upon prolyl-3-hydroxylase 1 deficiency","description":"Type I collagen is the main structural protein in mammals and other vertebrate life forms. During the biosynthesis of collagens, prolyl-3-hydroxylase 1 (P3H1) catalyzes 3-hydroxylation of proline residues and acts as a chaperone. Deficiency of P3H1 causes Osteogenesis Imperfecta (OI), a hereditary disorder primarily associated with mutations in type I collagen and collagen-related genes. However, the full impact of P3H1 deficiency on the collagen biosynthesis machinery and post-translational modifications (PTMs) is not known. In this comprehensive study, we conducted a detailed investigation of P3h1 knockout mice collagen by performing amino acid analysis, high-resolution tandem mass spectrometry (MS/MS)-based identification and site-specific quantification of collagen PTMs, and gene expression analysis to unravel the impact of P3H1 deficiency on type I collagen biosynthesis in mouse tail tendon. Amino acid analysis revealed a general overmodification of prolines and lysines in mouse tendon type I collagen. Site-specific MS/MS-based quantification of collagen PTMs verified the P3H1-dependent 3-hydroxyproline sites COL1A1-P1153 and COL1A2-P803, but demonstrated frequent overhydroxylation of prolines, including 3- and 4-hydroxylation, as well as increased 5-hydroxylation of lysines in unprecedented detail. Gene expression analysis in P3H1-deficient mouse tail tenocytes unveiled upregulation of Col1a1 expression along with several other genes encoding collagen biosynthetic enzymes. Interestingly, upregulation of P4ha2 expression stood out and correlated with specific overhydroxylation of prolyl-4-hydroxylation sites containing the P4HA2 preferred motif EPG. In summary, the loss of P3H1 led to a profound imbalance in the entire ER-resident collagen biosynthetic machinery and drastically altered the collagen I PTM network. In conclusion, our findings offer a novel mechanism underlying overmodification in addition to prolonged exposure of unfolded collagen chains in the ER, suggest the presence of so far unknown feedback mechanisms between ER-resident collagen biosynthesis and collagen biosynthetic gene expression, and further emphasize the essential role of P3H1 in maintaining collagen quality 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