{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067688/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067688/XA02350B2SA_Aor_dbAA2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067688/XA02350B2SA_Aor_mTA3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067688/XA02350B2SA_Aor_dbAA4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067688/XA02350B2SA_Aor_dbTA1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067688/XA02350B2SA_Aor_mAA4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067688/XA02350B2SA_Aor_dbTA4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067688/XA02350B2SA_Aor_mAA3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067688/XA02350B2SA_Aor_dbTA2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067688/XA02350B2SA_Aor_mTA1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067688/XA02350B2SA_Aor_mAA1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067688/XA02350B2SA_Aor_dbAA3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067688/XA02350B2SA_Aor_mTA4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067688/XA02350B2SA_Aor_dbAA1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067688/XA02350B2SA_Aor_dbTA3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067688/XA02350B2SA_Aor_mAA2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067688/XA02350B2SA_Aor_mTA2.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067688/result.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["superandy333@gmail.com"],"submitter":["Chak Kwong Cheng"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Aorta; diabetes mellitus; obesity; proteomic","proteomic","Aorta","diabetes mellitus","obesity"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067688"],"sample_protocol":["Laser-capture microdissection (LCM) was conducted using the Zeiss PALM LCM System: the system was first powered on for 15 minutes to stabilize laser energy, then configured with microscope/laser settings (zoom: 20x; cut energy: 39, focus: 62; catapulting energy: 64, focus: 70; cycle number: 1; cut speed: 100). A dried H&E-stained aortic section slide was placed on the LCM microscope’s slide adapter, regions of interest were marked with an LCM marker pen, microdissected using the above settings, and collected into Zeiss microtubes (415190-9201-000). The microdissected samples were resuspended in 5 μL of lysis buffer and sonicated for 3 minutes using a high-intensity, contactless ultrasonic processor (Scientz, Zhejiang, China). The lysates were then incubated at 95°C for 10 minutes. After cooling to room temperature, 5 mmol/L dithiothreitol was added, and the mixture was incubated at 56°C for 30 minutes to facilitate reduction. Next, 11 mmol/L iodoacetamide was added, followed by a 15-minute incubation at room temperature in the dark. For protein digestion, 10 ng/μL trypsin was added to the samples, which were then digested overnight at 37°C . Following digestion, the resulting peptides were desalted using C18 Zip Tips per the manufacturer’s instructions and vacuum-dried to prepare for subsequent MS analysis. The tryptic peptides were dissolved in solvent A and loaded directly onto an in-house reverse-phase analytical column (15 cm × 100 μm internal diameter) using a Vanquish Neo UPLC system (Thermo Fisher Scientific). The mobile phase consisted of solvent A (0.1% formic acid in water) and solvent B (0.1% formic acid in 80% acetonitrile-water), and chromatographic separation was achieved with the following gradient program at a constant flow rate of 200 nL/min: 0–1.6 min, 4%–22.5% B; 1.6–2.0 min, 22.5%–35% B; 2.0–2.1 min, 35.0%–35.1% B; 2.1–2.3 min, 35.1% B; 2.3–9.2 min, 35.1%–35.2% B; 9.2–9.6 min, 35.2%–55.0% B; 9.6–10.1 min, 55.0%–99.0% B; 10.1–12.0 min, 99% B. The separated peptides were ionized via a nano-electrospray ion source at 1900 V and analyzed on an Orbitrap Astral mass spectrometer (Thermo Fisher Scientific). Full-scan MS spectra (400–800 m/z) were acquired in the Orbitrap mass analyzer at a resolution of 240,000, while tandem MS (MS/MS) spectra were obtained in the Astral analyzer at a resolution of 80,000 with a fixed first mass of 150.0 m/z. Higher-energy collisional dissociation was applied at a normalized collision energy of 25%. Automatic gain control was set to 800% with a maximum ion injection time of 15 ms to optimize sensitivity and dynamic range."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Data-independent acquisition (DIA) data were analyzed using the DIA-NN computational platform (v1.8) . Tandem mass spectra were queried against the Mus_musculus_10090_SP_20231220.fasta database (17191 entries), which was concatenated with a reverse decoy database. Trypsin/P was designated as the proteolytic enzyme, with allowance for up to one missed cleavage. Fixed modifications included N-terminal methionine excision and cysteine carbamidomethylation. Peptide and protein identifications were filtered at a global false discovery rate (FDR) threshold of 1%. To enhance analytical quality, further data filtering was applied to the database search results, ensuring that each identified protein contained at least one peptide."],"omics_type":["Proteomics"],"labhead":["Chak Kwong Cheng"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Department of Biomedical Sciences, City University of Hong Kong, Hong Kong, China"],"species":["Mus Musculus (mouse)"],"publication":["41930346 Cheng CK, Meng S, Li T, Ding H, Jiang M, Tian Z, Ng CF, Xia Y, Offermanns S, Huang Y. Spatially Characterized Aortic Proteome Reveals Novel Regional Signatures and Glucocorticoid Receptor/Dipeptidase 1 Axis in Diabetic Vasculopathy. MedComm (2020). 2026 7(4):e70714 10.1002/mco2.70714"],"submitter_mail":["superandy333@gmail.com"],"submitter_affiliation":["City University of Hong Kong"],"submitter_country":["China"],"pubmed_abstract":["Diabetes mellitus poses a major global health burden and is intricately linked to cardiovascular complications, yet the spatial molecular landscape of diabetic vasculopathy remains poorly defined. Since thoracic and abdominal aortas differ in embryological origin and hemodynamic microenvironments, we applied laser-capture microdissection to map their spatial proteomes in health and diabetes, using a multidimensional framework across longitudinal (region) and transverse (disease) axes. This approach uncovered region-specific protein and pathway signatures obscured by conventional bulk analyses, highlighting spatial heterogeneity in transcriptional regulators and flow-sensitive proteins. We identified dipeptidase 1 (DPEP1), a membrane-bound zinc metalloprotease, as selectively upregulated in the diabetic thoracic aorta and inducible by diabetic conditions and shear stress. Mechanistically, laminar shear stress promoted glucocorticoid receptor (GR) nuclear translocation to drive a GR/DPEP1 axis, potentially explaining region-specific DPEP1 induction and its synergy with diabetic conditions. Functionally, chronic Dpep1 inhibition by cilastatin and endothelium-specific Dpep1 knockdown attenuated neutrophilic vascular inflammation and rescued endothelial dysfunction in diabetic mice. Furthermore, the corticosteroid dexamethasone activated the shear stress-responsive GR/DPEP1 axis in vivo, yet exerted time-dependent vascular effects-acutely dampening neutrophilic inflammation, but chronically worsening hyperglycemia and aggravating vascular dysfunction. These findings reveal spatially defined biomarkers and highlight DPEP1 as a therapeutic target in diabetic vasculopathy."],"pubmed_title":["Spatially Characterized Aortic Proteome Reveals Novel Regional Signatures and Glucocorticoid Receptor/Dipeptidase 1 Axis in Diabetic Vasculopathy."],"pubmed_authors":["Cheng Chak Kwong CK, Meng Shuhui S, Li Teng T, Ding Huanyu H, Jiang Minchun M, Tian Zizhao Z, Ng Chi-Fai CF, Xia Yin Y, Offermanns Stefan S, Huang Yu Y"],"additional_accession":[]},"is_claimable":false,"name":"Proteome profiles in diabetic thoracic and abdominal aortas","description":"This study provides a comprehensive atlas of how proteomic profiles are distinct in thoracic and abdominal aortas of spontaneously diabetic 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