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PXD073409

PXD073409 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleEndothelial Glycocalyx Injury in Obstructive Sleep Apnea Links Repetitive Hypoxemia to Immunothrombotic Endothelial Dysfunction
DescriptionBACKGROUND: Obstructive sleep apnea (OSA) is associated with cardiovascular disease. The endothelial glycocalyx (eGCX) is a shear-sensitive, interfacial barrier towards the intravascular compartment. The relevance of OSA and intermittent hypoxia (IH) for eGCX injury and, subsequently, cardiovascular pathologies in humans remains unclear. METHODS: In a prospective, single-center observational study in men, polysomnography quantified apnea-hypopnea index (AHI), oxygen desaturation index (ODI), and hypoxic burden (HB). Plasma levels of the key eGCX glycosaminoglycans hyaluronan (HA) and heparan sulfate (HS) and the proteoglycan syndecan-1 (SDC-1) were related to OSA severity and repetitive hypoxemia. Plasma proteomics defined pathways associated with OSA and an HA/HS-derived eGCX score. In parallel, shear-matured primary human endothelial cells were exposed to OSA-characteristic IH cycles under arterial flow to assess eGCX structure, oxidative stress, nitric-oxide (NO) signaling, thromboinflammatory status, and to test N-acetylcysteine as an antioxidant. RESULTS: Plasma levels of HA and HS were higher in OSA than in non-OSA individuals and increased stepwise with disease severity, tracking AHI, ODI and HB. Plasma SDC-1 did not differ between the groups. Proteomics revealed enrichment of inflammation, coagulation, and oxidative stress-related pathways that strengthened with increasing OSA burden and higher eGCX scores. Experimentally, IH caused loss of endothelial surface HA/HS with increased shedding, increased reactive oxygen species, reduced redox capacity, and decreased endothelial NO synthase expression and NO bioavailability. IH or enzymatic eGCX digestion each enhanced monocyte adhesion and fibrin deposition on the endothelium under physiological shear, while N-acetylcysteine attenuated oxidative stress and partially restored surface HA expression. CONCLUSIONS: Integrated patient and IH-model data indicate that OSA is associated with eGCX degradation linked to oxidative-inflammatory stress and a pro-adhesive, pro-thrombotic endothelial phenotype. These data highlight circulating HA and HS as translational biomarkers of OSA-related eGCX injury with potential utility for risk stratification and as pharmacodynamic readouts for eGCX-stabilizing adjunct therapies.
HostingRepositoryPRIDE
AnnounceDate2026-06-29
AnnouncementXMLSubmission_2026-06-28_17:01:41.253.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterTeresa Barth
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: NEWT:9606;
ModificationListiodoacetamide derivatized residue
InstrumentOrbitrap Exploris 480
Dataset History
RevisionDatetimeStatusChangeLog Entry
02026-01-22 06:25:55ID requested
12026-06-28 17:01:42announced
Publication List
10.1186/s12967-026-08409-2;
M, ü, ller MB, Kammerer T, Khan H, Schmid A, Hirschberger S, H, ü, bner M, Barth TK, Mitsigiorgi R, Stihl C, Holzer M, Jira D, Patscheider M, Weiss BG, Reichel CA, Uhl B, Endothelial glycocalyx perturbation in obstructive sleep apnea is associated with repetitive hypoxemia and immunothrombotic endothelial dysfunction. J Transl Med, 24(1):(2026) [pubmed]
Keyword List
submitter keyword: Plasma proteomics, neat plasma
Contact List
Martin Bernhard Mueller
contact affiliation1 Department of Anaesthesiology, LMU University Hospital, Ludwig-Maximilian-University (LMU), Munich, Germany 2 Walter Brendel Center of Experimental Medicine, Research Unit Immune Function and Immune Metabolism, Ludwig-Maximilian-University (LMU), Munich, Germany
contact emailMartin_Bernhard.Mueller@med.uni-muenchen.de
lab head
Teresa Barth
contact affiliationBiomedical Center Munich, Ludwig-Maximilians-Universitaet Munich
contact emailteresa.barth@bmc.med.lmu.de
dataset submitter
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