Erythrocyte-Associated Proteins Underlie the Reported Oxidative-Stress Enrichment in Plasma Proteomics of Obstructive Sleep Apnoea: A Secondary Quality Marker Analysis of Public Datasets
8 affiliations
- 1Department of Biostatistics and Medical Informatics, Faculty of Medicine, Inonu University, Malatya 44280, Türkiye
- 2Department of Biostatistics, and Medical Informatics, Faculty of Medicine, Balikesir University, Balikesir 10145, Türkiye
- 3Department of Therapy and Rehabilitation, Kozaklı Vocational School, Nevşehir Hacı Bektaş Veli University, Nevşehir 50600, Türkiye
- 4Department of Computer Sciences, College of Computer and Information Sciences, Princess Nourah bint Abdulrahman University, P.O. Box 84428, Riyadh 11671, Saudi Arabia
- 5Department of Physiology, College of Medicine, King Khalid University, Abha 61421, Saudi Arabia
- 6Department of Cariology, Institute of Odontology, The Sahlgrenska Academy, University of Gothenburg, 41390 Gothenburg, Sweden
- 7Department of Applied Dental Sciences, Faculty of Applied Medical Sciences, Jordan University of Science and Technology, Irbid 22110, Jordan
- 8Department of Pathology, Saveetha Medical College and Hospital, Saveetha Institute of Medical and Technical Sciences, Chennai 602 105, Tamil Nadu, India
Abstract
Background: Erythrocyte proteins released into plasma carry oxidation-related annotations and can be read as evidence of oxidative stress. We examined whether this applies to an oxidative-stress enrichment reported in a plasma proteomic study of obstructive sleep apnoea (OSA). Methods: In a secondary analysis of public data (PXD073409; men; 15 non-OSA, 15 mild OSA, 15 severe OSA; 422 proteins), erythrocyte, platelet and coagulation quality marker indices were computed from the panels of Geyer et al.; the erythrocyte panel was only partly quantified (15 of 29 entries). The original differential and over-representation analyses were repeated with panel members excluded, with adjustment for the erythrocyte index, and with leave-one-protein-out indices. A second public dataset (PXD069503; 15 severe OSA, 15 mild-to-moderate OSA, 15 controls) was used for directional comparison. Clinical covariates were not available. Results: The erythrocyte index was higher in mild (ratio of geometric means 1.74, 95% CI 1.04 to 2.80) and severe OSA (2.43, 1.68 to 3.47) than in non-OSA participants. Six of the 13 proteins that are increased in severe OSA were erythrocyte panel members, and all nine enriched terms consisted of panel members only, including hydrogen peroxide catabolic process (HBA1, HBB, HBD, PRDX2). After adjustment, PRDX2 was accounted for by erythrocyte content, whereas the haemoglobin chains remained elevated and carried seven of the terms. The index alone separated severe- from non-OSA participants (AUROC 0.858); the data could not show whether all 422 proteins (AUROC 0.969) add to it (difference +0.111, 95% CI −0.009 to +0.268). In the second dataset the index was higher in severe OSA than in controls (1.55, 1.06 to 2.35). Conclusions: The reported oxidative-stress enrichment rests on erythrocyte-associated proteins and, on these data, is not evidence of altered oxidative activity in plasma. Whether this content arises before or after venepuncture cannot be determined. Quality marker indices should be reported alongside plasma proteomic biomarker results.
Related
- Multi-organ proteomics identifies oxidative stress pathways underlying genetic and pharmacological SGLT2 suppression
- Extraplatelet Molecule Enrichment Enhances the Ability of Platelet-Rich Plasma Releasate to Buffer IL-1β-Induced Inflammation and Oxidative Stress in a Primary Human Chondrocyte–Synoviocyte Co-Culture In Vitro System of Osteoarthritis
- Enrichment-Free Rare Cell Profiling in Pediatric Osteosarcoma Reveals a Circulating Cell Population Associated with Relapse-Free Survival
- Endogenous APP-Associated Proteomics in Mouse Brain Defines a Candidate Resource for APP Trafficking and Proteostasis Studies
- Identification of candidate selenium-associated transcriptomic biomarkers in chronic obstructive pulmonary disease: an integrated bioinformatics and expression validation study
BibTeX
@article{yasar2026erythrocyteassociated,
title = {{Erythrocyte-Associated Proteins Underlie the Reported Oxidative-Stress Enrichment in Plasma Proteomics of Obstructive Sleep Apnoea: A Secondary Quality Marker Analysis of Public Datasets}},
author = {Seyma Yasar and Fatma Hilal Yagin and Busra Nur Findik and Sarah A. Alzakari and Amal K. Alkhalifa and Fahaid Al-Hashem and Abedelmalek Kalefh Tabnjh},
journal = {Journal of Clinical Medicine},
year = {2026},
month = oct,
doi = {10.3390/jcm15208081},
url = {https://www.mdpi.com/2077-0383/15/20/8081},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Erythrocyte-Associated Proteins Underlie the Reported Oxidative-Stress Enrichment in Plasma Proteomics of Obstructive Sleep Apnoea: A Secondary Quality Marker Analysis of Public Datasets
AU - Seyma Yasar
AU - Fatma Hilal Yagin
AU - Busra Nur Findik
AU - Sarah A. Alzakari
AU - Amal K. Alkhalifa
AU - Fahaid Al-Hashem
AU - Abedelmalek Kalefh Tabnjh
PY - 2026
DA - 2026/10/01
JO - Journal of Clinical Medicine
DO - 10.3390/jcm15208081
UR - https://www.mdpi.com/2077-0383/15/20/8081
AB - Background: Erythrocyte proteins released into plasma carry oxidation-related annotations and can be read as evidence of oxidative stress. We examined whether this applies to an oxidative-stress enrichment reported in a plasma proteomic study of obstructive sleep apnoea (OSA). Methods: In a secondary analysis of public data (PXD073409; men; 15 non-OSA, 15 mild OSA, 15 severe OSA; 422 proteins), erythrocyte, platelet and coagulation quality marker indices were computed from the panels of Geyer et al.; the erythrocyte panel was only partly quantified (15 of 29 entries). The original differential and over-representation analyses were repeated with panel members excluded, with adjustment for the erythrocyte index, and with leave-one-protein-out indices. A second public dataset (PXD069503; 15 severe OSA, 15 mild-to-moderate OSA, 15 controls) was used for directional comparison. Clinical covariates were not available. Results: The erythrocyte index was higher in mild (ratio of geometric means 1.74, 95% CI 1.04 to 2.80) and severe OSA (2.43, 1.68 to 3.47) than in non-OSA participants. Six of the 13 proteins that are increased in severe OSA were erythrocyte panel members, and all nine enriched terms consisted of panel members only, including hydrogen peroxide catabolic process (HBA1, HBB, HBD, PRDX2). After adjustment, PRDX2 was accounted for by erythrocyte content, whereas the haemoglobin chains remained elevated and carried seven of the terms. The index alone separated severe- from non-OSA participants (AUROC 0.858); the data could not show whether all 422 proteins (AUROC 0.969) add to it (difference +0.111, 95% CI −0.009 to +0.268). In the second dataset the index was higher in severe OSA than in controls (1.55, 1.06 to 2.35). Conclusions: The reported oxidative-stress enrichment rests on erythrocyte-associated proteins and, on these data, is not evidence of altered oxidative activity in plasma. Whether this content arises before or after venepuncture cannot be determined. Quality marker indices should be reported alongside plasma proteomic biomarker results.
SN - 2077-0383
ER -