Exosome Proteomics Reveals the Deregulation of Coagulation, Complement and Lipid Metabolism Proteins in Gestational Diabetes Mellitus

• Published in: Molecules (Basel, Switzerland) Vol. 27; no. 17; p. 5502
• Main Authors: Bernea, Elena G, Suica, Viorel I, Uyy, Elena, Cerveanu-Hogas, Aurel, Boteanu, Raluca M, Ivan, Luminita, Ceausu, Iuliana, Mihai, Doina A, Ionescu-Tîrgoviște, Constantin, Antohe, Felicia
• Format: Journal Article
• Language: English
• Published: Basel MDPI AG 26-08-2022; MDPI
• Subjects: Analysis; Blood platelets; C4b-binding protein; Chains; Cholesterol; Coagulation; Complement; Complement activation; Complement component C3; Complement component C4; Complement component C5; complement system; Correlation analysis; Deregulation; Diabetes in pregnancy; Diabetes mellitus; Exosomes; Extracellular vesicles; Gestational diabetes; Hyperglycemia; Inflammation; Insulin resistance; Lipid metabolism; Lipids; Mass spectrometry; Metabolic disorders; Metabolites; Pathogenesis; Patients; Physiological aspects; Physiology; Plasma; platelet activation; Pregnancy; Pregnant women; Protein binding; Proteins; Proteomics; prothrombotic factors; Scientific equipment and supplies industry; Severe acute respiratory syndrome coronavirus 2; Spectrometry; Type 2 diabetes; Womens health; United States; United Kingdom; Romania
• ISSN: 1420-3049; 1420-3049
• DOI: 10.3390/molecules27175502

Exosomes are small extracellular vesicles with a variable protein cargo in consonance with cell origin and pathophysiological conditions. Gestational diabetes mellitus (GDM) is characterized by different levels of chronic low-grade inflammation and vascular dysfunction; however, there are few data characterizing the serum exosomal protein cargo of GDM patients and associated signaling pathways. Eighteen pregnant women were enrolled in the study: 8 controls (CG) and 10 patients with GDM. Blood samples were collected from patients, for exosomes’ concentration. Protein abundance alterations were demonstrated by relative mass spectrometric analysis and their association with clinical parameters in GDM patients was performed using Pearson’s correlation analysis. The proteomics analysis revealed 78 significantly altered proteins when comparing GDM to CG, related to complement and coagulation cascades, platelet activation, prothrombotic factors and cholesterol metabolism. Down-regulation of Complement C3 (C3), Complement C5 (C5), C4-B (C4B), C4b-binding protein beta chain (C4BPB) and C4b-binding protein alpha chain (C4BPA), and up-regulation of C7, C9 and F12 were found in GDM. Our data indicated significant correlations between factors involved in the pathogenesis of GDM and clinical parameters that may improve the understanding of GDM pathophysiology. Data are available via ProteomeXchange with identifier PXD035673.