Abstract: TH-PO711
Adductome of HDL from Non-Diabetic Hemodialysis Patients
Session Information
- Hypertension and CVD: Epidemiology, Risk Factors
November 07, 2019 | Location: Exhibit Hall, Walter E. Washington Convention Center
Abstract Time: 10:00 AM - 12:00 PM
Category: Hypertension and CVD
- 1403 Hypertension and CVD: Mechanisms
Authors
- Florens, Nans, Hospices Civils de Lyon, Lyon, France
- Calzada, Catherine, CarMeN, INSERM, U1060, INSA Lyon, Villeurbanne, France
- Delolme, Frédéric, CNRS, Lyon, France
- Guebre Egziabher, Fitsum, Hospices Civils de Lyon, Lyon, France
- Juillard, Laurent, Hospices Civils de Lyon, Lyon, France
- Soulage, Christophe O., CarMeN, INSERM, U1060, INSA Lyon, Villeurbanne, France
Background
HDL dysfunction could participe in the increased cardiovascular mortality in CKD. have been pointed out in this burden. Post-translational modifications (PTM) of HDL were highlighted as potential mediators of HDL dysfunction. We aimed to describe PTM of HDL proteins from non-diabetic hemodialysis (HD) patients.
Methods
HDL were sampled from the plasma of 9 non-diabetic HD and 9 potential kidney-donors patients with a sequential ultracentrifugation. Samples were analyzed using an nano-RSLC coupled on line with a Q-Orbitrap. Data were processed with Proteome Discoverer 2.2 software and quantified with a label free quantitation approach. Oxidation,acetylation, carbonylation (with 4-HNE), carbamylation, guanidinylation, chlorination, nitration and nitrosylation were set as variable modifications. Protein quantitation was based on pairwise ratios and ANOVA hypothesis test.
Results
522 proteins were identified in HDL from HD patients and controls among which 73 (i.e. 14%) presented adduction sites. The main PTM were glycation (26%), guanidynilation (17%), carbamylation (15%), nitration (14%), carbonylation by the 4-HNE (11%), nitrosilation (9%) and chlorination (8%). Those proteins were involved in lipid metabolism, acute phase response, hemostasis, wound healing and muscular metabolism. Apolipoprotein A2 and 1 were the proteins the more prone to adduction (28 and 27% respectively) followed by serum albumin (15%), apolipoprotein C3 (9%) and serum amyloid A4 (8%, Figure 1). Most of the key-proteins of HDL metabolism were found to be adductable.
Conclusion
HDL from HD patients presented several post-translational modifications of their proteins. Those proteins are involved in most of the biological functions of HDL and their modifications could contribute the dysfunction of HDL in CKD.