Abstract T P172: Putative Blood Biomarkers for Reversible Cerebral Vasoconstriction Syndrome
Background: The pathophysiology and molecular mechanisms of Reversible Cerebral Vasoconstriction Syndrome (RCVS) are unknown. Objective of the study was to identify putative biomarker proteins for RCVS.
Methods: Patients were recruited from our institution’s prospective RCVS registry. Plasma samples were collected from 6 patients with RCVS during the acute cerebral vasoconstrictive phase, 2 patients at 6-month follow-up after resolution of vasoconstriction, and 4 patients with CNS vasculitis.
After appropriate processing, plasma samples were analyzed by liquid chromatography tandem mass spectrometry (LC-MS/MS) on a high resolution Orbitrap-Elite FT-MS system. The quantitation was performed by searching the data with the programs Mascot and Sequest. These search results were then uploaded into the program Scaffold. Quantitation was performed by comparing normalized spectral counts (nSC) for the samples. The data was filtered based on several parameters including 2 matching peptides, a FDR of 1.0%, a protein threshold of 95%, and identification of at least 3 peptides in the samples. In order for a protein to be considered as a putative biomarker, the relative abundance needed to be at least two fold different with the T-test derived p-value < 0.05.
Results: A total of 228 proteins were identified. Three, 5 and 4 proteins were found to be of higher abundance in a) follow-up samples of RCVS compared to baseline RCVS, b) CNS vasculitis samples compared to baseline RCVS, and c) baseline RCVS samples compared to CNS vasculitis respectively.(Table 1)
Conclusion: This is a preliminary study looking at proteomic analysis of RCVS plasma samples. Results of this study show proteins that might be potential biomarkers for RCVS and which could help differentiate RCVS from its mimic CNS vasculitis. Further studies with larger number of patients are needed to assess reproducibility. The function and the pathways of these differentially expressed proteins should be further explored.
Author Disclosures: S. John: None. B. Willard: None. L. Calabrese: None. T. Hammad: None. K. Uchino: None. S. Tepper: None. M. Stillman: None. R. Hajj-Ali: None.
- © 2014 by American Heart Association, Inc.