TY - JOUR
T1 - Myelin Basic Protein Phospholipid Complexation Likely Competes with Deimination in Experimental Autoimmune Encephalomyelitis Mouse Model
AU - Valdivia, Anddre Osmar
AU - Agarwal, Pratul K.
AU - Bhattacharya, Sanjoy K.
N1 - Funding Information:
This work was supported by an unrestricted grant to the University of Miami from Research to Prevent Blindness (RPB), Department of Defense Grant WHX81-16-0715 and NIH Grant EY027257, EY14801, and NIH Grant GM105978 (to P.K.A.). This work used the Extreme Science and Engineering Discovery Environment (XSEDE), which is supported by National Science Foundation grant number ACI-1548562. XSEDE computing allocation were awarded to P.K.A. (MCB-180199 and MCB-190044).
Funding Information:
The authors would like to thank Dr. Jae Lee for his valuable insight into the preparation of the manuscript, Drs. Roberta Brambilla and Haritha Desu for their guidance in the generation of the EAE mouse model, and Dr. David Broyles for his guidance during circular dichroism experiments, EY14801and NIH Grant GM105978 (to PKA). This work used the Extreme Science and Engineering Discovery Environment (XSEDE), which is supported by National Science Foundation grant number ACI-1548562. XSEDE computing allocation were awarded to P.K.A. (MCB-180199 and MCB-190044).
PY - 2020/6/30
Y1 - 2020/6/30
N2 - Multiple sclerosis has complex pathogenesis encompassing a variety of components (immunologic, genetic, and environmental). The autoimmunogenicity against the host's myelin basic protein is a major contributor. An increase in myelin basic protein deimination (a post-translational modification) and a change in phospholipid composition have been associated with multiple sclerosis. The interaction of myelin basic protein with phospholipids in the myelin membrane is an important contributor to the stability and maintenance of proper myelin sheath function. The study of this aspect of multiple sclerosis is an area that has yet to be fully explored and that the present study seeks to understand. Several biochemical methods, a capillary electrophoresis coupled system and mass spectrometry, were used in this study. These methods identified four specific phospholipids complexing with myelin basic protein. We show that lysophosphatidylcholine 18:1 provides a robust competitive effect against hyper-deimination. Our data suggest that lysophosphatidylcholine 18:1 has a different biochemical behavior when compared to other phospholipids and lysophosphatidylcholines 14:0, 16:0, and 18:0.
AB - Multiple sclerosis has complex pathogenesis encompassing a variety of components (immunologic, genetic, and environmental). The autoimmunogenicity against the host's myelin basic protein is a major contributor. An increase in myelin basic protein deimination (a post-translational modification) and a change in phospholipid composition have been associated with multiple sclerosis. The interaction of myelin basic protein with phospholipids in the myelin membrane is an important contributor to the stability and maintenance of proper myelin sheath function. The study of this aspect of multiple sclerosis is an area that has yet to be fully explored and that the present study seeks to understand. Several biochemical methods, a capillary electrophoresis coupled system and mass spectrometry, were used in this study. These methods identified four specific phospholipids complexing with myelin basic protein. We show that lysophosphatidylcholine 18:1 provides a robust competitive effect against hyper-deimination. Our data suggest that lysophosphatidylcholine 18:1 has a different biochemical behavior when compared to other phospholipids and lysophosphatidylcholines 14:0, 16:0, and 18:0.
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U2 - 10.1021/acsomega.0c01590
DO - 10.1021/acsomega.0c01590
M3 - Article
AN - SCOPUS:85086849177
VL - 5
SP - 15454
EP - 15467
JO - ACS Omega
JF - ACS Omega
SN - 2470-1343
IS - 25
ER -