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BioMed Research International
Volume 2014, Article ID 926394, 10 pages
Research Article

Glatiramer Acetate and Nanny Proteins Restrict Access of the Multiple Sclerosis Autoantigen Myelin Basic Protein to the 26S Proteasome

1Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, V-437, Moscow 117871, Russia
2Chemistry Department, Lomonosov Moscow State University, Moscow 119991, Russia
3Kazan Federal University, Kazan, Republic of Tatarstan 420008, Russia
4Nanotechnology Research and Education Centre RAS, St. Petersburg Academic University, St. Petersburg 194021, Russia
5Institute of Gene Biology, Russian Academy of Sciences, Moscow 117334, Russia

Received 9 May 2014; Revised 13 August 2014; Accepted 16 August 2014; Published 8 September 2014

Academic Editor: W. David Arnold

Copyright © 2014 Ekaterina Kuzina et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


We recently showed that myelin basic protein (MBP) is hydrolyzed by 26S proteasome without ubiquitination. The previously suggested concept of charge-mediated interaction between MBP and the proteasome led us to attempt to compensate or mimic its positive charge to inhibit proteasomal degradation. We demonstrated that negatively charged actin and calmodulin (CaM), as well as basic histone H1.3, inhibit MBP hydrolysis by competing with the proteasome and MBP, respectively, for binding their counterpart. Interestingly, glatiramer acetate (GA), which is used to treat multiple sclerosis (MS) and is structurally similar to MBP, inhibits intracellular and in vitro proteasome-mediated MBP degradation. Therefore, the data reported in this study may be important for myelin biogenesis in both the normal state and pathophysiological conditions.