Deimination of the myelin basic protein decelerates its proteasome-mediated metabolism

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• 作者：E. S. Kuzina ; A. A. Kudriaeva ; I. S. Glagoleva…
• 刊名：Doklady Biochemistry and Biophysics
• 出版年：2016
• 出版时间：July 2016
• 年：2016
• 卷：469
• 期：1
• 页码：277-280
• 全文大小：496 KB
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Biophysics and Biomedical Physics
  Russian Library of Science
  
• 出版者：MAIK Nauka/Interperiodica distributed exclusively by Springer Science+Business Media LLC.
• ISSN：1608-3091
• 卷排序：469

文摘

Deimination of myelin basic protein (MBP) by peptidylarginine deiminase (PAD) prevents its binding to the proteasome and decelerates its degradation by the proteasome in mammalian cells. Potential anticancer drug tetrazole analogue of chloramidine 2, at concentrations greater than 1 µM inhibits the enzymatic activity of PAD in vitro. The observed acceleration of proteasome hydrolysis of MBP to antigenic peptides in the presence of PAD inhibitor may increase the efficiency of lesion of the central nervous system by cytotoxic lymphocytes in multiple sclerosis. We therefore suggest that clinical trials and the introduction of PAD inhibitors in clinical practice for the treatment of malignant neoplasms should be performed only after a careful analysis of their potential effect on the induction of autoimmune neurodegeneration processes.