Effects of a novel arginine methyltransferase inhibitor on T-helper cell cytokine production

The protein arginine methyltransferase (PRMT) family of enzymes catalyzes the transfer of methyl groups from S-adenosylmethionine to the guanidino nitrogen atom of peptidylarginine to form monomethylarginine or dimethylarginine. We created several less polar analogs of the specific PRMT inhibitor ar...

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Bibliographic Details
Published in:The FEBS journal 2010-05, Vol.277 (9), p.2096-2108
Main Authors: Bonham, Kevin, Hemmers, Saskia, Lim, Yeon-Hee, Hill, Dawn M, Finn, M.G, Mowen, Kerri A
Format: Article
Language:English
Subjects:
Animals
Biochemistry
Cell Proliferation - drug effects
Cells, Cultured
Cellular biology
Cytokines
Enzyme Inhibitors - chemistry
Enzyme Inhibitors - pharmacology
Enzymes
Histones
Humans
inhibitors
Interferon-gamma - biosynthesis
Interferon-gamma - immunology
Interleukin-4 - biosynthesis
Interleukin-4 - genetics
Interleukin-4 - immunology
Methylation
Mice
Mice, Inbred BALB C
Molecular Structure
Nitrogen
nuclear factor of activated T cells interacting protein 45 kDa (NIP45)
Promoter Regions, Genetic
protein arginine methyltransferase
Protein-Arginine N-Methyltransferases - antagonists & inhibitors
Structure-Activity Relationship
T-helper cell
T-Lymphocytes, Helper-Inducer - cytology
T-Lymphocytes, Helper-Inducer - drug effects
T-Lymphocytes, Helper-Inducer - immunology
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Summary:The protein arginine methyltransferase (PRMT) family of enzymes catalyzes the transfer of methyl groups from S-adenosylmethionine to the guanidino nitrogen atom of peptidylarginine to form monomethylarginine or dimethylarginine. We created several less polar analogs of the specific PRMT inhibitor arginine methylation inhibitor-1, and one such compound was found to have improved PRMT inhibitory activity over the parent molecule. The newly identified PRMT inhibitor modulated T-helper-cell function and thus may serve as a lead for further inhibitors useful for the treatment of immune-mediated disease.
ISSN:1742-464X
1742-4658
DOI:10.1111/j.1742-4658.2010.07623.x