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

ABSTRACT: 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.

SUBMITTER: Bonham K

PROVIDER: S-EPMC2903848 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature

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

Bonham Kevin K Hemmers Saskia S Lim Yeon-Hee YH Hill Dawn M DM Finn M G MG Mowen Kerri A KA

The FEBS journal 20100322 9

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 ...[more]

PMID: 20345902

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