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Effects of a novel arginine methyltransferase inhibitor on T‐helper cell cytokine production
Author(s) -
Bonham Kevin,
Hemmers Saskia,
Lim YeonHee,
Hill Dawn M.,
Finn M. G.,
Mowen Kerri A.
Publication year - 2010
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2010.07623.x
Subject(s) - immunoprecipitation , methyltransferase , methylation , arginine , biochemistry , uniprot , immune system , chemistry , biology , amino acid , immunology , gene
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. Structured digital abstract• MINT‐7710141 : Prmt1 (uniprotkb: Q63009 ) physically interacts ( MI:0915 ) with nip45 (uniprotkb: O09130 ) by anti tag coimmunoprecipitation ( MI:0007 ) • MINT‐7710127 : Prmt1 (uniprotkb: Q63009 ) physically interacts ( MI:0915 ) with Prmt1 (uniprotkb: Q63009 ) by anti tag coimmunoprecipitation ( MI:0007 )