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- W156735602 abstract "Polyisoprenylation is a protein modification with 15 or 20 carbon isoprenes. Polyisoprenylated proteins (PP) undergo S-adenosyl-L-methionine-dependent methylation of the terminal -COOH. PP mediate various intracellular processes such as signaling, cell proliferation, differentiation and apoptosis and mutations of PP are encountered in about 30% of cancers. The methylation by PP methyl transferase (PPMTase) is counteracted by PMPMEase and constitute the only reversible step of the pathway. The relative amounts of the acid and ester forms of PP are determined by the two enzymes. Since PMPMEase and PPMTase may influence functional conformations of PP, a thorough knowledge of these enzymes is essential to the understanding of the significance of PP. Unlike the well studied PPMTase, PMPMEase is less understood. PMPMEase's ability to hydrolyze food-derived substances has led us to hypothesize a regulatory role of PUFAs on the enzyme activity. A series of saturated and PUFAs were tested for PMPMEase inhibition using an HPLC-based assay. Shorter chain, more unsaturated, cis fatty acids were the most inhibitory, with an IC50 of 11.6 μM for eicosapentaenoic acid. The anticancer and other benefits of short chain fatty acids and PUFAs may be related to PMPMEase inhibition given the many putative PP substrates that impact various biochemical events. Supported by NIH/NIGMS/SCORE (GM 08111-35) & NIH/NCRR (G12 RR0 3020)." @default.
- W156735602 created "2016-06-24" @default.
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- W156735602 date "2009-04-01" @default.
- W156735602 modified "2023-09-27" @default.
- W156735602 title "Polyunsaturated Fatty Acids (PUFAs) Inhibit Polyisoprenylated Methylated Protein Methyl Esterase (PMPMEase)" @default.
- W156735602 doi "https://doi.org/10.1096/fasebj.23.1_supplement.675.3" @default.
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