Proteomics

Dataset Information

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Statin therapy inhibits Fatty Acid Synthase via dynamic protein modifications


ABSTRACT: Recent discoveries revealed HMG-CoA is a reactive metabolite that can non-enzymatically modify proteins and impact their activity. Therefore, we predicted that inhibition of HMGCR by statins might increase HMG-CoA levels and protein modifications. Upon statin treatment, we observed a strong increase in HMG-CoA levels, and only a single protein was modified. Mass spectrometry revealed fatty acid synthase (FAS) was modified on active site residues and, importantly, the modification is located on non-lysine side-chains.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human) Sus Scrofa Domesticus (domestic Pig)

TISSUE(S): Liver

SUBMITTER: Alec Trub  

LAB HEAD: Matthew D Hirschey

PROVIDER: PXD030952 | Pride | 2022-05-20

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
ID24562_01_E749_4374_072916.raw Raw
ID26058_01_E749_4374_110916.raw Raw
ID27366_01_E749_4374_120816.raw Raw
ID42063_01_FSN20357_4374_101918.raw Raw
ID42064_01_FSN20357_4374_101918.raw Raw
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Publications


Statins are a class of drug widely prescribed for the prevention of cardiovascular disease, with pleiotropic cellular effects. Statins inhibit HMG-CoA reductase (HMGCR), which converts the metabolite HMG-CoA into mevalonate. Recent discoveries have shown HMG-CoA is a reactive metabolite that can non-enzymatically modify proteins and impact their activity. Therefore, we predicted that inhibition of HMGCR by statins might increase HMG-CoA levels and protein modifications. Upon statin treatment, we  ...[more]

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