Biochemical Mechanisms of Sirtuin-Directed Protein Acylation in Hepatic Pathologies of Mitochondrial Dysfunction.

acetylation alcoholic liver disease histone deacetylase metabolic syndrome mitochondria non-alcoholic liver disease sirtuin

Journal

Cells
ISSN: 2073-4409
Titre abrégé: Cells
Pays: Switzerland
ID NLM: 101600052

Informations de publication

Date de publication:
28 06 2022
Historique:
received: 16 05 2022
revised: 06 06 2022
accepted: 10 06 2022
entrez: 9 7 2022
pubmed: 10 7 2022
medline: 14 7 2022
Statut: epublish

Résumé

Mitochondrial protein acetylation is associated with a host of diseases including cancer, Alzheimer's, and metabolic syndrome. Deciphering the mechanisms regarding how protein acetylation contributes to disease pathologies remains difficult due to the complex diversity of pathways targeted by lysine acetylation. Specifically, protein acetylation is thought to direct feedback from metabolism, whereby nutritional status influences mitochondrial pathways including beta-oxidation, the citric acid cycle, and the electron transport chain. Acetylation provides a crucial connection between hepatic metabolism and mitochondrial function. Dysregulation of protein acetylation throughout the cell can alter mitochondrial function and is associated with numerous liver diseases, including non-alcoholic and alcoholic fatty liver disease, steatohepatitis, and hepatocellular carcinoma. This review introduces biochemical mechanisms of protein acetylation in the regulation of mitochondrial function and hepatic diseases and offers a viewpoint on the potential for targeted therapies.

Identifiants

pubmed: 35805129
pii: cells11132045
doi: 10.3390/cells11132045
pmc: PMC9266223
pii:
doi:

Substances chimiques

Mitochondrial Proteins 0
Sirtuin 3 EC 3.5.1.-
Sirtuins EC 3.5.1.-

Types de publication

Journal Article Review Research Support, Non-U.S. Gov't Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NIAAA NIH HHS
ID : R21 AA026928
Pays : United States
Organisme : NIEHS NIH HHS
ID : T32 ES007091
Pays : United States
Organisme : NIAAA NIH HHS
ID : R21 AA029218
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK109964
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM137910
Pays : United States

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Auteurs

Courtney D McGinnis (CD)

Skaggs School of Pharmacy and Pharmaceutical Sciences, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA.

Erin Q Jennings (EQ)

Department of Pharmacology and Toxicology, College of Pharmacy, University of Arizona, Tucson, AZ 85721, USA.

Peter S Harris (PS)

Skaggs School of Pharmacy and Pharmaceutical Sciences, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA.

James J Galligan (JJ)

Department of Pharmacology and Toxicology, College of Pharmacy, University of Arizona, Tucson, AZ 85721, USA.

Kristofer S Fritz (KS)

Skaggs School of Pharmacy and Pharmaceutical Sciences, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA.

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