심현채 (성균관대학교)

이상규 (성균관대학교)

심현채 (성균관대학교)

김재용 (성균관대학교)

이지현 (조선대학교)

Yan Gao (경북대학교)

나안예 (경북대학교 G-램프 사업단)

기성환 (조선대학교)

이상규 (성균관대학교)

It is known that obesity is often linked with hyperacetylation on proteins and induces intricate changes in post-translational modification, affecting instability in mitochondrion regulations. Unveiling the complexity of the biological networks underlying obesity, high-fat diet-fed mice livers were lysed and immunoprecipitated with acetyl-lysine antibody-conjugated beads, then labeled with isotopic 18O for multiplexing. The twenty-cm homemade column packed with C18 resin was then connected to the Orbitrap Velos MS for tandem MS analysis. A total of 2,282 proteins and 1,384 acetyl-lysine sites were discovered. The expressed levels of acetylome were divided to protein expression for normalization, and approximately one-third of acetylome was quantified. Differentially expressed acetylated proteins were annotated by GO analysis, and upregulated proteins mainly belonged to the fatty acid related terms. Among them, the four proteins, Gstt1, ldh2, Gsta3, and Uox, were analyzed that have two-folded changes higher levels of acetyl-lysine than normal diet-fed mice. Interpro protein domains enrichment analysis show that significant motifs were clustered in several unique groups, predominantly enriched in NAD(P)-binding domain superfamily. Our data show that investigating the acetylation landscapes can provide potential insights into the molecular mechanisms driving obesity by lysine acetylome and suggesting targets for therapeutic intervention.

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