AACS (gene)
In today's world, AACS (gene) has become a topic of great relevance and interest to a wide spectrum of people. Whether due to its impact on society, its relevance in history, its influence on popular culture, AACS (gene) has managed to capture the attention of millions of individuals around the world. This phenomenon has generated extensive debate and analysis in different areas, which has led to the production of numerous articles that seek to explore and explain its multiple facets. In this sense, the importance of addressing the topic of AACS (gene) lies in its ability to inspire reflections, raise questions and generate greater understanding about its significance today.
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The acetoacetyl-CoA synthetase (AACS) gene encodes a protein of the same name, which converts acetoacetate to acetoacetyl-CoA, and plays a crucial role in ketone body utilization and fatty acid synthesis. The gene is found on human chromosome 12.
The AACS protein is a member of the acetyl-CoA synthetase family and is involved in cellular energy production, ketogenesis, and cholesterol synthesis.[5] It is expressed in a wide range of human tissues.[6]
Function
The protein's function is regulated transcriptionally by sterol regulatory element-binding protein (SREBP) and peroxisome proliferator-activated receptor gamma (PPARγ).[7]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000081760 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029482 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Q86V21 · AACS_HUMAN". www.uniprot.org. Uniprot. Retrieved 2023-12-09.
- ^ "AACS acetoacetyl-CoA synthetase". www.ncbi.nlm.nih.gov. NCBI Gene. Retrieved 2023-12-09.
- ^ Aguiló F, Camarero N, Relat J, Marrero PF, Haro D (March 2010). "Transcriptional regulation of the human acetoacetyl-CoA synthetase gene by PPARgamma" (PDF). The Biochemical Journal. 427 (2): 255–264. doi:10.1042/bj20090851. PMID 20102333. S2CID 1043396.
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