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Rare centenarian variant of SIRT6 enhances genome stability and promotes longevity
Sirtuins are a family of proteins involved in the regulation of aging and metabolism through multiple cellular pathways.
Disclaimer: These news are based on the article preprint, which has yet to be peer-reviewed and published
Sirtuins are a family of proteins involved in the regulation of aging and metabolism through multiple cellular pathways. Among them, evolutionary conserved SIRT6 draws particular attention due to its strong correlation with maximum lifespan. The known mechanisms for SIRT6 include DNA repair, telomere maintenance, regulation of glucose homeostasis, inflammation, and tumor suppression. The observed influence of SIRT6 on species longevity (particularly in genetically modified mice) raised the question of whether it might be connected with increased longevity in humans. Analysis of single nucleotide polymorphism (SNP, genetic variation based on a difference in a single nucleotide) revealed non-coding genetic polymorphisms in the SIRT6 gene region associated with human longevity. The SNP in non-coding regions while affecting the gene expression, does not influence the structure of the corresponding protein. And previously no beneficial mutations in SIRT6 associated with longevity have been functionally characterized.
The research group of Simon et al. identified two novel variants of SIRT6 enriched in a population of human centenarians. They performed targeted sequencing of SIRT6 locus (position on a chromosome) in a population of 496 Ashkenazi Jewish centenarians and 572 Ashkenazi Jewish controls (individuals without a family history of exceptional longevity). They observed two rare variants, one of which – centSIRT6 – had nearly double frequency among the centenarians. centSIRT6 demonstrated altered biological activities leading to an enhancement in DNA repair and increased resistance to oxidative stress. Additionally, the centenarian allele (version of the gene) possesses higher efficiency against cancer cells.
The mechanism behind centSIRT6 efficiency was found to be, firstly, the improvement in ADP-ribosylation activity. ADP-ribosylation is a process in which adenosine diphosphate ribose molecules are added to the protein. Such addition influences enzymatic functionality and is part of vital cellular processes, such as DNA repair and cell signaling. Secondly, researchers observed enhanced binding between SIRT6 and LMNA (lamin A/C protein) involved in the regulation of DNA oxidative damage. These findings hold potential for the development of potential target therapeutics to enhance SIRT6 activity and develop new anti-aging interventions.
Source: bioRxiv https://doi.org/10.1101/2021.12.13.472381
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Disclaimer: These news are based on the article preprint, which has yet to be peer-reviewed and published
Sirtuins are a family of proteins involved in the regulation of aging and metabolism through multiple cellular pathways. Among them, evolutionary conserved SIRT6 draws particular attention due to its strong correlation with maximum lifespan. The known mechanisms for SIRT6 include DNA repair, telomere maintenance, regulation of glucose homeostasis, inflammation, and tumor suppression. The observed influence of SIRT6 on species longevity (particularly in genetically modified mice) raised the question of whether it might be connected with increased longevity in humans. Analysis of single nucleotide polymorphism (SNP, genetic variation based on a difference in a single nucleotide) revealed non-coding genetic polymorphisms in the SIRT6 gene region associated with human longevity. The SNP in non-coding regions while affecting the gene expression, does not influence the structure of the corresponding protein. And previously no beneficial mutations in SIRT6 associated with longevity have been functionally characterized.
The research group of Simon et al. identified two novel variants of SIRT6 enriched in a population of human centenarians. They performed targeted sequencing of SIRT6 locus (position on a chromosome) in a population of 496 Ashkenazi Jewish centenarians and 572 Ashkenazi Jewish controls (individuals without a family history of exceptional longevity). They observed two rare variants, one of which – centSIRT6 – had nearly double frequency among the centenarians. centSIRT6 demonstrated altered biological activities leading to an enhancement in DNA repair and increased resistance to oxidative stress. Additionally, the centenarian allele (version of the gene) possesses higher efficiency against cancer cells.
The mechanism behind centSIRT6 efficiency was found to be, firstly, the improvement in ADP-ribosylation activity. ADP-ribosylation is a process in which adenosine diphosphate ribose molecules are added to the protein. Such addition influences enzymatic functionality and is part of vital cellular processes, such as DNA repair and cell signaling. Secondly, researchers observed enhanced binding between SIRT6 and LMNA (lamin A/C protein) involved in the regulation of DNA oxidative damage. These findings hold potential for the development of potential target therapeutics to enhance SIRT6 activity and develop new anti-aging interventions.
Source: bioRxiv https://doi.org/10.1101/2021.12.13.472381
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Dr. Ana Baroni MD. Ph.D.
Scientific & Medical Advisor
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Ana has over 20 years of consultancy experience in longevity, regenerative and precision medicine. She has a multifaceted understanding of genomics, molecular biology, clinical biochemistry, nutrition, aging markers, hormones and physical training. This background allows her to bridge the gap between longevity basic sciences and evidence-based real interventions, putting them into the clinic, to enhance the healthy aging of people. She is co-founder of Origen.life, and Longevityzone. Board member at Breath of Health, BioOx and American Board of Clinical Nutrition. She is Director of International Medical Education of the American College of Integrative Medicine, Professor in IL3 Master of Longevity at Barcelona University and Professor of Nutrigenomics in Nutrition Grade in UNIR University.
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