Related Experiment Video

Updated: Dec 18, 2025

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
14:32

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates

Published on: February 27, 2016

8.5K

[Coronavirus disease (COVID-19) and sirtuins]

Ronald Eleazar Huarachi Olivera1, Antonio Lazarte Rivera2

  • 1Laboratorio de Biotecnologia Celular y Molecular Avanzada, Universidad Nacional de San Agustìn. ronaldhuarachiolivera@gmail.com.

Revista De La Facultad De Ciencias Medicas (Cordoba, Argentina)
|June 20, 2020
PubMed
Abstract

Insights

Sirtuins (SIRTs) are NAD+-dependent deacetylases. This review explores SIRTs in cancer and SIRT1 inhibition in COVID-19 patients, finding key roles in cancer development and viral pathology.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Sirtuins (SIRTs) are a class of NAD+-dependent protein deacetylases.
  • These proteins play crucial roles in cellular processes, including aging, metabolism, and disease.
  • Dysregulation of sirtuin activity is implicated in various pathologies, notably cancer and viral infections.

Purpose of the Study:

  • To review the involvement of sirtuins in cancer development.
  • To examine studies on SIRT1 inhibition in patients with COVID-19.
  • To elucidate the specific functions of different sirtuin family members in disease.

Main Methods:

  • A comprehensive literature search was conducted across Medline, Scopus, and Web of Science databases.
  • Descriptive studies focusing on the functions of sirtuins were included.
  • The review synthesized recent scientific research on sirtuin roles in cancer and viral diseases.

Main Results:

  • SIRT1, SIRT2, and SIRT4 are implicated in cancer development.
  • SIRT5 and SIRT7 suppression promotes cancer cell apoptosis.
  • SIRT6 attenuates Kaposi's Sarcoma-associated herpesvirus (KSHV) replication.
  • SIRT1 inhibition may be linked to inflammatory processes in COVID-19.

Conclusions:

  • Sirtuins play multifaceted roles in cancer, acting as both tumor suppressors and promoters.
  • SIRT1 activity is linked to the pathology of COVID-19, potentially through inflammatory pathways.
  • Targeting specific sirtuins offers potential therapeutic strategies for cancer and viral infections.
Keywords:
coronavirus infectionsneoplasmshistone deacetylasesNADsirtuins

More Related Videos

Live Imaging and Quantification of Viral Infection in K18 hACE2 Transgenic Mice Using Reporter-Expressing Recombinant SARS-CoV-208:41

Live Imaging and Quantification of Viral Infection in K18 hACE2 Transgenic Mice Using Reporter-Expressing Recombinant SARS-CoV-2

Published on: November 5, 2021

3.2K
Visualization of SARS-CoV-2 using Immuno RNA-Fluorescence In Situ Hybridization05:23

Visualization of SARS-CoV-2 using Immuno RNA-Fluorescence In Situ Hybridization

Published on: December 23, 2020

6.4K

Related Concept Videos

Single Nucleotide Polymorphisms-SNPs01:05

Single Nucleotide Polymorphisms-SNPs

A single nucleotide polymorphism or SNP is a single nucleotide variation at a specific genomic position in a large population. It is the most prevalent type of sequence variation found in the human genome. Point mutations that occur in more than 1% of the population qualify as SNPs. These are present once every 1000 nucleotides on an average in the human genome. Replacement of a purine with another purine (A/G) or a pyrimidine with another pyrimidine (C/T) is known as a transition. In contrast,...
17.7K
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
2.9K
siRNA - Small Interfering RNAs02:30

siRNA - Small Interfering RNAs

Small interfering RNAs, or siRNAs, are short regulatory RNA molecules that can silence genes post-transcriptionally, as well as the transcriptional level in some cases. siRNAs are important for protecting cells against viral infections and silencing transposable genetic elements.
In the cytoplasm, siRNA is processed from a double-stranded RNA, which comes from either endogenous DNA transcription or exogenous sources like a virus. This double-stranded RNA is then cleaved by the...
18.1K
Rous Sarcoma Virus (RSV) and Cancer01:03

Rous Sarcoma Virus (RSV) and Cancer

Rous Sarcoma virus or RSV was discovered by F. Peyton Rous in the year 1911 as a filterable transmissible agent that could cause tumors in chickens. He won a Nobel Prize for this discovery in 1966. His experiments clearly demonstrated that some cancers could be caused by infectious agents and led to the discovery of many more cancer-causing viruses in animals as well as humans.
RSV is a retrovirus that contains two copies of a plus-strand  RNA genome. Its genome consists of four main open...
6.0K
mTOR Signaling and Cancer Progression03:03

mTOR Signaling and Cancer Progression

The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
4.5K
The Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
6.1K