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文献检索文档翻译深度研究

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Loss of Sirtuin 1 (SIRT1) potentiates endothelial dysfunction via impaired glycolysis during infectious challenge.

作者信息

Stark Ryan J, Koch Stephen R, Stothers Cody L, Pourquoi Allison, Lamb Celia K, Miller Michael R, Choi Hyehun

机构信息

Department of Pediatrics, Vanderbilt University Medical Center, Nashville, Tennessee.

出版信息

Clin Transl Med. 2022 Sep;12(9):e1054. doi: 10.1002/ctm2.1054.

DOI:10.1002/ctm2.1054

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9473483/

Abstract

摘要

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/50a0/9473483/2ca1107be8b2/CTM2-12-e1054-g003.jpg

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/50a0/9473483/526e089ee2c6/CTM2-12-e1054-g002.jpg

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/50a0/9473483/f09976a17d0e/CTM2-12-e1054-g004.jpg

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/50a0/9473483/8b029bb94fb3/CTM2-12-e1054-g001.jpg

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/50a0/9473483/2ca1107be8b2/CTM2-12-e1054-g003.jpg

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/50a0/9473483/526e089ee2c6/CTM2-12-e1054-g002.jpg

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/50a0/9473483/f09976a17d0e/CTM2-12-e1054-g004.jpg

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/50a0/9473483/8b029bb94fb3/CTM2-12-e1054-g001.jpg

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/50a0/9473483/2ca1107be8b2/CTM2-12-e1054-g003.jpg

相似文献

[1]

Loss of Sirtuin 1 (SIRT1) potentiates endothelial dysfunction via impaired glycolysis during infectious challenge.

Clin Transl Med. 2022-9

[2]

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[3]

Sirtuin 1 ablation in endothelial cells is associated with impaired angiogenesis and diastolic dysfunction.

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[4]

Childhood psychosocial stress is linked with impaired vascular endothelial function, lower SIRT1, and oxidative stress in young adulthood.

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[5]

Knockdown of circ0082374 inhibits cell viability, migration, invasion and glycolysis in glioma cells by miR-326/SIRT1.

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[6]

Sirtuin 1 stimulates the proliferation and the expression of glycolysis genes in pancreatic neoplastic lesions.

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[7]

P66Shc-Induced MicroRNA-34a Causes Diabetic Endothelial Dysfunction by Downregulating Sirtuin1.

Arterioscler Thromb Vasc Biol. 2016-12

[8]

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[9]

Targeting SIRT1 Rescues Age- and Obesity-Induced Microvascular Dysfunction in Ex Vivo Human Vessels.

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[10]

Neuronal SIRT1 (Silent Information Regulator 2 Homologue 1) Regulates Glycolysis and Mediates Resveratrol-Induced Ischemic Tolerance.

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引用本文的文献

[1]

Impact of FASN-enriched EVs on endothelial cell function in obstructive sleep apnea hypopnea syndrome.

J Pharm Anal. 2025-5

[2]

Research progress in the regulatory mechanism of silent information regulator 1 in sepsis (Review).

Mol Med Rep. 2025-8

[3]

Protein-mediated interactions in the dynamic regulation of acute inflammation.

Biocell. 2023

本文引用的文献

[1]

Endothelial-Dependent Responses Correlate with Pediatric SOFA Scores During Severe Sepsis and Septic Shock.

J Cardiovasc Transl Res. 2022-8

[2]

Clinical Significance of Pro-inflammatory Cytokines and Their Correlation with Disease Severity and Blood Coagulation in Septic Patients with Bacterial Co-infection.

Shock. 2021-9-1

[3]

The Role of Sirtuin1 in Regulating Endothelial Function, Arterial Remodeling and Vascular Aging.

Front Physiol. 2019-9-12

[4]

Mortality and morbidity in community-acquired sepsis in European pediatric intensive care units: a prospective cohort study from the European Childhood Life-threatening Infectious Disease Study (EUCLIDS).

Crit Care. 2018-5-31

[5]

Epidemiology of sepsis and septic shock in critical care units: comparison between sepsis-2 and sepsis-3 populations using a national critical care database.

Br J Anaesth. 2017-10-1

[6]

Neuronal SIRT1 (Silent Information Regulator 2 Homologue 1) Regulates Glycolysis and Mediates Resveratrol-Induced Ischemic Tolerance.

Stroke. 2017-11

[7]

Broad defects in the energy metabolism of leukocytes underlie immunoparalysis in sepsis.

Nat Immunol. 2016-3-7

[8]

THE ENDOTHELIUM IN SEPSIS.

Shock. 2016-3

[9]

E. coli endotoxin modulates the expression of Sirtuin proteins in PBMC in humans.

Mediators Inflamm. 2013-11-19

[10]

SIRT1 is a redox-sensitive deacetylase that is post-translationally modified by oxidants and carbonyl stress.

FASEB J. 2010-4-12

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