Roles of DNA repair enzyme OGG1 in innate immunity and its significance for lung cancer.
Innate immune response
Kirsten-Ras
Lung cancer
Metastasis
OGG1
Reactive oxygen species
Journal
Pharmacology & therapeutics
ISSN: 1879-016X
Titre abrégé: Pharmacol Ther
Pays: England
ID NLM: 7905840
Informations de publication
Date de publication:
02 2019
02 2019
Historique:
pubmed:
22
9
2018
medline:
29
2
2020
entrez:
22
9
2018
Statut:
ppublish
Résumé
Cytokines are pivotal mediators of the immune response, and their coordinated expression protects host tissue from excessive damage and oxidant stress. Nevertheless, the development of lung pathology, including asthma, chronic obstructive pulmonary disease, and ozone-induced lung injury, is associated with oxidant stress; as evidence, there is a significant increase in levels of the modified guanine base 7,8-dihydro-8-oxoguanine (8-oxoG) in the genome. 8-OxoG is primarily recognized by 8-oxoguanine glycosylase 1 (OGG1), which catalyzes the first step in the DNA base excision repair pathway. However, oxidant stress in the cell transiently halts enzymatic activity of substrate-bound OGG1. The stalled OGG1 facilitates DNA binding of transactivators, including NF-κB, to their cognate sites to enable expression of cytokines and chemokines, with ensuing recruitments of inflammatory cells. Hence, defective OGG1 will modulate the coordination between innate and adaptive immunity through excessive oxidant stress and cytokine dysregulation. Both oxidant stress and cytokine dysregulation constitute key elements of oncogenesis by KRAS, which is mechanistically coupled to OGG1. Thus, analysis of the mechanism by which OGG1 modulates gene expression helps discern between beneficial and detrimental effects of oxidant stress, exposes a missing functional link as a marker, and yields a novel target for lung cancer.
Identifiants
pubmed: 30240635
pii: S0163-7258(18)30159-1
doi: 10.1016/j.pharmthera.2018.09.004
pmc: PMC6504182
mid: NIHMS1026305
pii:
doi:
Substances chimiques
NF-kappa B
0
Reactive Oxygen Species
0
DNA Glycosylases
EC 3.2.2.-
oxoguanine glycosylase 1, human
EC 3.2.2.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
59-72Subventions
Organisme : NIAID NIH HHS
ID : P01 AI062885
Pays : United States
Organisme : NIEHS NIH HHS
ID : P30 ES006676
Pays : United States
Organisme : NIEHS NIH HHS
ID : R01 ES018948
Pays : United States
Informations de copyright
Copyright © 2018 Elsevier Inc. All rights reserved.
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