Arsenic-protein interactions as a mechanism of arsenic toxicity.
Animals
Arsenic Poisoning
/ etiology
Arsenicals
/ adverse effects
Cysteine
DNA Repair
/ drug effects
Endocrine Disruptors
/ adverse effects
Environmental Pollutants
/ adverse effects
Epigenesis, Genetic
/ drug effects
Humans
Protein Binding
Proteins
/ genetics
RING Finger Domains
Risk Assessment
Zinc Fingers
Arsenic
Cysteine
Interaction
Protein
Zinc finger
Journal
Toxicology and applied pharmacology
ISSN: 1096-0333
Titre abrégé: Toxicol Appl Pharmacol
Pays: United States
ID NLM: 0416575
Informations de publication
Date de publication:
15 11 2021
15 11 2021
Historique:
received:
23
07
2021
revised:
28
09
2021
accepted:
30
09
2021
pubmed:
8
10
2021
medline:
31
12
2021
entrez:
7
10
2021
Statut:
ppublish
Résumé
Millions of people worldwide are exposed to arsenic, a metalloid listed as one of the top chemical pollutants of concern to human health. Epidemiological and experimental studies link arsenic exposure to the development of cancer and other diseases. Several mechanisms have been proposed to explain the effects induced by arsenic. Notably, arsenic and its metabolites interact with proteins by direct binding to individual cysteine residues, cysteine clusters, zinc finger motifs, and RING finger domains. Consequently, arsenic interactions with proteins disrupt the functions of proteins and may lead to the development and progression of diseases. In this review, we focus on current evidence in the literature that implicates the interaction of arsenic with proteins as a mechanism of arsenic toxicity. Data show that arsenic-protein interactions affect multiple cellular processes and alter epigenetic regulation, cause endocrine disruption, inhibit DNA damage repair mechanisms, and deregulate gene expression, among other adverse effects.
Identifiants
pubmed: 34619159
pii: S0041-008X(21)00342-2
doi: 10.1016/j.taap.2021.115738
pii:
doi:
Substances chimiques
Arsenicals
0
Endocrine Disruptors
0
Environmental Pollutants
0
Proteins
0
Cysteine
K848JZ4886
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
115738Informations de copyright
Copyright © 2021 Elsevier Inc. All rights reserved.