The 4-Hydroxynonenal-Protein Adducts and Their Biological Relevance: Are Some Proteins Preferred Targets?
4-HNE–protein adducts
4-hydroxynonenal (4-HNE)
adaptive response
ferroptosis
immunochemical methods
lipid peroxidation
mass spectrometry (MS)
the NRF2/KEAP1 signaling
Journal
Antioxidants (Basel, Switzerland)
ISSN: 2076-3921
Titre abrégé: Antioxidants (Basel)
Pays: Switzerland
ID NLM: 101668981
Informations de publication
Date de publication:
01 Apr 2023
01 Apr 2023
Historique:
received:
15
02
2023
revised:
27
03
2023
accepted:
29
03
2023
medline:
28
4
2023
pubmed:
28
4
2023
entrez:
28
4
2023
Statut:
epublish
Résumé
It is well known that oxidative stress and lipid peroxidation (LPO) play a role in physiology and pathology. The most studied LPO product with pleiotropic capabilities is 4-hydroxynonenal (4-HNE). It is considered as an important mediator of cellular signaling processes and a second messenger of reactive oxygen species. The effects of 4-HNE are mainly attributed to its adduction with proteins. Whereas the Michael adducts thus formed are preferred in an order of potency of cysteine > histidine > lysine over Schiff base formation, it is not known which proteins are the preferred targets for 4-HNE under what physiological or pathological conditions. In this review, we briefly discuss the methods used to identify 4-HNE-protein adducts, the progress of mass spectrometry in deciphering the specific protein targets, and their biological relevance, focusing on the role of 4-HNE protein adducts in the adaptive response through modulation of the NRF2/KEAP1 pathway and ferroptosis.
Identifiants
pubmed: 37107229
pii: antiox12040856
doi: 10.3390/antiox12040856
pmc: PMC10135105
pii:
doi:
Types de publication
Journal Article
Review
Langues
eng
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