Monoamine oxidase B induces ERK-dependent cell mitogenesis by hydrogen peroxide generation.
Biochem Biophys Res Commun
; 271(1): 181-5, 2000 Apr 29.
Article
in En
| MEDLINE
| ID: mdl-10777699
ABSTRACT
The mitochondrial enzyme monoamine oxidase (MAO) A and B catalyze the oxidative deamination of various endogenous and exogenous biogenic amines. In the present study, we used human embryonic kidney 293 (HEK 293) cells stably transfected with human MAO-B cDNA to investigate the potential role of hydrogen peroxide (H(2)O(2)) produced by MAO-B isoform as an intracellular messenger involved in regulation of cell signaling and function. The MAO substrate tyramine induced tyrosine phosphorylation of Shc, ERK activation, and an increase in DNA synthesis in HEK 293 expressing MAO-B, but not in wild type HEK 293 cells, which do not express MAO. Tyramine effects were fully prevented by cell pretreatment with the MAO inhibitor pargyline or the antioxidant N-acetylcysteine. These results show that MAO-B induces MAPK/ERK activation and cell mitogenesis through H(2)O(2) production.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Mitogen-Activated Protein Kinases
/
Adaptor Proteins, Vesicular Transport
/
Adaptor Proteins, Signal Transducing
/
Hydrogen Peroxide
/
Monoamine Oxidase
Limits:
Humans
Language:
En
Journal:
Biochem Biophys Res Commun
Year:
2000
Document type:
Article
Affiliation country:
France