Function of bcl-X proteins in Nitric Oxide-induced Apoptosis in RAW 264.7 Macrophages.
- Author:
Sang Gi PAIK
;
Young Sang KIM
;
Joo Young IM
;
Jeong Heon YOON
- Publication Type:Original Article
- Keywords:
Nitric oxide;
bcl-X;
Apoptosis
- MeSH:
Apoptosis*;
Arginine;
bcl-X Protein*;
Cell Death;
DNA, Complementary;
Humans;
Macrophages*;
Nitric Oxide;
Nitric Oxide Synthase
- From:Korean Journal of Immunology
1999;21(3):229-236
- CountryRepublic of Korea
- Language:Korean
-
Abstract:
LPS and IFN-r induce nitric oxide synthase in macrophages and the resultant NO causes apoptotic cell death in the activated macrophages. NO production and apoptosis were inhibited by N-monomethyl L-arginine (NMMA), a competitive inhibitor of NO synthase. To study the role of BCL-X proteins, RAW 264.7 cells were transfected with the expression vectors with human bcl-Xl or bcl-Xs cDNAs, respectively. Stable transfectants were selected and confirmed by RT-PCR. NO production in response to LPS and IFN-r caused apoptosis in RAW 264.7 cells and vector transfected control cells within 24 hr. Both NO production and apoptosis were inhibited by N(G)-monomethyl L-arginine (NMMA). In contrast, bcl-Xs transfectant appeared slightly susceptible and bcl-X(L)< transfectant appeared slightly resistant, although NO production was similar to control cells. These results suggest that bcl-X proteins play roles in both positive and negative regulation of apoptosis induced by NO.
