Function of bcl-X proteins in Nitric Oxide-induced Apoptosis in RAW 264.7 Macrophages / 대한면역학회지
Korean Journal of Immunology
; : 229-236, 1999.
Article
in Ko
| WPRIM
| ID: wpr-224757
Responsible library:
WPRO
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.
Key words
Full text:
1
Index:
WPRIM
Main subject:
Arginine
/
Cell Death
/
Apoptosis
/
DNA, Complementary
/
Nitric Oxide Synthase
/
Bcl-X Protein
/
Macrophages
/
Nitric Oxide
Limits:
Humans
Language:
Ko
Journal:
Korean Journal of Immunology
Year:
1999
Type:
Article