PMID- 8576237
OWN - NLM
STAT- MEDLINE
DCOM- 19960312
LR  - 20210210
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 271
IP  - 5
DP  - 1996 Feb 2
TI  - Coinduction of nitric oxide synthase, argininosuccinate synthetase, and 
      argininosuccinate lyase in lipopolysaccharide-treated rats. RNA blot, immunoblot, 
      and immunohistochemical analyses.
PG  - 2658-62
AB  - Nitric oxide (NO) is synthesized from arginine by nitric oxide synthase (NOS), 
      and citrulline which is generated can be recycled to arginine by 
      argininosuccinate synthetase (AS) and argininosuccinate lyase (AL). Rats were 
      injected with bacterial lipopolysaccharide (LPS), and expression of the inducible 
      isoform of NOS (iNOS), AS, and AL was analyzed. In RNA blot analysis, iNOS mRNA 
      was undetectable before the LPS treatment but was induced by LPS in the lung, 
      heart, liver, and spleen, and less strongly in the skeletal muscle and testis. AS 
      mRNA was induced in the lung and spleen, and AL mRNA was weakly induced in these 
      tissues. AS and AL mRNAs were abundant in the control liver and remained 
      unchanged after the treatment. Kinetic studies showed that iNOS mRNA increased 
      rapidly in both spleen and lung, reached a maximum 2-5 h after the treatment, and 
      decreased thereafter. On the other hand, AS mRNA increased more slowly and 
      reached a maximum in 6-12 h (by about 10-fold in the spleen and 2-fold in the 
      lung). AL mRNA in the spleen and lung increased slowly and remained high up to 24 
      h. In immunoblot analysis, increase of iNOS protein was evident in the lung, 
      liver, and spleen, and there was an increase of AS protein in the lung and 
      spleen. In immunohistochemical analysis, macrophages in the spleen that were 
      negative for iNOS and AS before LPS treatment were strongly positive for both 
      iNOS and AS after this treatment. As iNOS, AS, and AL were coinduced in rat 
      tissues and cells, citrulline-arginine recycling seems to be important in NO 
      synthesis under the conditions of stimulation.
FAU - Nagasaki, A
AU  - Nagasaki A
AD  - Department of Molecular Genetics, Kumamoto University School of Medicine, Japan.
FAU - Gotoh, T
AU  - Gotoh T
FAU - Takeya, M
AU  - Takeya M
FAU - Yu, Y
AU  - Yu Y
FAU - Takiguchi, M
AU  - Takiguchi M
FAU - Matsuzaki, H
AU  - Matsuzaki H
FAU - Takatsuki, K
AU  - Takatsuki K
FAU - Mori, M
AU  - Mori M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Lipopolysaccharides)
RN  - 0 (RNA, Messenger)
RN  - EC 1.14.13.39 (Nitric Oxide Synthase)
RN  - EC 4.3.2.1 (Argininosuccinate Lyase)
RN  - EC 6.3.4.5 (Argininosuccinate Synthase)
SB  - IM
MH  - Animals
MH  - Argininosuccinate Lyase/*biosynthesis/genetics
MH  - Argininosuccinate Synthase/*biosynthesis/genetics
MH  - Enzyme Induction
MH  - Immunohistochemistry
MH  - Kinetics
MH  - Lipopolysaccharides/*pharmacology
MH  - Liver/enzymology
MH  - Lung/enzymology
MH  - Macrophages/enzymology
MH  - Male
MH  - Myocardium/enzymology
MH  - Nitric Oxide Synthase/*biosynthesis/genetics
MH  - RNA, Messenger/genetics/metabolism
MH  - Rats
MH  - Rats, Wistar
MH  - Spleen/cytology/enzymology
EDAT- 1996/02/02 00:00
MHDA- 1996/02/02 00:01
CRDT- 1996/02/02 00:00
PHST- 1996/02/02 00:00 [pubmed]
PHST- 1996/02/02 00:01 [medline]
PHST- 1996/02/02 00:00 [entrez]
AID - S0021-9258(17)45722-X [pii]
AID - 10.1074/jbc.271.5.2658 [doi]
PST - ppublish
SO  - J Biol Chem. 1996 Feb 2;271(5):2658-62. doi: 10.1074/jbc.271.5.2658.