Molecular cloning of cDNA for nonhepatic mitochondrial arginase (arginase II) and comparison of its induction with nitric oxide synthase in a murine macrophage-like cell line

FEBS Letters ◽  
1996 ◽  
Vol 395 (2-3) ◽  
pp. 119-122 ◽  
Author(s):  
Tomomi Gotoh ◽  
Takashi Sonoki ◽  
Akitoshi Nagasaki ◽  
Kazutoyo Terada ◽  
Masaki Takiguchi ◽  
...  
1998 ◽  
Vol 275 (5) ◽  
pp. E740-E747 ◽  
Author(s):  
Sidney M. Morris ◽  
Diane Kepka-Lenhart ◽  
Li-Chun Chen

Activated macrophages avidly consume arginine via the action of inducible nitric oxide synthase (iNOS) and/or arginase. In contrast to our knowledge regarding macrophage iNOS expression, the stimuli and mechanisms that regulate expression of the cytosolic type I (arginase I) or mitochondrial type II (arginase II) isoforms of arginase in macrophages are poorly defined. We show that one or both arginase isoforms may be induced in the RAW 264.7 murine macrophage cell line and that arginase expression is regulated independently of iNOS expression. For example, 8-bromo-cAMP strongly induced both arginase I and II mRNAs but not iNOS. Whereas interferon-γ induced iNOS but not arginase, 8-bromo-cAMP and interferon-γ mutually antagonized induction of iNOS and arginase I mRNAs. Dexamethasone, which did not induce either arginase or iNOS, almost completely abolished induction of arginase I mRNA by 8-bromo-cAMP but enhanced induction of arginase II mRNA. Lipopolysaccharide (LPS) induced arginase II mRNA, but 8-bromo-cAMP plus LPS resulted in synergistic induction of both arginase I and II mRNAs. In all cases, increases in arginase mRNAs were sufficient to account for the increases in arginase activity. These complex patterns of expression suggest that the arginase isoforms may play distinct, although partially overlapping, functional roles in macrophage arginine metabolism.


1995 ◽  
Vol 49 (2) ◽  
pp. 105-115 ◽  
Author(s):  
Salvatore Milano ◽  
Francesco Arcoleo ◽  
Mariella Dieli ◽  
Rita D'Agostino ◽  
Pietro D'Agostino ◽  
...  

2018 ◽  
Vol 13 (1) ◽  
pp. 1934578X1801300 ◽  
Author(s):  
Zhi-Jun Zhang ◽  
Wu-Fu Chen ◽  
Bo-Rong Peng ◽  
Zhi-Hong Wen ◽  
Ping-Jyun Sung

A new natural marine nor-sesquiterpenoid, (+)-pathylactone A (1), along with a know nor-sesquiterpenoid, napalilactoe (2), were isolated from the octocoral Paralemnalia thyrsoides. The structure of 1 was established on the basis of spectroscopic methods and by comparison of the spectral data with those of synthetic analogues. Nor-sesquiterpenoid 1 was found to inhibit the protein experssion of pro-inflammatory inducible nitric oxide synthase (iNOS) in a murine macrophage-like cell line.


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