نتایج جستجو برای: argininosuccinate synthase

تعداد نتایج: 83823  

2012
Ramadan B Sopi Syed IA Zaidi Mitko Mladenov Hazbije Sahiti Zahide Istrefi Icko Gjorgoski Azem Lajçi Muharrem Jakupaj

BACKGROUND Hyperoxia is shown to impair airway relaxation via limiting L-arginine bioavailability to nitric oxide synthase (NOS) and reducing NO production as a consequence. L-arginine can also be synthesized by L-citrulline recycling. The role of L-citrulline supplementation was investigated in the reversing of hyperoxia-induced impaired relaxation of rat tracheal smooth muscle (TSM). METHOD...

Journal: :The Journal of biological chemistry 2012
Claudiana Lameu Cleber A Trujillo Telma T Schwindt Priscilla D Negraes Micheli M Pillat Katia L P Morais Ivo Lebrun Henning Ulrich

The diffusible messenger NO plays multiple roles in neuroprotection, neurodegeneration, and brain plasticity. Argininosuccinate synthase (AS) is a ubiquitous enzyme in mammals and the key enzyme of the NO-citrulline cycle, because it provides the substrate L-arginine for subsequent NO synthesis by inducible, endothelial, and neuronal NO synthase (NOS). Here, we provide evidence for the particip...

2017
Jiri Volf Ondrej Polansky Zuzana Sekelova Philippe Velge Catherine Schouler Bernd Kaspers Ivan Rychlik

Gut microbiota is of considerable importance for each host. Despite this, germ-free animals can be obtained and raised to sexual maturity and consequences of the presence or absence of gut microbiota on gene expression of the host remain uncharacterised. In this study, we performed an unbiased study of protein expression in the caecum of germ-free and colonised chickens. The major difference be...

1999
TOMOMI GOTOH HIROTAKA ISOBE MASATAKA MORI Tomomi Gotoh

Salimuddin,Akitoshi Nagasaki, Tomomi Gotoh, Hirotaka Isobe, and Masataka Mori. Regulation of the genes for arginase isoforms and related enzymes in mouse macrophages by lipopolysaccharide. Am. J. Physiol. 277 (Endocrinol. Metab. 40): E110–E117, 1999.—Arginase exists in two isoforms, the hepatic (arginase I) and extrahepatic types (arginase II). Arginase I is markedly induced in rat peritoneal m...

Journal: :The Journal of biological chemistry 2008
Yanmei Zhao Jinfang Zhang Huiying Li Yiyu Li Jie Ren Ming Luo Xiaofeng Zheng

NADPH is an important cofactor in many biosynthesis pathways that control fundamental cellular processes. We recently determined the crystal structure of HSCARG, with functions previously unknown, and demonstrated it is an NADPH sensor, which undergoes restructuring and redistribution in response to changes of intracellular NADPH/NADP levels. In this study, we identified argininosuccinate synth...

2017
Takafumi Miyamoto Paulisally Hau Yi Lo Naomi Saichi Koji Ueda Makoto Hirata Chizu Tanikawa Koichi Matsuda

Laboratory of Genome Technology, Human Genome Center, Institute of Medical Science, University of Tokyo, Tokyo, Japan. Cancer Proteomics Group, Genome Center, Japanese Foundation for Cancer Research, Tokyo, Japan. Laboratory of Clinical Genome Sequencing, Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, University of Tokyo, Tokyo, Japan. *Correspon...

2003
Larry P. Solomonson Brenda R. Flam Laura C. Pendleton L. Goodwin Duane C. Eichler

catalyzes the production of NO from the amino acid arginine in endothelial cells, plays a key role in vasoregulation as well as in other important physiological processes such as angiogenesis. Impaired production of endothelial NO has been associated with hypertension, heart failure, hypercholesterolemia, atherosclerosis and diabetes (Govers and Rabelink, 2001; Vallance and Chan, 2001; Maxwell,...

Journal: :The American journal of physiology 1999
Salimuddin Akitoshi Nagasaki Tomomi Gotoh Hirotaka Isobe Masataka Mori

Arginase exists in two isoforms, the hepatic (arginase I) and extrahepatic types (arginase II). Arginase I is markedly induced in rat peritoneal macrophages and rat tissues in vivo by bacterial lipopolysaccharide (LPS). In contrast, both arginase I and arginase II are induced in LPS-activated mouse peritoneal macrophages. In the present study, expression of arginase isoforms and related enzymes...

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