نتایج جستجو برای: cuzn superoxide dismutase sod1

تعداد نتایج: 35610  

Journal: :Atherosclerosis 2000
P Strålin S L Marklund

Oxygen free radicals as well as immunological reactions have been suggested to play important roles in atherogenesis and other pathological processes of the blood vessel wall. We have previously shown that the vascular wall contains exceptionally large amounts of extracellular superoxide dismutase (EC-SOD) and that the enzyme is produced and secreted to the extracellular space by the smooth mus...

Journal: :Arteriosclerosis and thrombosis : a journal of vascular biology 1992
H A Lehr M Becker S L Marklund C Hübner K E Arfors A Kohlschütter K Messmer

Low density lipoprotein modified by oxidation (Ox-LDL) causes adhesion of leukocytes to the endothelium, a feature common in early atherogenesis. Because leukocyte adhesion under various pathophysiological conditions involves superoxide generation, we explored the possibility that superoxide is likewise involved in leukocyte adhesion in response to Ox-LDL. For our studies, we used the dorsal sk...

Journal: :Biochemistry 2000
A L Lamb A S Torres T V O'Halloran A C Rosenzweig

Copper, zinc superoxide dismutase (SOD1) is activated in vivo by the copper chaperone for superoxide dismutase (CCS). The molecular mechanisms by which CCS recognizes and docks with SOD1 for metal ion insertion are not well understood. Two models for the oligomerization state during copper transfer have been proposed: a heterodimer comprising one monomer of CCS and one monomer of SOD1 and a dim...

Journal: :Cell 2013
Amit R. Reddi Valeria C. Culotta

Cu/Zn superoxide dismutase (SOD1) is an abundant enzyme that has been best studied as a regulator of antioxidant defense. Using the yeast Saccharomyces cerevisiae, we report that SOD1 transmits signals from oxygen and glucose to repress respiration. The mechanism involves SOD1-mediated stabilization of two casein kinase 1-gamma (CK1γ) homologs, Yck1p and Yck2p, required for respiratory repressi...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2008
Christine Vande Velde Timothy M Miller Neil R Cashman Don W Cleveland

Mutations in copper/zinc superoxide dismutase (SOD1) are causative for dominantly inherited amyotrophic lateral sclerosis (ALS). Despite high variability in biochemical properties among the disease-causing mutants, a proportion of both dismutase-active and -inactive mutants are stably bound to spinal cord mitochondria. This mitochondrial proportion floats with mitochondria rather than sedimenti...

Journal: :Investigative ophthalmology & visual science 1998
A Behndig B Svensson S L Marklund K Karlsson

PURPOSE The authors determined the levels of the secreted, interstitially located extracellular superoxide dismutase (EC-SOD), the cytosolic copper- and zinc-containing SOD (CuZn-SOD), and the mitochondrial manganese-containing SOD (Mn-SOD) in tears, cornea, sclera, aqueous humor, lens, vitreous body, and retina of the human eye. METHODS SOD enzymatic activity was determined by the direct spe...

Journal: :The Biochemical journal 2007
Pedro Iñarrea Hadi Moini Derick Han Daniel Rettori Ignacio Aguiló Maria Angeles Alava María Iturralde Enrique Cadenas

IMS (intermembrane space) SOD1 (Cu/Zn-superoxide dismutase) is inactive in isolated intact rat liver mitochondria and is activated following oxidative modification of its critical thiol groups. The present study aimed to identify biochemical pathways implicated in the regulation of IMS SOD1 activity and to assess the impact of its functional state on key mitochondrial events. Exogenous H2O2 (5 ...

Journal: :Chemical communications 2012
Inhee Choi Young In Yang Eunhye Jeong Kihoon Kim Surin Hong Taewook Kang Jongheop Yi

In this communication, we describe a new, simplified colorimetric method for in situ tracking of structural evolution of Cu/Zn-superoxide dismutase (SOD1) aggregates, based on changes in plasmonic coupling between gold nanoparticles (GNPs) embedded along the structural backbone of the SOD1 aggregates.

Journal: :Genetics 1994
P Chary D Dillon A L Schroeder D O Natvig

Enzymatic superoxide-dismutase activity is believed to be important in defense against the toxic effects of superoxide. Although superoxide dismutases are among the best studied proteins, numerous questions remain concerning the specific biological roles of the various superoxide-dismutase types. In part, this is because the proposed damaging effects of superoxide are manifold, ranging from ina...

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