نتایج جستجو برای: cuzn superoxide dismutase 1 sod1

تعداد نتایج: 2775979  

Journal: :The Biochemical journal 1981
K Grankvist S L Marklund I B Täljedal

Exogenous superoxide dismutase, catalase and scavengers of the hydroxyl radical protect pancreatic-islet cells against the toxic actions of alloxan in vitro [Grankvist et al. (1979) Biochem. J. 182, 17--25]. To test whether the extraordinary sensitivity of islet cells to alloxan is due to a deficiency of endogenous enzymes protecting against oxygen-reduction products, we assayed CuZn-superoxide...

Journal: :Neuron 2004
Jian Liu Concepción Lillo P.Andreas Jonsson Christine Vande Velde Christopher M Ward Timothy M Miller Jamuna R Subramaniam Jeffery D Rothstein Stefan Marklund Peter M Andersen Thomas Brännström Ole Gredal Philip C Wong David S Williams Don W Cleveland

One cause of amyotrophic lateral sclerosis (ALS) is mutation in ubiquitously expressed copper/zinc superoxide dismutase (SOD1), but the mechanism of toxicity to motor neurons is unknown. Multiple disease-causing mutants, but not wild-type SOD1, are now demonstrated to be recruited to mitochondria, but only in affected tissues. This is independent of the copper chaperone for SOD1 and dismutase a...

Journal: :Neuro endocrinology letters 2015
Hidetaka Hamasaki Yu Takeuchi Yoshinori Masui Yasuyuki Ohta Koji Abe Hiide Yoshino Hidekatsu Yanai

Familial amyotrophic lateral sclerosis (ALS) are caused by the mutations in the copper (Cu) / zinc (Zn) superoxide dismutase 1 (SOD1) gene. SOD1 has been reported to play a critical role in glucose metabolism in yeast and cell models, and mice. However, effects of SOD1 for glucose metabolism in humans remain unknown. A 72-year-old woman was admitted to our hospital due to hyperglycemia. She sho...

HJ Kim JJ Sung KW Lee M Kim WM Cho YH Hong

Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disorder characterized by the progressive loss of motor neurons leading to paralysis and death. Mutations of the human Cu/Zn superoxide dismutase (SOD1) are found in some cases of familial ALS (fALS). Recent evidences suggest the accumulation of intracellular calcium is one of the primary mechanisms of motor neuronal degeneration. In th...

Journal: :Cancer research 2005
Rita A Busuttil Ana Maria Garcia Carlos Cabrera Armando Rodriguez Yousin Suh Woo Ho Kim Ting-Ting Huang Jan Vijg

Reactive oxygen species have been implicated as a cause of cancer and aging in mammals. Mice deficient for the antioxidant enzyme CuZn-superoxide dismutase (Sod1) have a decreased life span and an elevated incidence of liver cancer. To test the hypothesis that the cancer-prone phenotype in such mice is due to accelerated spontaneous mutation accumulation, we crossed these mutants with mice harb...

Journal: :Human molecular genetics 2010
Bradley J Turner Steven Ackerley Kay E Davies Kevin Talbot

Mutant superoxide dismutase 1 (SOD1) action within non-neuronal cells is implicated in damage to spinal motor neurons in a genetic form of amyotrophic lateral sclerosis (ALS). Central nervous system glial cells such as astrocytes and microglia drive progression in transgenic mutant SOD1 mice, however, the role of myelinating glia remains unclear. Specifically, peripheral myelinating glial cells...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2008
Jose C Juarez Mari Manuia Mark E Burnett Oscar Betancourt Benoit Boivin David E Shaw Nicholas K Tonks Andrew P Mazar Fernando Doñate

Superoxide dismutase 1 (SOD1) is an abundant copper/zinc enzyme found in the cytoplasm that converts superoxide into hydrogen peroxide and molecular oxygen. Tetrathiomolybdate (ATN-224) has been recently identified as an inhibitor of SOD1 that attenuates FGF-2- and VEGF-mediated phosphorylation of ERK1/2 in endothelial cells. However, the mechanism for this inhibition was not elucidated. Growth...

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