نتایج جستجو برای: cuzn superoxide dismutase sod1

تعداد نتایج: 35610  

Journal: :American journal of physiology. Heart and circulatory physiology 2001
M Zanetti J Sato Z S Katusic T O'Brien

Increased production of oxygen free radicals is an important mechanism of endothelial dysfunction in diabetes mellitus. Our goal was to test whether adenovirus (Ad)-mediated gene transfer of copper/zinc (CuZn) or manganese superoxide dismutase (Mn SOD) improves relaxation of diabetic vessels. The aortas from 9 alloxan-induced diabetic mellitus (DM) and 16 control rabbits were used. Control and ...

2016
Gareth S. A. Wright Svetlana V. Antonyuk S. Samar Hasnain

A proportion of Amyotrophic lateral sclerosis (ALS) cases result from impaired mutant superoxide dismutase-1 (SOD1) maturation. The copper chaperone for SOD1 (hCCS) forms a transient complex with SOD1 and catalyses the final stages of its maturation. We find that a neurodegenerative disease-associated hCCS mutation abrogates the interaction with SOD1 by inhibiting hCCS zinc binding. Analogously...

Journal: :The Journal of neuroscience : the official journal of the Society for Neuroscience 2002
Cynthia M J Higgins Cheolwha Jung Hongliu Ding Zuoshang Xu

Mutations in Cu, Zn superoxide dismutase (SOD1) cause a fraction of amyotrophic lateral sclerosis (ALS), which involves motoneuron degeneration, paralysis, and death. An acquired activity by mutant SOD1 is responsible for the cellular toxicity, but how mutant SOD1 kills motoneurons is unclear. In transgenic mouse models of ALS, mitochondrial degeneration occurs early, before disease onset, rais...

Journal: :Genes & development 2008
Hideki Nishitoh Hisae Kadowaki Atsushi Nagai Takeshi Maruyama Takanori Yokota Hisashi Fukutomi Takuya Noguchi Atsushi Matsuzawa Kohsuke Takeda Hidenori Ichijo

Mutation in Cu/Zn-superoxide dismutase (SOD1) is a cause of familial amyotrophic lateral sclerosis (ALS). Mutant SOD1 protein (SOD1(mut)) induces motor neuron death, although the molecular mechanism of SOD1(mut)-induced cell death remains controversial. Here we show that SOD1(mut) specifically interacted with Derlin-1, a component of endoplasmic reticulum (ER)-associated degradation (ERAD) mach...

Journal: :Cancer epidemiology, biomarkers & prevention : a publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology 2007
Daehee Kang Kyoung-Mu Lee Sue Kyung Park Sonja I Berndt Ulrike Peters Douglas Reding Nilanjan Chatterjee Robert Welch Stephen Chanock Wen-Yi Huang Richard B Hayes

Superoxide dismutase (SOD) plays a key role in the detoxification of superoxide free radicals. We evaluated the association of prostate cancer with genetic polymorphisms in SOD1 (CuZn-SOD; IVS3-251A>G), SOD2 [MnSOD; Ex2+24T>C (V16A)], and SOD3 (EC-SOD; IVS1+186C>T, Ex3-631C>G, Ex3-516C>T, and Ex3-489C>T), the three main isoforms of SOD. Prostate cancer cases (n = 1,320) from the screening arm o...

2016
Itsuki Anzai Keisuke Toichi Eiichi Tokuda Atsushi Mukaiyama Shuji Akiyama Yoshiaki Furukawa

Dominant mutations in Cu/Zn-superoxide dismutase (SOD1) gene have been shown to cause a familial form of amyotrophic lateral sclerosis (SOD1-ALS). A major pathological hallmark of this disease is abnormal accumulation of mutant SOD1 oligomers in the affected spinal motor neurons. While no effective therapeutics for SOD1-ALS is currently available, SOD1 oligomerization will be a good target for ...

Journal: :Circulation research 1992
T Abrahamsson U Brandt S L Marklund P O Sjöqvist

Extracellular superoxide dismutase type C (EC-SOD C) is a secretory SOD isoenzyme that, in vivo, is bound to heparan sulfate proteoglycans in the glycocalyx of various cell types (e.g., endothelial cells) and in the connective tissue matrix. The aim of this study was to investigate the efficacy of vascular bound EC-SOD C in protecting arterial relaxation mediated by endothelium-derived relaxing...

Journal: :Muscles 2023

Amyotrophic lateral sclerosis (ALS) is a complex systemic disease that primarily involves motor neuron dysfunction and skeletal muscle atrophy. One commonly used mouse model to study ALS was generated by transgenic expression of mutant form human superoxide dismutase 1 (SOD1) gene harboring single amino acid substitution glycine alanine at codon 93 (G93A*SOD1). Although mutant-SOD1 ubiquitously...

Journal: :Neuron 2015
Adrian Israelson Dara Ditsworth Shuying Sun SungWon Song Jason Liang Marian Hruska-Plochan Melissa McAlonis-Downes Salah Abu-Hamad Guy Zoltsman Tom Shani Marcus Maldonado Anh Bui Michael Navarro Huilin Zhou Martin Marsala Brian K. Kaspar Sandrine Da Cruz Don W. Cleveland

Mutations in superoxide dismutase (SOD1) cause amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by loss of motor neurons and accompanied by accumulation of misfolded SOD1 onto the cytoplasmic faces of intracellular organelles, including mitochondria and the endoplasmic reticulum (ER). Using inhibition of misfolded SOD1 deposition onto mitochondria as an assay, a ch...

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