کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5905231 | 1159869 | 2016 | 30 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Mutant SOD1 mediated pathogenesis of Amyotrophic Lateral Sclerosis
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کلمات کلیدی
Upper motor neuronsEndoplasmic Reticulum-Golgi intermediate compartmenttdp43ERGICRXRRetinoid X receptormRNASOD1AAVC9orf72familial ALS - ALS خانوادگیFUs - FUSO2− - O2-Hydrogen peroxide - آب اکسیژنهAdenosine Triphosphate - آدنوزین تری فسفاتATP - آدنوزین تری فسفات یا ATP superoxide anion - آنیون سوپر اکسیدamyotrophic lateral sclerosis - اسکلروز جانبی آمیوتروفیکOxygen - اکسیژنALS - بیماری اسکلروز جانبی آمیوتروفیکTar - تارNeurodegeneration - تولید نوروژنیکmutations - جهش یا میوتیشنmessenger ribonucleic acid - رسوب ریبونوکلئیک اسیدSOD - سدLower motor neurons - نورونهای حرکتی پایینH2O2 - هیدروژن پراکسیدAdeno-associated viruses - ویروس های مرتبط با آدنوtar DNA-binding protein 43 - پروتئین متصل به DNA DNA 39chromosome 9 open reading frame 72 - کروموزوم 9 قاب خواندن باز 72
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
ژنتیک
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Amyotrophic lateral sclerosis (ALS) is a neural disorder that causes death of the motor neurons in the brain and spinal cord; this affects the voluntary muscles and gradually leads to paralysis of the whole body. Most ALS cases are sporadic, though about 5-10% are familial. ALS is caused by multiple factors including mutation in any one of a number of specific genes, one of the most frequently affected is superoxide dismutase (SOD) 1. Alterations in SOD 1 have been linked with several variants of familial ALS. SOD 1 is a powerful antioxidant enzyme that protects cells from the damaging effects of superoxide radicals. The enzyme binds both copper and zinc ions that are directly involved in the deactivation of toxic superoxide radicals. Mutated SOD1 gene can acquire both gain and loss of function mutations. The most commonly identified mutations in SOD1 that affect protein activity are D90A, A4V and G93A. Deleterious mutations have been shown to modify SOD1 activity, which leads to the accumulation of highly toxic hydroxyl radicals. Accumulation of these free radicals causes degradation of both nuclear and mitochondrial DNA and protein misfolding, features which can be used as pathological indicators associated with ALS. Numerous clinical trials have been carried out over last few years with limited success. In some patients advanced techniques like gene and stem cell therapy have been trialed. However no definitive treatment option can provide a cure and currently ALS is managed by drugs and other supportive therapies. Consequently there is a need to identify new approaches for treatment of this ultimately fatal disease.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Gene - Volume 577, Issue 2, 15 February 2016, Pages 109-118
Journal: Gene - Volume 577, Issue 2, 15 February 2016, Pages 109-118
نویسندگان
Simran J. Kaur, Stephanie R. McKeown, Shazia Rashid,