The roles of free radicals in amyotrophic lateral sclerosis

Danxia Liu

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

The mutations of the Cu,Zn superoxide dismutase (Cu,Zn-SOD) gene observed in amyotrophic lateral sclerosis (ALS) patients suggest that free radicals play a role in this fatal disease. Free radicals trigger oxidative damage to proteins, membrane lipids, and DNA, thereby destroying neurons. Mutations of the SOD gene may reduce its superoxide dismutase activity, thereby elevating free radical levels. In addition, the mutant SOD protein may function as a peroxidase to oxidize cellular components, and it may also react with peroxynitrite-a product of the reaction between superoxide and nitric oxide-to ultimately form nitrate proteins. The selective degeneration of motor neurons in ALS may be caused by the high level of Cu,Zn-SOD present in and the large number of glutamatergic synapses projecting to these neurons. Free radical-triggered and age-accumulated oxidation may modify the program controlling motor neuron death, thereby initiating apoptosis of motor neurons in young adults.

Original languageEnglish (US)
Pages (from-to)159-167
Number of pages9
JournalJournal of Molecular Neuroscience
Volume7
Issue number3
DOIs
StatePublished - Sep 1996

Fingerprint

Amyotrophic Lateral Sclerosis
Neurons
Free Radicals
Motor Neurons
Mutation
Genes
Peroxynitrous Acid
Mutant Proteins
Membrane Lipids
Superoxides
Nitrates
Synapses
Peroxidase
Superoxide Dismutase
Young Adult
Nitric Oxide
Proteins
Apoptosis
DNA
Oxidation

Keywords

  • Amyotrophic lateral sclerosis
  • Cu,Zn superoxide dismutase
  • free radicals
  • glutamate toxicity
  • motor neuron degeneration
  • oxidative damage
  • programmed neuron death

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience
  • Biochemistry
  • Genetics
  • Neuroscience(all)

Cite this

The roles of free radicals in amyotrophic lateral sclerosis. / Liu, Danxia.

In: Journal of Molecular Neuroscience, Vol. 7, No. 3, 09.1996, p. 159-167.

Research output: Contribution to journalArticle

@article{9073773dafef44a188edd15276ee73f1,
title = "The roles of free radicals in amyotrophic lateral sclerosis",
abstract = "The mutations of the Cu,Zn superoxide dismutase (Cu,Zn-SOD) gene observed in amyotrophic lateral sclerosis (ALS) patients suggest that free radicals play a role in this fatal disease. Free radicals trigger oxidative damage to proteins, membrane lipids, and DNA, thereby destroying neurons. Mutations of the SOD gene may reduce its superoxide dismutase activity, thereby elevating free radical levels. In addition, the mutant SOD protein may function as a peroxidase to oxidize cellular components, and it may also react with peroxynitrite-a product of the reaction between superoxide and nitric oxide-to ultimately form nitrate proteins. The selective degeneration of motor neurons in ALS may be caused by the high level of Cu,Zn-SOD present in and the large number of glutamatergic synapses projecting to these neurons. Free radical-triggered and age-accumulated oxidation may modify the program controlling motor neuron death, thereby initiating apoptosis of motor neurons in young adults.",
keywords = "Amyotrophic lateral sclerosis, Cu,Zn superoxide dismutase, free radicals, glutamate toxicity, motor neuron degeneration, oxidative damage, programmed neuron death",
author = "Danxia Liu",
year = "1996",
month = "9",
doi = "10.1007/BF02736837",
language = "English (US)",
volume = "7",
pages = "159--167",
journal = "Journal of Molecular Neuroscience",
issn = "0895-8696",
publisher = "Humana Press",
number = "3",

}

TY - JOUR

T1 - The roles of free radicals in amyotrophic lateral sclerosis

AU - Liu, Danxia

PY - 1996/9

Y1 - 1996/9

N2 - The mutations of the Cu,Zn superoxide dismutase (Cu,Zn-SOD) gene observed in amyotrophic lateral sclerosis (ALS) patients suggest that free radicals play a role in this fatal disease. Free radicals trigger oxidative damage to proteins, membrane lipids, and DNA, thereby destroying neurons. Mutations of the SOD gene may reduce its superoxide dismutase activity, thereby elevating free radical levels. In addition, the mutant SOD protein may function as a peroxidase to oxidize cellular components, and it may also react with peroxynitrite-a product of the reaction between superoxide and nitric oxide-to ultimately form nitrate proteins. The selective degeneration of motor neurons in ALS may be caused by the high level of Cu,Zn-SOD present in and the large number of glutamatergic synapses projecting to these neurons. Free radical-triggered and age-accumulated oxidation may modify the program controlling motor neuron death, thereby initiating apoptosis of motor neurons in young adults.

AB - The mutations of the Cu,Zn superoxide dismutase (Cu,Zn-SOD) gene observed in amyotrophic lateral sclerosis (ALS) patients suggest that free radicals play a role in this fatal disease. Free radicals trigger oxidative damage to proteins, membrane lipids, and DNA, thereby destroying neurons. Mutations of the SOD gene may reduce its superoxide dismutase activity, thereby elevating free radical levels. In addition, the mutant SOD protein may function as a peroxidase to oxidize cellular components, and it may also react with peroxynitrite-a product of the reaction between superoxide and nitric oxide-to ultimately form nitrate proteins. The selective degeneration of motor neurons in ALS may be caused by the high level of Cu,Zn-SOD present in and the large number of glutamatergic synapses projecting to these neurons. Free radical-triggered and age-accumulated oxidation may modify the program controlling motor neuron death, thereby initiating apoptosis of motor neurons in young adults.

KW - Amyotrophic lateral sclerosis

KW - Cu,Zn superoxide dismutase

KW - free radicals

KW - glutamate toxicity

KW - motor neuron degeneration

KW - oxidative damage

KW - programmed neuron death

UR - http://www.scopus.com/inward/record.url?scp=0030228631&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030228631&partnerID=8YFLogxK

U2 - 10.1007/BF02736837

DO - 10.1007/BF02736837

M3 - Article

C2 - 8906612

AN - SCOPUS:0030228631

VL - 7

SP - 159

EP - 167

JO - Journal of Molecular Neuroscience

JF - Journal of Molecular Neuroscience

SN - 0895-8696

IS - 3

ER -