Amyotrophic lateral sclerosis glutamate

Trotti, D Rolfs, A., Danbolt, N. C Brown, R. H Jr., and Hediger, M. A. (1999) SOD1 mutants linked to amyotrophic lateral sclerosis selectively inactivate a glial glutamate transporter. [erratum appears in Nat Neurosci 1999 Sep 2(9) 848], Nat. Neurosci. 2,427—433. 

Bruno V, Battaglia G, Copani A, et al (2001) Metabotropic glutamate receptor subtypes as targets for neuroprotective drugs. J Cereb Blood FlowMetab 21 1013-1033 Bryson HM, Fulton B, Benfield P (1996) Riluzole—a review of its pharmacodynamic and pharmacokinetic properties and therapeutic potential in amyotrophic lateral sclerosis. Drugs 52 549-563... 

Lin C. L., Bristol L. A., Jin L., Dykes-Hoberg M., Crawford T., Clawson L., and Rothstein J. D. (1998). Aberrant RNA processing in a neurodegenerative disease the cause for absent EAAT2, a glutamate transporter, in amyotrophic lateral sclerosis. Neuron 20 589-602. 

Munch C., Ebstein M., Seefried U., Zhu B., Stamm S., Landwehrmeyer G. B., Ludolph A. C., Schwalenstocker B., and Meyer T. (2002). Alternative splicing of the 5 -sequences of the mouse EAAT2 glutamate transporter and expression in a transgenic model for amyotrophic lateral sclerosis. J. Neurochem. 82 594-603. 

Rothstein J. D., Martin L. J., and Kuncl R. W. (1992). Decreased glutamate transport by the brain and spinal cord in amyotrophic lateral sclerosis. N. Engl. J. Med. 326 1464-1468. 

Shaw P J. and Ince P G. (1997). Glutamate, excitotoxicity and amyotrophic lateral sclerosis. J. Neurol. 244 Suppl 2 S3-S14. 

The excessive activity of excitatory amino acids, such as L-glutamate and L-aspartate, followed by elevation of intracellular free Ca2+ concentration and accumulation of free radicals has been postulated to underlie the neurodegeneration that occurs after ischemic insults and trauma. Additionally, an excitotoxic component has been shown to play an important role in the pathogenesis of chronic neurodegenerative disorders, such as Alzheimer s disease, Parkinson s disease, amyotrophic lateral sclerosis, and Huntington s disease, which are characterized by progressive loss of neuronal elements. 

Polar biomarkers have also been investigated by NMR (SO) in postmortem BT samples. These samples were treated with perchloric acid, and metabolic extracts were analyzed to compare AD with amyotrophic lateral sclerosis (ALS) (80). After multivariate statistical analysis of the 8 AD and the 11 ALS samples, a high score in the statistical parameters of OPLS was obtained with the exclusion of 1 AD sample. Increased concentration of branched amino acids, alanine, acetate, glutamine, glutamate, and glyceropho-sphocholine in AD patients was observed when compared to ALS (80). 

V. Glutamate Release from Gliosomes in a Mouse Model of Amyotrophic Lateral Sclerosis... 

Dal Canto, M. C., and Gurney, M. E. (1994). Development of central nervous system pathology in a murine transgenic model of human amyotrophic lateral sclerosis. Am.J. Pathol. 145, 1271-1279. Daniels, K. K., and Vickroy, T. W. (1999). Reversible activation of glutamate transport in rat brain glia by protein kinase C and an okadaic acid-sensitive phosphoprotein phosphatase. Neurochem. Res. 24, 1017-1025. 

Raiteri, L., Paolucd, E., Prisco, S., Raiteri, M., and Bonanno, G. (2003). Activation of a glycine transporter on spinal cord neurons causes enhanced glutamate release in a mouse model of amyotrophic lateral sclerosis. Br.J. Pharmacol. 138, 1021-1025. 

Pathological activation of glutamate receptors is a common feature and one of the primary causes of neuronal death in acute neuronal injury (such as trauma, epilepsy, and brain ischemia) and chronic neurodegenerative diseases (such as Parkinson s disease, Alzheimer diseases, amyotrophic lateral sclerosis, and AIDS dementia) (Choi, 1988 Doble, 1999 Lipton and Rosemberg, 1994). In particular, elevation of extracellular glutamate level is a key factor in the development of neuronal damage under ischemic conditions. 

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