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المؤلفون: Lena Brundin, Martha L. Escobar Galvis, Viviane Labrie, Keerthi Thirtamara-Rajamani, Patrik Brundin, Peipei Li
المصدر: Journal of Parkinson's Disease
مصطلحات موضوعية: 0301 basic medicine, Kynurenine pathway, Parkinson's disease, Carboxy-Lyases, Review, neuroinflammation, Pathogenesis, 03 medical and health sciences, Cellular and Molecular Neuroscience, chemistry.chemical_compound, 0302 clinical medicine, medicine, Missense mutation, Animals, Humans, oxidative stress, Gene, Genetics, Inflammation, Parkinsonism, Brain, Parkinson Disease, Quinolinic Acid, medicine.disease, 3. Good health, 030104 developmental biology, ACMSD, chemistry, Mutation, Parkinson’s disease, Neurology (clinical), NAD+ kinase, excitotoxicity, 030217 neurology & neurosurgery, Quinolinic acid, kynurenine pathway
الوصف: Several large genome wide association studies have identified a locus in close proximity to the gene encoding the enzyme aminocarboxymuconate-semialdehyde-decarboxylase (ACMSD) to be associated with the risk for Parkinson’s disease (PD), tentatively suggesting that this enzyme might influence PD pathogenesis. Further support for this comes from the recent identification of a disease-segregating stop codon mutation in ACMSD in a family with Parkinsonism, and a missense mutation in the ACMSD gene predicted to disrupt enzyme function in an individual with typical PD. ACMSD is part of the kynurenine pathway, responsible for the catalytic breakdown of tryptophan into NAD+, generating several neuroactive metabolites in the process. The enzyme is located at a key branch-point of the pathway, limiting the production of the neurotoxin quinolinic acid, which has excitotoxic and inflammatory properties. In this review, we discuss the genetic findings in light of the functions of ACMSD and its potential involvement in PD pathogenesis.
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2e57a70b9fcc7373bcba4765f6c5444Test
https://pubmed.ncbi.nlm.nih.gov/29103054Test -
2دورية أكاديمية
المؤلفون: Thirtamara-Rajamani, Keerthi1, Peipei Li1, Escobar Galvis, Martha L.1, Labrie, Viviane1, Brundin, Patrik1, Brundin, Lena1 Lena.Brundin@vai.org
المصدر: Journal of Parkinson's Disease. 2017, Vol. 7 Issue 4, p577-587. 11p.
مصطلحات موضوعية: *PARKINSON'S disease treatment, *ENZYME inhibitors, *DIAGNOSIS, *KYNURENINE, *METABOLITES, *THERAPEUTICS
مستخلص: Several large genome wide association studies have identified a locus in close proximity to the gene encoding the enzyme aminocarboxymuconate-semialdehyde-decarboxylase (ACMSD) to be associated with the risk for Parkinson's disease (PD), tentatively suggesting that this enzyme might influence PD pathogenesis. Further support for this comes from the recent identification of a disease-segregating stop codon mutation in ACMSD in a family with Parkinsonism, and a missense mutation in the ACMSD gene predicted to disrupt enzyme function in an individual with typical PD. ACMSD is part of the kynurenine pathway, responsible for the catalytic breakdown of tryptophan into NAD+, generating several neuroactive metabolites in the process. The enzyme is located at a key branch-point of the pathway, limiting the production of the neurotoxin quinolinic acid, which has excitotoxic and inflammatory properties. In this review, we discuss the genetic findings in light of the functions of ACMSD and its potential involvement in PD pathogenesis. [ABSTRACT FROM AUTHOR]