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Current Knowledge on the Function of α-Methyl Acyl-CoA Racemase in Human Diseases
Branched chain fatty acids perform very important functions in human diet and drug metabolism. they cannot be metabolized in mitochondria and are instead processed and degraded in peroxisomes due to the presence of methyl groups on the carbon chains. Oxidative degradation pathways for lipids include...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7372137/ https://www.ncbi.nlm.nih.gov/pubmed/32760737 http://dx.doi.org/10.3389/fmolb.2020.00153 |
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author | Kong, Gyeyeong Lee, Hyunji Tran, Quangdon Kim, Chaeyeong Park, Jisoo Kwon, So Hee Kim, Seon-Hwan Park, Jongsun |
author_facet | Kong, Gyeyeong Lee, Hyunji Tran, Quangdon Kim, Chaeyeong Park, Jisoo Kwon, So Hee Kim, Seon-Hwan Park, Jongsun |
author_sort | Kong, Gyeyeong |
collection | PubMed |
description | Branched chain fatty acids perform very important functions in human diet and drug metabolism. they cannot be metabolized in mitochondria and are instead processed and degraded in peroxisomes due to the presence of methyl groups on the carbon chains. Oxidative degradation pathways for lipids include α- and β-oxidation and several pathways. In all metabolic pathways, α-methyl acyl-CoA racemase (AMACR) plays an essential role by regulating the metabolism of lipids and drugs. AMACR regulates β-oxidation of branched chain lipids in peroxisomes and mitochondria and promotes chiral reversal of 2-methyl acids. AMACR defects cause sensory-motor neuronal and liver abnormalities in humans. These phenotypes are inherited and are caused by mutations in AMACR. In addition, AMACR has been found to be overexpressed in prostate cancer. In addition, the protein levels of AMACR have increased significantly in many types of cancer. Therefore, AMACR may be an important marker in tumors. In this review, a comprehensive overview of AMACR studies in human disease will be described. |
format | Online Article Text |
id | pubmed-7372137 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-73721372020-08-04 Current Knowledge on the Function of α-Methyl Acyl-CoA Racemase in Human Diseases Kong, Gyeyeong Lee, Hyunji Tran, Quangdon Kim, Chaeyeong Park, Jisoo Kwon, So Hee Kim, Seon-Hwan Park, Jongsun Front Mol Biosci Molecular Biosciences Branched chain fatty acids perform very important functions in human diet and drug metabolism. they cannot be metabolized in mitochondria and are instead processed and degraded in peroxisomes due to the presence of methyl groups on the carbon chains. Oxidative degradation pathways for lipids include α- and β-oxidation and several pathways. In all metabolic pathways, α-methyl acyl-CoA racemase (AMACR) plays an essential role by regulating the metabolism of lipids and drugs. AMACR regulates β-oxidation of branched chain lipids in peroxisomes and mitochondria and promotes chiral reversal of 2-methyl acids. AMACR defects cause sensory-motor neuronal and liver abnormalities in humans. These phenotypes are inherited and are caused by mutations in AMACR. In addition, AMACR has been found to be overexpressed in prostate cancer. In addition, the protein levels of AMACR have increased significantly in many types of cancer. Therefore, AMACR may be an important marker in tumors. In this review, a comprehensive overview of AMACR studies in human disease will be described. Frontiers Media S.A. 2020-07-14 /pmc/articles/PMC7372137/ /pubmed/32760737 http://dx.doi.org/10.3389/fmolb.2020.00153 Text en Copyright © 2020 Kong, Lee, Tran, Kim, Park, Kwon, Kim and Park. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Molecular Biosciences Kong, Gyeyeong Lee, Hyunji Tran, Quangdon Kim, Chaeyeong Park, Jisoo Kwon, So Hee Kim, Seon-Hwan Park, Jongsun Current Knowledge on the Function of α-Methyl Acyl-CoA Racemase in Human Diseases |
title | Current Knowledge on the Function of α-Methyl Acyl-CoA Racemase in Human Diseases |
title_full | Current Knowledge on the Function of α-Methyl Acyl-CoA Racemase in Human Diseases |
title_fullStr | Current Knowledge on the Function of α-Methyl Acyl-CoA Racemase in Human Diseases |
title_full_unstemmed | Current Knowledge on the Function of α-Methyl Acyl-CoA Racemase in Human Diseases |
title_short | Current Knowledge on the Function of α-Methyl Acyl-CoA Racemase in Human Diseases |
title_sort | current knowledge on the function of α-methyl acyl-coa racemase in human diseases |
topic | Molecular Biosciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7372137/ https://www.ncbi.nlm.nih.gov/pubmed/32760737 http://dx.doi.org/10.3389/fmolb.2020.00153 |
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