Journal article 1146 views
Role of α-Methylacyl-CoA Racemase (Amacr) and peroxisomal Multifunctional Enzyme 1 (Mfe-1) in bile acid synthesis in mice
Biochemical Journal
Swansea University Authors:
William Griffiths , Yuqin Wang
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DOI (Published version): 10.1042/BJ20130915
Abstract
Cholesterol is catabolized to bile acids by peroxisomal β-oxidation in which the side-chain of C27-bile acid intermediates is shortened by three carbon atoms to form mature C24-bile acids. Knock-out mouse models deficient in α-methylacyl coenzyme A racemase (Amacr) or multifunctional enzyme type 2 (...
Published in: | Biochemical Journal |
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Published: |
2014
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URI: | https://cronfa.swan.ac.uk/Record/cronfa17830 |
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2019-09-24T16:07:45.8226127 v2 17830 2014-04-17 Role of α-Methylacyl-CoA Racemase (Amacr) and peroxisomal Multifunctional Enzyme 1 (Mfe-1) in bile acid synthesis in mice 3316b1d1b524be1831790933eed1c26e 0000-0002-4129-6616 William Griffiths William Griffiths true false c92729b58622f9fdf6a0e7d8f4ce5081 0000-0002-3063-3066 Yuqin Wang Yuqin Wang true false 2014-04-17 BMS Cholesterol is catabolized to bile acids by peroxisomal β-oxidation in which the side-chain of C27-bile acid intermediates is shortened by three carbon atoms to form mature C24-bile acids. Knock-out mouse models deficient in α-methylacyl coenzyme A racemase (Amacr) or multifunctional enzyme type 2 (Mfe-2), in which this β-oxidation pathway is prevented, display a residual mature C24-bile acid pool although greatly reduced, which implies the existence of alternative pathways of bile acid synthesis. One alternative pathway could involve peroxisomal multifunctional enzyme type 1 (Mfe-1) either with or without Amacr. To test this hypothesis, we generated a double knock-out mouse model lacking both Amacr and Mfe-1 activities and studied the bile acid profiles in wild-type, Mfe-1 and Amacr single knock-out and Mfe-1 and Amacr double knock-out mouse lines. The total bile acid pool was decreased in Mfe-1 -/- mice compared to wild-type and the levels of mature C24-bile acids were reduced in the double knock-out mice when compared to Amacr-deficient mice. These results indicate that peroxisomal Mfe-1 can contribute to the synthesis of mature bile acids in both an Amacr–dependent and an Amacr-independent manner. Journal Article Biochemical Journal 31 12 2014 2014-12-31 10.1042/BJ20130915 COLLEGE NANME Biomedical Sciences COLLEGE CODE BMS Swansea University 2019-09-24T16:07:45.8226127 2014-04-17T09:29:48.5488383 Faculty of Medicine, Health and Life Sciences Swansea University Medical School - Medicine 1 William Griffiths 0000-0002-4129-6616 2 Yuqin Wang 0000-0002-3063-3066 3 |
title |
Role of α-Methylacyl-CoA Racemase (Amacr) and peroxisomal Multifunctional Enzyme 1 (Mfe-1) in bile acid synthesis in mice |
spellingShingle |
Role of α-Methylacyl-CoA Racemase (Amacr) and peroxisomal Multifunctional Enzyme 1 (Mfe-1) in bile acid synthesis in mice William Griffiths Yuqin Wang |
title_short |
Role of α-Methylacyl-CoA Racemase (Amacr) and peroxisomal Multifunctional Enzyme 1 (Mfe-1) in bile acid synthesis in mice |
title_full |
Role of α-Methylacyl-CoA Racemase (Amacr) and peroxisomal Multifunctional Enzyme 1 (Mfe-1) in bile acid synthesis in mice |
title_fullStr |
Role of α-Methylacyl-CoA Racemase (Amacr) and peroxisomal Multifunctional Enzyme 1 (Mfe-1) in bile acid synthesis in mice |
title_full_unstemmed |
Role of α-Methylacyl-CoA Racemase (Amacr) and peroxisomal Multifunctional Enzyme 1 (Mfe-1) in bile acid synthesis in mice |
title_sort |
Role of α-Methylacyl-CoA Racemase (Amacr) and peroxisomal Multifunctional Enzyme 1 (Mfe-1) in bile acid synthesis in mice |
author_id_str_mv |
3316b1d1b524be1831790933eed1c26e c92729b58622f9fdf6a0e7d8f4ce5081 |
author_id_fullname_str_mv |
3316b1d1b524be1831790933eed1c26e_***_William Griffiths c92729b58622f9fdf6a0e7d8f4ce5081_***_Yuqin Wang |
author |
William Griffiths Yuqin Wang |
author2 |
William Griffiths Yuqin Wang |
format |
Journal article |
container_title |
Biochemical Journal |
publishDate |
2014 |
institution |
Swansea University |
doi_str_mv |
10.1042/BJ20130915 |
college_str |
Faculty of Medicine, Health and Life Sciences |
hierarchytype |
|
hierarchy_top_id |
facultyofmedicinehealthandlifesciences |
hierarchy_top_title |
Faculty of Medicine, Health and Life Sciences |
hierarchy_parent_id |
facultyofmedicinehealthandlifesciences |
hierarchy_parent_title |
Faculty of Medicine, Health and Life Sciences |
department_str |
Swansea University Medical School - Medicine{{{_:::_}}}Faculty of Medicine, Health and Life Sciences{{{_:::_}}}Swansea University Medical School - Medicine |
document_store_str |
0 |
active_str |
0 |
description |
Cholesterol is catabolized to bile acids by peroxisomal β-oxidation in which the side-chain of C27-bile acid intermediates is shortened by three carbon atoms to form mature C24-bile acids. Knock-out mouse models deficient in α-methylacyl coenzyme A racemase (Amacr) or multifunctional enzyme type 2 (Mfe-2), in which this β-oxidation pathway is prevented, display a residual mature C24-bile acid pool although greatly reduced, which implies the existence of alternative pathways of bile acid synthesis. One alternative pathway could involve peroxisomal multifunctional enzyme type 1 (Mfe-1) either with or without Amacr. To test this hypothesis, we generated a double knock-out mouse model lacking both Amacr and Mfe-1 activities and studied the bile acid profiles in wild-type, Mfe-1 and Amacr single knock-out and Mfe-1 and Amacr double knock-out mouse lines. The total bile acid pool was decreased in Mfe-1 -/- mice compared to wild-type and the levels of mature C24-bile acids were reduced in the double knock-out mice when compared to Amacr-deficient mice. These results indicate that peroxisomal Mfe-1 can contribute to the synthesis of mature bile acids in both an Amacr–dependent and an Amacr-independent manner. |
published_date |
2014-12-31T03:20:44Z |
_version_ |
1763750596803821568 |
score |
11.021648 |