No Cover Image

Journal article 1096 views

Role of α-Methylacyl-CoA Racemase (Amacr) and peroxisomal Multifunctional Enzyme 1 (Mfe-1) in bile acid synthesis in mice

, William Griffiths Orcid Logo, Yuqin Wang Orcid Logo

Biochemical Journal

Swansea University Authors: William Griffiths Orcid Logo, Yuqin Wang Orcid Logo

Full text not available from this repository: check for access using links below.

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 (...

Full description

Published in: Biochemical Journal
Published: 2014
URI: https://cronfa.swan.ac.uk/Record/cronfa17830
Tags: Add Tag
No Tags, Be the first to tag this record!
first_indexed 2014-04-18T01:30:01Z
last_indexed 2019-09-24T19:18:08Z
id cronfa17830
recordtype SURis
fullrecord <?xml version="1.0"?><rfc1807><datestamp>2019-09-24T16:07:45.8226127</datestamp><bib-version>v2</bib-version><id>17830</id><entry>2014-04-17</entry><title>Role of &#x3B1;-Methylacyl-CoA Racemase (Amacr) and peroxisomal Multifunctional Enzyme 1 (Mfe-1) in bile acid synthesis in mice</title><swanseaauthors><author><sid>3316b1d1b524be1831790933eed1c26e</sid><ORCID>0000-0002-4129-6616</ORCID><firstname>William</firstname><surname>Griffiths</surname><name>William Griffiths</name><active>true</active><ethesisStudent>false</ethesisStudent></author><author><sid>c92729b58622f9fdf6a0e7d8f4ce5081</sid><ORCID>0000-0002-3063-3066</ORCID><firstname>Yuqin</firstname><surname>Wang</surname><name>Yuqin Wang</name><active>true</active><ethesisStudent>false</ethesisStudent></author></swanseaauthors><date>2014-04-17</date><deptcode>BMS</deptcode><abstract>Cholesterol is catabolized to bile acids by peroxisomal &#x3B2;-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 &#x3B1;-methylacyl coenzyme A racemase (Amacr) or multifunctional enzyme type 2 (Mfe-2), in which this &#x3B2;-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&#x2013;dependent and an Amacr-independent manner.</abstract><type>Journal Article</type><journal>Biochemical Journal</journal><publisher/><keywords/><publishedDay>31</publishedDay><publishedMonth>12</publishedMonth><publishedYear>2014</publishedYear><publishedDate>2014-12-31</publishedDate><doi>10.1042/BJ20130915</doi><url/><notes></notes><college>COLLEGE NANME</college><department>Biomedical Sciences</department><CollegeCode>COLLEGE CODE</CollegeCode><DepartmentCode>BMS</DepartmentCode><institution>Swansea University</institution><apcterm/><lastEdited>2019-09-24T16:07:45.8226127</lastEdited><Created>2014-04-17T09:29:48.5488383</Created><path><level id="1">Faculty of Medicine, Health and Life Sciences</level><level id="2">Swansea University Medical School - Medicine</level></path><authors><author><order>1</order></author><author><firstname>William</firstname><surname>Griffiths</surname><orcid>0000-0002-4129-6616</orcid><order>2</order></author><author><firstname>Yuqin</firstname><surname>Wang</surname><orcid>0000-0002-3063-3066</orcid><order>3</order></author></authors><documents/><OutputDurs/></rfc1807>
spelling 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 11.013619

Similar Items