Substrate Preferences of a Lysophosphatidylcholine Acyltransferase Highlight Its Role in Phospholipid Remodeling
An important enzyme involved in phospholipid turnover is the acyl-CoA: lysophosphatidylcholine acyltransferase (LPCAT). Here, we report characterization of a newly discovered human LPCAT (LPCAT3), which has distinct substrate preferences strikingly consistent with a role in phosphatidylcholine (PtdC...
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| Veröffentlicht in: | Lipids 2008-10, Vol.43 (10), p.895-902 |
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| creator | Kazachkov, Michael Chen, Qilin Wang, Liping Zou, Jitao |
| description | An important enzyme involved in phospholipid turnover is the acyl-CoA: lysophosphatidylcholine acyltransferase (LPCAT). Here, we report characterization of a newly discovered human LPCAT (LPCAT3), which has distinct substrate preferences strikingly consistent with a role in phosphatidylcholine (PtdCho) remodeling and modulating fatty acid composition of PtdCho. LPCAT3 prefers lysophosphatidylcholine (lysoPtdCho) with saturated fatty acid at the sn-1 position and exhibits acyl donor preference towards linoleoyl-CoA and arachidonoyl-CoA. Furthermore, LPCAT3 is active in mediating 1-O-alkyl-sn-glycero-3-phosphocholine acylation with long chain fatty acyl-CoAs to generate 1-O-alkyl-phosphatidylcholine, another very important constitute of mammalian membrane systems. These properties are precisely the known attributes of LPCAT previously ascribed to the isoform involved in Lands' cycle, and thus strongly suggest that LPCAT3 is involved in phospholipids remodeling to achieve appropriate membrane lipid fatty acid composition. |
| doi_str_mv | 10.1007/s11745-008-3233-y |
| format | Article |
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Here, we report characterization of a newly discovered human LPCAT (LPCAT3), which has distinct substrate preferences strikingly consistent with a role in phosphatidylcholine (PtdCho) remodeling and modulating fatty acid composition of PtdCho. LPCAT3 prefers lysophosphatidylcholine (lysoPtdCho) with saturated fatty acid at the sn-1 position and exhibits acyl donor preference towards linoleoyl-CoA and arachidonoyl-CoA. Furthermore, LPCAT3 is active in mediating 1-O-alkyl-sn-glycero-3-phosphocholine acylation with long chain fatty acyl-CoAs to generate 1-O-alkyl-phosphatidylcholine, another very important constitute of mammalian membrane systems. These properties are precisely the known attributes of LPCAT previously ascribed to the isoform involved in Lands' cycle, and thus strongly suggest that LPCAT3 is involved in phospholipids remodeling to achieve appropriate membrane lipid fatty acid composition.</description><identifier>ISSN: 0024-4201</identifier><identifier>EISSN: 1558-9307</identifier><identifier>DOI: 10.1007/s11745-008-3233-y</identifier><identifier>PMID: 18781350</identifier><language>eng</language><publisher>Berlin/Heidelberg: Berlin/Heidelberg : Springer-Verlag</publisher><subject>1-Acylglycerophosphocholine O-Acyltransferase - genetics ; 1-Acylglycerophosphocholine O-Acyltransferase - metabolism ; Acyl Coenzyme A - metabolism ; Animals ; Arachidonic acid ; Biomedical and Life Sciences ; Fatty acids ; Fatty Acids - metabolism ; Gene Expression Profiling ; Humans ; Life Sciences ; Lipidology ; LPCAT ; Medical Biochemistry ; Medicinal Chemistry ; Mice ; Microbial Genetics and Genomics ; Neurochemistry ; Nutrition ; Original Article ; Phosphatidylcholines - metabolism ; Phospholipid ; Phospholipids - metabolism ; Phylogeny ; PtdCho turnover ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - genetics ; Substrate Specificity</subject><ispartof>Lipids, 2008-10, Vol.43 (10), p.895-902</ispartof><rights>AOCS 2008</rights><rights>2008 American Oil Chemists' Society (AOCS)</rights><rights>Copyright AOCS Press Oct 2008</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5505-54858f18acafb1f6de8c7fd2e6b00f67d026a0be2995583ec1e8ee22e1aceff63</citedby><cites>FETCH-LOGICAL-c5505-54858f18acafb1f6de8c7fd2e6b00f67d026a0be2995583ec1e8ee22e1aceff63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11745-008-3233-y$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11745-008-3233-y$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,1411,27903,27904,41467,42536,45553,45554,51297</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18781350$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kazachkov, Michael</creatorcontrib><creatorcontrib>Chen, Qilin</creatorcontrib><creatorcontrib>Wang, Liping</creatorcontrib><creatorcontrib>Zou, Jitao</creatorcontrib><title>Substrate Preferences of a Lysophosphatidylcholine Acyltransferase Highlight Its Role in Phospholipid Remodeling</title><title>Lipids</title><addtitle>Lipids</addtitle><addtitle>Lipids</addtitle><description>An important enzyme involved in phospholipid turnover is the acyl-CoA: lysophosphatidylcholine acyltransferase (LPCAT). Here, we report characterization of a newly discovered human LPCAT (LPCAT3), which has distinct substrate preferences strikingly consistent with a role in phosphatidylcholine (PtdCho) remodeling and modulating fatty acid composition of PtdCho. LPCAT3 prefers lysophosphatidylcholine (lysoPtdCho) with saturated fatty acid at the sn-1 position and exhibits acyl donor preference towards linoleoyl-CoA and arachidonoyl-CoA. Furthermore, LPCAT3 is active in mediating 1-O-alkyl-sn-glycero-3-phosphocholine acylation with long chain fatty acyl-CoAs to generate 1-O-alkyl-phosphatidylcholine, another very important constitute of mammalian membrane systems. These properties are precisely the known attributes of LPCAT previously ascribed to the isoform involved in Lands' cycle, and thus strongly suggest that LPCAT3 is involved in phospholipids remodeling to achieve appropriate membrane lipid fatty acid composition.</description><subject>1-Acylglycerophosphocholine O-Acyltransferase - genetics</subject><subject>1-Acylglycerophosphocholine O-Acyltransferase - metabolism</subject><subject>Acyl Coenzyme A - metabolism</subject><subject>Animals</subject><subject>Arachidonic acid</subject><subject>Biomedical and Life Sciences</subject><subject>Fatty acids</subject><subject>Fatty Acids - metabolism</subject><subject>Gene Expression Profiling</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Lipidology</subject><subject>LPCAT</subject><subject>Medical Biochemistry</subject><subject>Medicinal Chemistry</subject><subject>Mice</subject><subject>Microbial Genetics and Genomics</subject><subject>Neurochemistry</subject><subject>Nutrition</subject><subject>Original Article</subject><subject>Phosphatidylcholines - metabolism</subject><subject>Phospholipid</subject><subject>Phospholipids - metabolism</subject><subject>Phylogeny</subject><subject>PtdCho turnover</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Substrate Specificity</subject><issn>0024-4201</issn><issn>1558-9307</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqFksFq3DAQhkVpabZJH6CXVvSQm5ORZNnyMaRNs7DQJWnOQpZHuw5ey5Vsgt--Sr0Q6KE5CCH4vmFmfhHyicEFAygvI2NlLjMAlQkuRDa_ISsmpcoqAeVbsgLgeZZzYCfkQ4yP6cnySr4nJ0yVigkJKzLcT3UcgxmRbgM6DNhbjNQ7auhmjn7Y-zjszdg2c2f3vmt7pFd27pLSx4SbiPS23e27dEa6HiO98x3Stqfbv2Yyhrahd3jwDSZ7d0beOdNF_Hi8T8nDzfdf17fZ5ueP9fXVJrNSgsxkrqRyTBlrXM1c0aCypWs4FjWAK8oGeGGgRl5VaWCBlqFC5ByZsehcIU7J-VJ3CP73hHHUhzZa7DrTo5-iLipZ5AIggV__AR_9FPrUm-ZlXkjBOU8QWyAbfIxpUXoI7cGEWTPQz1noJQudstDPWeg5OZ-Phaf6gM2LcVx-AsoFeGo7nF-vqDfr7TdQlUwmX8yYpH6H4aXn__XzZZGc8drsQhv1w336HAKYzEEm6A8nAbEb</recordid><startdate>200810</startdate><enddate>200810</enddate><creator>Kazachkov, Michael</creator><creator>Chen, Qilin</creator><creator>Wang, Liping</creator><creator>Zou, Jitao</creator><general>Berlin/Heidelberg : Springer-Verlag</general><general>Springer-Verlag</general><general>Springer‐Verlag</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7T7</scope><scope>7TK</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>7X8</scope></search><sort><creationdate>200810</creationdate><title>Substrate Preferences of a Lysophosphatidylcholine Acyltransferase Highlight Its Role in Phospholipid Remodeling</title><author>Kazachkov, Michael ; Chen, Qilin ; Wang, Liping ; Zou, Jitao</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5505-54858f18acafb1f6de8c7fd2e6b00f67d026a0be2995583ec1e8ee22e1aceff63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>1-Acylglycerophosphocholine O-Acyltransferase - genetics</topic><topic>1-Acylglycerophosphocholine O-Acyltransferase - metabolism</topic><topic>Acyl Coenzyme A - metabolism</topic><topic>Animals</topic><topic>Arachidonic acid</topic><topic>Biomedical and Life Sciences</topic><topic>Fatty acids</topic><topic>Fatty Acids - metabolism</topic><topic>Gene Expression Profiling</topic><topic>Humans</topic><topic>Life Sciences</topic><topic>Lipidology</topic><topic>LPCAT</topic><topic>Medical Biochemistry</topic><topic>Medicinal Chemistry</topic><topic>Mice</topic><topic>Microbial Genetics and Genomics</topic><topic>Neurochemistry</topic><topic>Nutrition</topic><topic>Original Article</topic><topic>Phosphatidylcholines - metabolism</topic><topic>Phospholipid</topic><topic>Phospholipids - metabolism</topic><topic>Phylogeny</topic><topic>PtdCho turnover</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kazachkov, Michael</creatorcontrib><creatorcontrib>Chen, Qilin</creatorcontrib><creatorcontrib>Wang, Liping</creatorcontrib><creatorcontrib>Zou, Jitao</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection (ProQuest)</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>MEDLINE - Academic</collection><jtitle>Lipids</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kazachkov, Michael</au><au>Chen, Qilin</au><au>Wang, Liping</au><au>Zou, Jitao</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Substrate Preferences of a Lysophosphatidylcholine Acyltransferase Highlight Its Role in Phospholipid Remodeling</atitle><jtitle>Lipids</jtitle><stitle>Lipids</stitle><addtitle>Lipids</addtitle><date>2008-10</date><risdate>2008</risdate><volume>43</volume><issue>10</issue><spage>895</spage><epage>902</epage><pages>895-902</pages><issn>0024-4201</issn><eissn>1558-9307</eissn><abstract>An important enzyme involved in phospholipid turnover is the acyl-CoA: lysophosphatidylcholine acyltransferase (LPCAT). Here, we report characterization of a newly discovered human LPCAT (LPCAT3), which has distinct substrate preferences strikingly consistent with a role in phosphatidylcholine (PtdCho) remodeling and modulating fatty acid composition of PtdCho. LPCAT3 prefers lysophosphatidylcholine (lysoPtdCho) with saturated fatty acid at the sn-1 position and exhibits acyl donor preference towards linoleoyl-CoA and arachidonoyl-CoA. Furthermore, LPCAT3 is active in mediating 1-O-alkyl-sn-glycero-3-phosphocholine acylation with long chain fatty acyl-CoAs to generate 1-O-alkyl-phosphatidylcholine, another very important constitute of mammalian membrane systems. These properties are precisely the known attributes of LPCAT previously ascribed to the isoform involved in Lands' cycle, and thus strongly suggest that LPCAT3 is involved in phospholipids remodeling to achieve appropriate membrane lipid fatty acid composition.</abstract><cop>Berlin/Heidelberg</cop><pub>Berlin/Heidelberg : Springer-Verlag</pub><pmid>18781350</pmid><doi>10.1007/s11745-008-3233-y</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Lipids, 2008-10, Vol.43 (10), p.895-902 |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Springer Nature - Complete Springer Journals |
| subjects | 1-Acylglycerophosphocholine O-Acyltransferase - genetics 1-Acylglycerophosphocholine O-Acyltransferase - metabolism Acyl Coenzyme A - metabolism Animals Arachidonic acid Biomedical and Life Sciences Fatty acids Fatty Acids - metabolism Gene Expression Profiling Humans Life Sciences Lipidology LPCAT Medical Biochemistry Medicinal Chemistry Mice Microbial Genetics and Genomics Neurochemistry Nutrition Original Article Phosphatidylcholines - metabolism Phospholipid Phospholipids - metabolism Phylogeny PtdCho turnover Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Substrate Specificity |
| title | Substrate Preferences of a Lysophosphatidylcholine Acyltransferase Highlight Its Role in Phospholipid Remodeling |
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