Mutants in a macrophage-like cell line are defective in plasmalogen biosynthesis, but contain functional peroxisomes
We have used a fluorescence-activated cytotoxicity protocol, 9-(1'-pyrene)nonanol (P9OH)/UV selection (Morand, O. H., Allen, L.-A. H., Zoeller, R. A., and Raetz, C. R. H. (1990) Biochim. Biophys. Acta 1034, 132-141), to isolate a series of plasmalogen-deficient mutants in a murine, macrophage-l...
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| Veröffentlicht in: | The Journal of biological chemistry 1992-04, Vol.267 (12), p.8299-8306 |
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| creator | Zoeller, R A Rangaswamy, S Herscovitz, H Rizzo, W B Hajra, A K Das, A K Moser, H W Moser, A Lazarow, P B Santos, M J |
| description | We have used a fluorescence-activated cytotoxicity protocol, 9-(1'-pyrene)nonanol (P9OH)/UV selection (Morand, O. H., Allen,
L.-A. H., Zoeller, R. A., and Raetz, C. R. H. (1990) Biochim. Biophys. Acta 1034, 132-141), to isolate a series of plasmalogen-deficient
mutants in a murine, macrophage-like cell line, RAW 264.7. Three of these mutants, RAW.7, RAW.12, and RAW.108, displayed varying
degrees of plasmalogen deficiency (48, 17, and 14% of wild-type levels, respectively), and all three mutants were deficient
in peroxisomal dihydroxyacetone phosphate (DHAP) acyltransferase activity (5% of wild-type). Unlike previously described Chinese
hamster ovary (CHO) cell mutants, the RAW mutants contained intact, functional, peroxisomes and normal levels of alkyl-DHAP
synthase activity, a peroxisomal, membrane-bound enzyme. In RAW.7 and RAW.108 cells, the loss of peroxisomal DHAP acyltransferase
is the primary lesion. RAW.12 displayed not only a deficiency in the DHAP acyltransferase activity, but also displayed a second
lesion in the biosynthetic pathway, a deficiency in delta 1'-desaturase activity (plasmanylethanolamine desaturase, EC 1.14.99.19),
the final step in plasmenylethanolamine biosynthesis. The deficiencies expressed in the mutants represent unique lesions in
plasmalogen biosynthesis. Since the RAW cell line is a macrophage-like responsive cell line, these mutants can be used to
examine the role of plasmalogens in cellular functions such as arachidonic acid metabolism, prostaglandin synthesis, protein
secretion, and signal transduction. |
| doi_str_mv | 10.1016/S0021-9258(18)42442-8 |
| format | Article |
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L.-A. H., Zoeller, R. A., and Raetz, C. R. H. (1990) Biochim. Biophys. Acta 1034, 132-141), to isolate a series of plasmalogen-deficient
mutants in a murine, macrophage-like cell line, RAW 264.7. Three of these mutants, RAW.7, RAW.12, and RAW.108, displayed varying
degrees of plasmalogen deficiency (48, 17, and 14% of wild-type levels, respectively), and all three mutants were deficient
in peroxisomal dihydroxyacetone phosphate (DHAP) acyltransferase activity (5% of wild-type). Unlike previously described Chinese
hamster ovary (CHO) cell mutants, the RAW mutants contained intact, functional, peroxisomes and normal levels of alkyl-DHAP
synthase activity, a peroxisomal, membrane-bound enzyme. In RAW.7 and RAW.108 cells, the loss of peroxisomal DHAP acyltransferase
is the primary lesion. RAW.12 displayed not only a deficiency in the DHAP acyltransferase activity, but also displayed a second
lesion in the biosynthetic pathway, a deficiency in delta 1'-desaturase activity (plasmanylethanolamine desaturase, EC 1.14.99.19),
the final step in plasmenylethanolamine biosynthesis. The deficiencies expressed in the mutants represent unique lesions in
plasmalogen biosynthesis. Since the RAW cell line is a macrophage-like responsive cell line, these mutants can be used to
examine the role of plasmalogens in cellular functions such as arachidonic acid metabolism, prostaglandin synthesis, protein
secretion, and signal transduction.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)42442-8</identifier><identifier>PMID: 1569085</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Acyltransferases - metabolism ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Catalase - metabolism ; Cell Line ; CHO Cells ; Cricetinae ; Fatty Alcohols - chemistry ; Fundamental and applied biological sciences. Psychology ; Glycerolipids, phospholipids ; Lipids ; Macrophages - metabolism ; Mice ; Microbodies - enzymology ; Microbodies - metabolism ; Microscopy, Fluorescence ; Mutation ; Other biological molecules ; Plasmalogens - biosynthesis ; Pyrenes - chemistry</subject><ispartof>The Journal of biological chemistry, 1992-04, Vol.267 (12), p.8299-8306</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c439t-de989a5aeabc7cc98020b1c0d0a73c757be705f27102676f1223bdf2e1379973</citedby><cites>FETCH-LOGICAL-c439t-de989a5aeabc7cc98020b1c0d0a73c757be705f27102676f1223bdf2e1379973</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5290224$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1569085$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zoeller, R A</creatorcontrib><creatorcontrib>Rangaswamy, S</creatorcontrib><creatorcontrib>Herscovitz, H</creatorcontrib><creatorcontrib>Rizzo, W B</creatorcontrib><creatorcontrib>Hajra, A K</creatorcontrib><creatorcontrib>Das, A K</creatorcontrib><creatorcontrib>Moser, H W</creatorcontrib><creatorcontrib>Moser, A</creatorcontrib><creatorcontrib>Lazarow, P B</creatorcontrib><creatorcontrib>Santos, M J</creatorcontrib><title>Mutants in a macrophage-like cell line are defective in plasmalogen biosynthesis, but contain functional peroxisomes</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>We have used a fluorescence-activated cytotoxicity protocol, 9-(1'-pyrene)nonanol (P9OH)/UV selection (Morand, O. H., Allen,
L.-A. H., Zoeller, R. A., and Raetz, C. R. H. (1990) Biochim. Biophys. Acta 1034, 132-141), to isolate a series of plasmalogen-deficient
mutants in a murine, macrophage-like cell line, RAW 264.7. Three of these mutants, RAW.7, RAW.12, and RAW.108, displayed varying
degrees of plasmalogen deficiency (48, 17, and 14% of wild-type levels, respectively), and all three mutants were deficient
in peroxisomal dihydroxyacetone phosphate (DHAP) acyltransferase activity (5% of wild-type). Unlike previously described Chinese
hamster ovary (CHO) cell mutants, the RAW mutants contained intact, functional, peroxisomes and normal levels of alkyl-DHAP
synthase activity, a peroxisomal, membrane-bound enzyme. In RAW.7 and RAW.108 cells, the loss of peroxisomal DHAP acyltransferase
is the primary lesion. RAW.12 displayed not only a deficiency in the DHAP acyltransferase activity, but also displayed a second
lesion in the biosynthetic pathway, a deficiency in delta 1'-desaturase activity (plasmanylethanolamine desaturase, EC 1.14.99.19),
the final step in plasmenylethanolamine biosynthesis. The deficiencies expressed in the mutants represent unique lesions in
plasmalogen biosynthesis. Since the RAW cell line is a macrophage-like responsive cell line, these mutants can be used to
examine the role of plasmalogens in cellular functions such as arachidonic acid metabolism, prostaglandin synthesis, protein
secretion, and signal transduction.</description><subject>Acyltransferases - metabolism</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Catalase - metabolism</subject><subject>Cell Line</subject><subject>CHO Cells</subject><subject>Cricetinae</subject><subject>Fatty Alcohols - chemistry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycerolipids, phospholipids</subject><subject>Lipids</subject><subject>Macrophages - metabolism</subject><subject>Mice</subject><subject>Microbodies - enzymology</subject><subject>Microbodies - metabolism</subject><subject>Microscopy, Fluorescence</subject><subject>Mutation</subject><subject>Other biological molecules</subject><subject>Plasmalogens - biosynthesis</subject><subject>Pyrenes - chemistry</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u1TAQhS1EVS6FR6hkCYRAasB24theoqr8SEUs6IKdNXEmN4bECXZC6dvj9F6VJbPxYr4z4zmHkHPO3nLG63ffGBO8MELq11y_qURViUI_IjvOdFmUkn9_THYPyBPyNKUfLFdl-Ck55bI2TMsdWb6sC4QlUR8o0BFcnOYe9lgM_idSh8NABx-QQkTaYodu8b9xg-cB0gjDtMdAGz-lu7D0mHy6oM26UDeFBTLVrSErpgADnTFOf3yaRkzPyEkHQ8Lnx_eM3Hy4urn8VFx__fj58v114arSLEWLRhuQgNA45ZzRTLCGO9YyUKVTUjWomOyE4kzUqu64EGXTdgJ5qYxR5Rl5dRg7x-nXimmxo0_bSRBwWpNVwmSh_D_IaymqWrMMygOYbUopYmfn6EeId5Yzu6Vi71Oxm-WWa3ufitVZd35csDYjtv9Uhxhy_-WxD8nB0EUIzqcHTG4fFVXGXhyw3u_7Wx_RZuddj6PN91ueNwljyr-o86H5</recordid><startdate>19920425</startdate><enddate>19920425</enddate><creator>Zoeller, R A</creator><creator>Rangaswamy, S</creator><creator>Herscovitz, H</creator><creator>Rizzo, W B</creator><creator>Hajra, A K</creator><creator>Das, A K</creator><creator>Moser, H W</creator><creator>Moser, A</creator><creator>Lazarow, P B</creator><creator>Santos, M J</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>IQODW</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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19920425</creationdate><title>Mutants in a macrophage-like cell line are defective in plasmalogen biosynthesis, but contain functional peroxisomes</title><author>Zoeller, R A ; Rangaswamy, S ; Herscovitz, H ; Rizzo, W B ; Hajra, A K ; Das, A K ; Moser, H W ; Moser, A ; Lazarow, P B ; Santos, M J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c439t-de989a5aeabc7cc98020b1c0d0a73c757be705f27102676f1223bdf2e1379973</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Acyltransferases - metabolism</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Catalase - metabolism</topic><topic>Cell Line</topic><topic>CHO Cells</topic><topic>Cricetinae</topic><topic>Fatty Alcohols - chemistry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycerolipids, phospholipids</topic><topic>Lipids</topic><topic>Macrophages - metabolism</topic><topic>Mice</topic><topic>Microbodies - enzymology</topic><topic>Microbodies - metabolism</topic><topic>Microscopy, Fluorescence</topic><topic>Mutation</topic><topic>Other biological molecules</topic><topic>Plasmalogens - biosynthesis</topic><topic>Pyrenes - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zoeller, R A</creatorcontrib><creatorcontrib>Rangaswamy, S</creatorcontrib><creatorcontrib>Herscovitz, H</creatorcontrib><creatorcontrib>Rizzo, W B</creatorcontrib><creatorcontrib>Hajra, A K</creatorcontrib><creatorcontrib>Das, A K</creatorcontrib><creatorcontrib>Moser, H W</creatorcontrib><creatorcontrib>Moser, A</creatorcontrib><creatorcontrib>Lazarow, P B</creatorcontrib><creatorcontrib>Santos, M J</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zoeller, R A</au><au>Rangaswamy, S</au><au>Herscovitz, H</au><au>Rizzo, W B</au><au>Hajra, A K</au><au>Das, A K</au><au>Moser, H W</au><au>Moser, A</au><au>Lazarow, P B</au><au>Santos, M J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mutants in a macrophage-like cell line are defective in plasmalogen biosynthesis, but contain functional peroxisomes</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1992-04-25</date><risdate>1992</risdate><volume>267</volume><issue>12</issue><spage>8299</spage><epage>8306</epage><pages>8299-8306</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>We have used a fluorescence-activated cytotoxicity protocol, 9-(1'-pyrene)nonanol (P9OH)/UV selection (Morand, O. H., Allen,
L.-A. H., Zoeller, R. A., and Raetz, C. R. H. (1990) Biochim. Biophys. Acta 1034, 132-141), to isolate a series of plasmalogen-deficient
mutants in a murine, macrophage-like cell line, RAW 264.7. Three of these mutants, RAW.7, RAW.12, and RAW.108, displayed varying
degrees of plasmalogen deficiency (48, 17, and 14% of wild-type levels, respectively), and all three mutants were deficient
in peroxisomal dihydroxyacetone phosphate (DHAP) acyltransferase activity (5% of wild-type). Unlike previously described Chinese
hamster ovary (CHO) cell mutants, the RAW mutants contained intact, functional, peroxisomes and normal levels of alkyl-DHAP
synthase activity, a peroxisomal, membrane-bound enzyme. In RAW.7 and RAW.108 cells, the loss of peroxisomal DHAP acyltransferase
is the primary lesion. RAW.12 displayed not only a deficiency in the DHAP acyltransferase activity, but also displayed a second
lesion in the biosynthetic pathway, a deficiency in delta 1'-desaturase activity (plasmanylethanolamine desaturase, EC 1.14.99.19),
the final step in plasmenylethanolamine biosynthesis. The deficiencies expressed in the mutants represent unique lesions in
plasmalogen biosynthesis. Since the RAW cell line is a macrophage-like responsive cell line, these mutants can be used to
examine the role of plasmalogens in cellular functions such as arachidonic acid metabolism, prostaglandin synthesis, protein
secretion, and signal transduction.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1569085</pmid><doi>10.1016/S0021-9258(18)42442-8</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1992-04, Vol.267 (12), p.8299-8306 |
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| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Acyltransferases - metabolism Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Catalase - metabolism Cell Line CHO Cells Cricetinae Fatty Alcohols - chemistry Fundamental and applied biological sciences. Psychology Glycerolipids, phospholipids Lipids Macrophages - metabolism Mice Microbodies - enzymology Microbodies - metabolism Microscopy, Fluorescence Mutation Other biological molecules Plasmalogens - biosynthesis Pyrenes - chemistry |
| title | Mutants in a macrophage-like cell line are defective in plasmalogen biosynthesis, but contain functional peroxisomes |
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