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Phosphatidylcholine turnover in activated human neutrophils. Agonist-induced cytidylyltransferase translocation is subsequent to phospholipase D activation
Phosphatidylcholine synthesis and degradation are tightly regulated to assure a constant amount of the phospholipid in cellular membranes. The chemotactic peptide fMLP and the phorbol ester, phorbol 12-myristate 13-acetate, are known to stimulate phosphatidylcholine degradation by phospholipase D in...
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| Published in: | The Journal of biological chemistry 1995-06, Vol.270 (22), p.13138-13146 |
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| Main Authors: | , , , , , |
| Format: | Article |
| Language: | English |
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| container_end_page | 13146 |
| container_issue | 22 |
| container_start_page | 13138 |
| container_title | The Journal of biological chemistry |
| container_volume | 270 |
| creator | Tronchère, H Planat, V Record, M Tercé, F Ribbes, G Chap, H |
| description | Phosphatidylcholine synthesis and degradation are tightly regulated to assure a constant amount of the phospholipid in cellular membranes. The chemotactic peptide fMLP and the phorbol ester, phorbol 12-myristate 13-acetate, are known to stimulate phosphatidylcholine degradation by phospholipase D in human neutrophils. fMLP alone triggered phosphatidylcholine breakdown into phosphatidic acid, but did not stimulate phosphatidylcholine synthesis or activation of the rate-limiting enzyme CTP:phosphocholine cytidylyltransferase. Adding cytochalasin B to fMLP led to some conversion of phosphatidic acid into diglyceride, and fMLP was then able to trigger choline incorporation into phosphatidylcholine, and cytidylyltransferase translocation from cytosol to membranes. Inhibition of phosphatidyl-choline-phospholipase D activation with tyrphostin led to inhibition of choline incorporation. Therefore, phosphatidic acid-derived diglyceride but not phosphatidic acid alone was effective to promote cytidylyltransferase translocation. With phorbol 12-myristate 13-acetate as agonist, and by selective labeling of phosphatidylinositol and phosphatidylcholine, we demonstrated that only phosphatidylcholine-derived diglyceride participated in cytidylyltransferase translocation. Oleic acid stimulated phosphatidylcholine synthesis, but induced a weak increase in diglyceride and a slight cytidylyltransferase translocation, and did not stimulate phospholipase D activity. Our data established that only diglyceride derived from phosphatidylcholine degradation by the phospholipase D/phosphatidate phosphatase pathway are required for agonist-induced cytidylyltransferase translocation and subsequent choline incorporation into phosphatidylcholine. |
| doi_str_mv | 10.1074/jbc.270.22.13138 |
| format | article |
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Adding cytochalasin B to fMLP led to some conversion of phosphatidic acid into diglyceride, and fMLP was then able to trigger choline incorporation into phosphatidylcholine, and cytidylyltransferase translocation from cytosol to membranes. Inhibition of phosphatidyl-choline-phospholipase D activation with tyrphostin led to inhibition of choline incorporation. Therefore, phosphatidic acid-derived diglyceride but not phosphatidic acid alone was effective to promote cytidylyltransferase translocation. With phorbol 12-myristate 13-acetate as agonist, and by selective labeling of phosphatidylinositol and phosphatidylcholine, we demonstrated that only phosphatidylcholine-derived diglyceride participated in cytidylyltransferase translocation. Oleic acid stimulated phosphatidylcholine synthesis, but induced a weak increase in diglyceride and a slight cytidylyltransferase translocation, and did not stimulate phospholipase D activity. Our data established that only diglyceride derived from phosphatidylcholine degradation by the phospholipase D/phosphatidate phosphatase pathway are required for agonist-induced cytidylyltransferase translocation and subsequent choline incorporation into phosphatidylcholine.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.270.22.13138</identifier><identifier>PMID: 7768909</identifier><language>eng</language><publisher>United States</publisher><subject>Biological Transport ; Catalysis ; Choline - metabolism ; Choline-Phosphate Cytidylyltransferase ; Cytochalasin B - pharmacology ; Enzyme Activation ; Humans ; Kinetics ; N-Formylmethionine Leucyl-Phenylalanine - pharmacology ; Neutrophil Activation ; Neutrophils - cytology ; Neutrophils - metabolism ; Nucleotidyltransferases - agonists ; Nucleotidyltransferases - metabolism ; Oleic Acid ; Oleic Acids - pharmacology ; Phosphatidylcholines - biosynthesis ; Phosphatidylcholines - metabolism ; Phospholipase D - metabolism ; Tetradecanoylphorbol Acetate - pharmacology</subject><ispartof>The Journal of biological chemistry, 1995-06, Vol.270 (22), p.13138-13146</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7768909$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tronchère, H</creatorcontrib><creatorcontrib>Planat, V</creatorcontrib><creatorcontrib>Record, M</creatorcontrib><creatorcontrib>Tercé, F</creatorcontrib><creatorcontrib>Ribbes, G</creatorcontrib><creatorcontrib>Chap, H</creatorcontrib><title>Phosphatidylcholine turnover in activated human neutrophils. Agonist-induced cytidylyltransferase translocation is subsequent to phospholipase D activation</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Phosphatidylcholine synthesis and degradation are tightly regulated to assure a constant amount of the phospholipid in cellular membranes. The chemotactic peptide fMLP and the phorbol ester, phorbol 12-myristate 13-acetate, are known to stimulate phosphatidylcholine degradation by phospholipase D in human neutrophils. fMLP alone triggered phosphatidylcholine breakdown into phosphatidic acid, but did not stimulate phosphatidylcholine synthesis or activation of the rate-limiting enzyme CTP:phosphocholine cytidylyltransferase. Adding cytochalasin B to fMLP led to some conversion of phosphatidic acid into diglyceride, and fMLP was then able to trigger choline incorporation into phosphatidylcholine, and cytidylyltransferase translocation from cytosol to membranes. Inhibition of phosphatidyl-choline-phospholipase D activation with tyrphostin led to inhibition of choline incorporation. Therefore, phosphatidic acid-derived diglyceride but not phosphatidic acid alone was effective to promote cytidylyltransferase translocation. With phorbol 12-myristate 13-acetate as agonist, and by selective labeling of phosphatidylinositol and phosphatidylcholine, we demonstrated that only phosphatidylcholine-derived diglyceride participated in cytidylyltransferase translocation. Oleic acid stimulated phosphatidylcholine synthesis, but induced a weak increase in diglyceride and a slight cytidylyltransferase translocation, and did not stimulate phospholipase D activity. Our data established that only diglyceride derived from phosphatidylcholine degradation by the phospholipase D/phosphatidate phosphatase pathway are required for agonist-induced cytidylyltransferase translocation and subsequent choline incorporation into phosphatidylcholine.</description><subject>Biological Transport</subject><subject>Catalysis</subject><subject>Choline - metabolism</subject><subject>Choline-Phosphate Cytidylyltransferase</subject><subject>Cytochalasin B - pharmacology</subject><subject>Enzyme Activation</subject><subject>Humans</subject><subject>Kinetics</subject><subject>N-Formylmethionine Leucyl-Phenylalanine - pharmacology</subject><subject>Neutrophil Activation</subject><subject>Neutrophils - cytology</subject><subject>Neutrophils - metabolism</subject><subject>Nucleotidyltransferases - agonists</subject><subject>Nucleotidyltransferases - metabolism</subject><subject>Oleic Acid</subject><subject>Oleic Acids - pharmacology</subject><subject>Phosphatidylcholines - biosynthesis</subject><subject>Phosphatidylcholines - metabolism</subject><subject>Phospholipase D - metabolism</subject><subject>Tetradecanoylphorbol Acetate - pharmacology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><recordid>eNo1kD1PwzAURS0EKqWwsyB5YkvwR1LbY1U-pUowgMQWObZDXCV2iJ1K-S38WdJS3vLecHTu1QPgGqMUI5bdbUuVEoZSQlJMMeUnYI4RpwnN8ecpmCNEcCJIzs_BRQhbNE0m8AzMGFtygcQc_LzVPnS1jFaPjap9Y52Bceid35keWgelinYno9GwHlrpoDND7H1X2yakcPXlnQ0xsU4PakLUePCMTeylC5XpZZhs-7vxasrwDtoAw1AG8z0YF2H0sDsUmIK7PXz_Hzixl-Cskk0wV8e9AB-PD-_r52Tz-vSyXm2SjlAWE5oRxHJSVZhjxjjBGuulrGQmFSIUCURVLpnOqiqXApdSUyaoKTVXnPEyN3QBbv-8Xe-nWiEWrQ3KNI10xg-hwEshKMnoBN4cwaFsjS663rayH4vjN-kvjl19Zg</recordid><startdate>19950602</startdate><enddate>19950602</enddate><creator>Tronchère, H</creator><creator>Planat, V</creator><creator>Record, M</creator><creator>Tercé, F</creator><creator>Ribbes, G</creator><creator>Chap, H</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7T5</scope><scope>H94</scope></search><sort><creationdate>19950602</creationdate><title>Phosphatidylcholine turnover in activated human neutrophils. Agonist-induced cytidylyltransferase translocation is subsequent to phospholipase D activation</title><author>Tronchère, H ; Planat, V ; Record, M ; Tercé, F ; Ribbes, G ; Chap, H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p237t-3420752ff18177821d1d6afa4ac0230903c5a7d4ff5a91bad3793ebd8c878b5e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Biological Transport</topic><topic>Catalysis</topic><topic>Choline - metabolism</topic><topic>Choline-Phosphate Cytidylyltransferase</topic><topic>Cytochalasin B - pharmacology</topic><topic>Enzyme Activation</topic><topic>Humans</topic><topic>Kinetics</topic><topic>N-Formylmethionine Leucyl-Phenylalanine - pharmacology</topic><topic>Neutrophil Activation</topic><topic>Neutrophils - cytology</topic><topic>Neutrophils - metabolism</topic><topic>Nucleotidyltransferases - agonists</topic><topic>Nucleotidyltransferases - metabolism</topic><topic>Oleic Acid</topic><topic>Oleic Acids - pharmacology</topic><topic>Phosphatidylcholines - biosynthesis</topic><topic>Phosphatidylcholines - metabolism</topic><topic>Phospholipase D - metabolism</topic><topic>Tetradecanoylphorbol Acetate - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tronchère, H</creatorcontrib><creatorcontrib>Planat, V</creatorcontrib><creatorcontrib>Record, M</creatorcontrib><creatorcontrib>Tercé, F</creatorcontrib><creatorcontrib>Ribbes, G</creatorcontrib><creatorcontrib>Chap, H</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tronchère, H</au><au>Planat, V</au><au>Record, M</au><au>Tercé, F</au><au>Ribbes, G</au><au>Chap, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphatidylcholine turnover in activated human neutrophils. Agonist-induced cytidylyltransferase translocation is subsequent to phospholipase D activation</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1995-06-02</date><risdate>1995</risdate><volume>270</volume><issue>22</issue><spage>13138</spage><epage>13146</epage><pages>13138-13146</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><notes>ObjectType-Article-2</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-1</notes><notes>content type line 23</notes><abstract>Phosphatidylcholine synthesis and degradation are tightly regulated to assure a constant amount of the phospholipid in cellular membranes. The chemotactic peptide fMLP and the phorbol ester, phorbol 12-myristate 13-acetate, are known to stimulate phosphatidylcholine degradation by phospholipase D in human neutrophils. fMLP alone triggered phosphatidylcholine breakdown into phosphatidic acid, but did not stimulate phosphatidylcholine synthesis or activation of the rate-limiting enzyme CTP:phosphocholine cytidylyltransferase. Adding cytochalasin B to fMLP led to some conversion of phosphatidic acid into diglyceride, and fMLP was then able to trigger choline incorporation into phosphatidylcholine, and cytidylyltransferase translocation from cytosol to membranes. Inhibition of phosphatidyl-choline-phospholipase D activation with tyrphostin led to inhibition of choline incorporation. Therefore, phosphatidic acid-derived diglyceride but not phosphatidic acid alone was effective to promote cytidylyltransferase translocation. With phorbol 12-myristate 13-acetate as agonist, and by selective labeling of phosphatidylinositol and phosphatidylcholine, we demonstrated that only phosphatidylcholine-derived diglyceride participated in cytidylyltransferase translocation. Oleic acid stimulated phosphatidylcholine synthesis, but induced a weak increase in diglyceride and a slight cytidylyltransferase translocation, and did not stimulate phospholipase D activity. Our data established that only diglyceride derived from phosphatidylcholine degradation by the phospholipase D/phosphatidate phosphatase pathway are required for agonist-induced cytidylyltransferase translocation and subsequent choline incorporation into phosphatidylcholine.</abstract><cop>United States</cop><pmid>7768909</pmid><doi>10.1074/jbc.270.22.13138</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1995-06, Vol.270 (22), p.13138-13146 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_16993243 |
| source | BACON - Elsevier - GLOBAL_SCIENCEDIRECT-OPENACCESS |
| subjects | Biological Transport Catalysis Choline - metabolism Choline-Phosphate Cytidylyltransferase Cytochalasin B - pharmacology Enzyme Activation Humans Kinetics N-Formylmethionine Leucyl-Phenylalanine - pharmacology Neutrophil Activation Neutrophils - cytology Neutrophils - metabolism Nucleotidyltransferases - agonists Nucleotidyltransferases - metabolism Oleic Acid Oleic Acids - pharmacology Phosphatidylcholines - biosynthesis Phosphatidylcholines - metabolism Phospholipase D - metabolism Tetradecanoylphorbol Acetate - pharmacology |
| title | Phosphatidylcholine turnover in activated human neutrophils. Agonist-induced cytidylyltransferase translocation is subsequent to phospholipase D activation |
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