Phosphatidylcholine-Specific Phospholipase D Activity Is Elevated in v-Fps-Transformed Cells
Activating the protein-tyrosine kinase of v-Fps results in a rapid increase in diglyceride (DG) in rat fibroblasts. The v-Fps-induced increases in DG were detected only when phospholipids were prelabeled with [3H]-myristate, which is incorporated primarily into phosphatidylcholine (PC). Inhibition o...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1994-09, Vol.203 (2), p.1195-1203 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Jiang, Y.W. Song, J.G. Zang, Q. Foster, D.A. |
| description | Activating the protein-tyrosine kinase of v-Fps results in a rapid increase in diglyceride (DG) in rat fibroblasts. The v-Fps-induced increases in DG were detected only when phospholipids were prelabeled with [3H]-myristate, which is incorporated primarily into phosphatidylcholine (PC). Inhibition of phosphatidic acid (PA) phosphatase (PAP), which converts PA to DG, blocked v-Fps-induced DG production. PA is a primary metabolite of type D phospholipases (PLD). Consistent with these observations, PLD activity was activated in response to the kinase activity of v-Fps. The increased PLD activity was detected only when the cells were prelabeled with the PC-specific [3H]-myristate. These data support the hypothesis that v-fps-induced DG is derived from PC via the PLD/PAP pathway. |
| doi_str_mv | 10.1006/bbrc.1994.2309 |
| format | Article |
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The v-Fps-induced increases in DG were detected only when phospholipids were prelabeled with [3H]-myristate, which is incorporated primarily into phosphatidylcholine (PC). Inhibition of phosphatidic acid (PA) phosphatase (PAP), which converts PA to DG, blocked v-Fps-induced DG production. PA is a primary metabolite of type D phospholipases (PLD). Consistent with these observations, PLD activity was activated in response to the kinase activity of v-Fps. The increased PLD activity was detected only when the cells were prelabeled with the PC-specific [3H]-myristate. These data support the hypothesis that v-fps-induced DG is derived from PC via the PLD/PAP pathway.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.1994.2309</identifier><identifier>PMID: 8093039</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Arachidonic Acid - metabolism ; Cell Line, Transformed ; Diglycerides - metabolism ; Enzyme Activation ; Fibroblasts - metabolism ; Fusion Proteins, gag-onc - pharmacology ; Myristic Acid ; Myristic Acids - metabolism ; Phosphatidate Phosphatase - antagonists & inhibitors ; Phosphatidic Acids - metabolism ; Phosphatidylcholines - metabolism ; Phospholipase D - metabolism ; Propranolol - pharmacology ; Protein-Tyrosine Kinases - metabolism ; Rats ; Temperature</subject><ispartof>Biochemical and biophysical research communications, 1994-09, Vol.203 (2), p.1195-1203</ispartof><rights>1994 Academic Press</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c339t-24144a2029e0a13b1dc02f68aaa01dfe176be6eaa3ecf28e0a3d32ffd11c4d703</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X84723096$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8093039$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jiang, Y.W.</creatorcontrib><creatorcontrib>Song, J.G.</creatorcontrib><creatorcontrib>Zang, Q.</creatorcontrib><creatorcontrib>Foster, D.A.</creatorcontrib><title>Phosphatidylcholine-Specific Phospholipase D Activity Is Elevated in v-Fps-Transformed Cells</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Activating the protein-tyrosine kinase of v-Fps results in a rapid increase in diglyceride (DG) in rat fibroblasts. The v-Fps-induced increases in DG were detected only when phospholipids were prelabeled with [3H]-myristate, which is incorporated primarily into phosphatidylcholine (PC). Inhibition of phosphatidic acid (PA) phosphatase (PAP), which converts PA to DG, blocked v-Fps-induced DG production. PA is a primary metabolite of type D phospholipases (PLD). Consistent with these observations, PLD activity was activated in response to the kinase activity of v-Fps. The increased PLD activity was detected only when the cells were prelabeled with the PC-specific [3H]-myristate. These data support the hypothesis that v-fps-induced DG is derived from PC via the PLD/PAP pathway.</description><subject>Animals</subject><subject>Arachidonic Acid - metabolism</subject><subject>Cell Line, Transformed</subject><subject>Diglycerides - metabolism</subject><subject>Enzyme Activation</subject><subject>Fibroblasts - metabolism</subject><subject>Fusion Proteins, gag-onc - pharmacology</subject><subject>Myristic Acid</subject><subject>Myristic Acids - metabolism</subject><subject>Phosphatidate Phosphatase - antagonists & inhibitors</subject><subject>Phosphatidic Acids - metabolism</subject><subject>Phosphatidylcholines - metabolism</subject><subject>Phospholipase D - metabolism</subject><subject>Propranolol - pharmacology</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Rats</subject><subject>Temperature</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kMFLwzAUh4Moc06v3oSevLW-JKVrjmM6HQwUnOBBCGnywiJdW5OusP_ejA1vngLv970feR8htxQyClA8VJXXGRUizxgHcUbGFASkjEJ-TsYQiZQJ-nlJrkL4BqA0L8SIjEoQHLgYk6-3TRu6jeqd2dd609auwfS9Q-2s08kxjMNOBUwek5nu3eD6fbIMyVONg-rRJK5JhnTRhXTtVRNs67dxOMe6Dtfkwqo64M3pnZCPxdN6_pKuXp-X89kq1ZyLPmU5zXPFgAkERXlFjQZmi1IpBdRYpNOiwgKV4qgtKyPEDWfWGkp1bqbAJ-T-2Nv59meHoZdbF3T8gWqw3QU5LaaMMc4imB1B7dsQPFrZebdVfi8pyINOedApDzrlQWdcuDs176p41h9-8hfz8phjPG9w6GXQDhuNxnnUvTSt-6_6F6qrhU4</recordid><startdate>19940915</startdate><enddate>19940915</enddate><creator>Jiang, Y.W.</creator><creator>Song, J.G.</creator><creator>Zang, Q.</creator><creator>Foster, D.A.</creator><general>Elsevier Inc</general><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>7X8</scope></search><sort><creationdate>19940915</creationdate><title>Phosphatidylcholine-Specific Phospholipase D Activity Is Elevated in v-Fps-Transformed Cells</title><author>Jiang, Y.W. ; Song, J.G. ; Zang, Q. ; Foster, D.A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c339t-24144a2029e0a13b1dc02f68aaa01dfe176be6eaa3ecf28e0a3d32ffd11c4d703</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Animals</topic><topic>Arachidonic Acid - metabolism</topic><topic>Cell Line, Transformed</topic><topic>Diglycerides - metabolism</topic><topic>Enzyme Activation</topic><topic>Fibroblasts - metabolism</topic><topic>Fusion Proteins, gag-onc - pharmacology</topic><topic>Myristic Acid</topic><topic>Myristic Acids - metabolism</topic><topic>Phosphatidate Phosphatase - antagonists & inhibitors</topic><topic>Phosphatidic Acids - metabolism</topic><topic>Phosphatidylcholines - metabolism</topic><topic>Phospholipase D - metabolism</topic><topic>Propranolol - pharmacology</topic><topic>Protein-Tyrosine Kinases - metabolism</topic><topic>Rats</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jiang, Y.W.</creatorcontrib><creatorcontrib>Song, J.G.</creatorcontrib><creatorcontrib>Zang, Q.</creatorcontrib><creatorcontrib>Foster, D.A.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jiang, Y.W.</au><au>Song, J.G.</au><au>Zang, Q.</au><au>Foster, D.A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphatidylcholine-Specific Phospholipase D Activity Is Elevated in v-Fps-Transformed Cells</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1994-09-15</date><risdate>1994</risdate><volume>203</volume><issue>2</issue><spage>1195</spage><epage>1203</epage><pages>1195-1203</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Activating the protein-tyrosine kinase of v-Fps results in a rapid increase in diglyceride (DG) in rat fibroblasts. The v-Fps-induced increases in DG were detected only when phospholipids were prelabeled with [3H]-myristate, which is incorporated primarily into phosphatidylcholine (PC). Inhibition of phosphatidic acid (PA) phosphatase (PAP), which converts PA to DG, blocked v-Fps-induced DG production. PA is a primary metabolite of type D phospholipases (PLD). Consistent with these observations, PLD activity was activated in response to the kinase activity of v-Fps. The increased PLD activity was detected only when the cells were prelabeled with the PC-specific [3H]-myristate. These data support the hypothesis that v-fps-induced DG is derived from PC via the PLD/PAP pathway.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>8093039</pmid><doi>10.1006/bbrc.1994.2309</doi><tpages>9</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1994-09, Vol.203 (2), p.1195-1203 |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Animals Arachidonic Acid - metabolism Cell Line, Transformed Diglycerides - metabolism Enzyme Activation Fibroblasts - metabolism Fusion Proteins, gag-onc - pharmacology Myristic Acid Myristic Acids - metabolism Phosphatidate Phosphatase - antagonists & inhibitors Phosphatidic Acids - metabolism Phosphatidylcholines - metabolism Phospholipase D - metabolism Propranolol - pharmacology Protein-Tyrosine Kinases - metabolism Rats Temperature |
| title | Phosphatidylcholine-Specific Phospholipase D Activity Is Elevated in v-Fps-Transformed Cells |
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