pp60v-src reactivation inhibits serum-induced accumulation of inositol phosphates and phosphatidylethanol in tsNRK
In tsRSV-infected NRK (tsNRK) cells, pp60(v-src) reactivation by temperature-shift from a nonpermissive temperature, 39 C, to a permissive one, 32 degrees C, induced the production of inositol phosphates (IPt) and phosphatidylethanol (PEt). This was accompanied by an increase in membrane-associated...
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| Veröffentlicht in: | IUBMB life 1999-07, Vol.48 (1), p.85-89 |
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| creator | Kim, B Y Kim, J H Han, Y J Ahn, S C Kang, D O Oh, W K Ko, H R Lee, H S Mheen, T I Ahn, J S |
| description | In tsRSV-infected NRK (tsNRK) cells, pp60(v-src) reactivation by temperature-shift from a nonpermissive temperature, 39 C, to a permissive one, 32 degrees C, induced the production of inositol phosphates (IPt) and phosphatidylethanol (PEt). This was accompanied by an increase in membrane-associated protein kinase C (PKC) activity in the absence of exogenous growth factors. However, with serum-stimulation, the amounts of IPt and PEt at 32 degrees C were less than those at 39 degrees C. Pretreatment with PKC inhibitors, Ro-31-8220 and staurosporine, enhanced the accumulation of IPt but not of PEt at 32 degrees C. The tyrosine phosphorylation of phospholipase Cgamma1 (PLCgamma1) was increased either by serum or by pp60(v-src) reactivation. These results suggest that serum transduces its signal through PLCgamma1 mediation, and that pp60(v-src), possibly through the PKC mediation, negatively affects serum-induced PLCgamma1 activation. |
| doi_str_mv | 10.1080/152165499307468 |
| format | Article |
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This was accompanied by an increase in membrane-associated protein kinase C (PKC) activity in the absence of exogenous growth factors. However, with serum-stimulation, the amounts of IPt and PEt at 32 degrees C were less than those at 39 degrees C. Pretreatment with PKC inhibitors, Ro-31-8220 and staurosporine, enhanced the accumulation of IPt but not of PEt at 32 degrees C. The tyrosine phosphorylation of phospholipase Cgamma1 (PLCgamma1) was increased either by serum or by pp60(v-src) reactivation. These results suggest that serum transduces its signal through PLCgamma1 mediation, and that pp60(v-src), possibly through the PKC mediation, negatively affects serum-induced PLCgamma1 activation.</description><identifier>ISSN: 1521-6543</identifier><identifier>EISSN: 1521-6551</identifier><identifier>DOI: 10.1080/152165499307468</identifier><identifier>PMID: 10791920</identifier><language>eng</language><publisher>England</publisher><subject>Animals ; Benzoquinones ; Cell Line, Transformed ; Culture Media ; Enzyme Inhibitors - pharmacology ; Genes, src ; Glycerophospholipids - metabolism ; Indoles - pharmacology ; Inositol Phosphates - metabolism ; Isoenzymes - metabolism ; Kidney ; Kinetics ; Lactams, Macrocyclic ; Oncogene Protein pp60(v-src) - metabolism ; Phospholipase C gamma ; Phosphotyrosine - metabolism ; Protein Kinase C - antagonists & inhibitors ; Protein Kinase C - metabolism ; Quinones - pharmacology ; Rats ; Rifabutin - analogs & derivatives ; Staurosporine - pharmacology ; Temperature ; Type C Phospholipases - metabolism</subject><ispartof>IUBMB life, 1999-07, Vol.48 (1), p.85-89</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10791920$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kim, B Y</creatorcontrib><creatorcontrib>Kim, J H</creatorcontrib><creatorcontrib>Han, Y J</creatorcontrib><creatorcontrib>Ahn, S C</creatorcontrib><creatorcontrib>Kang, D O</creatorcontrib><creatorcontrib>Oh, W K</creatorcontrib><creatorcontrib>Ko, H R</creatorcontrib><creatorcontrib>Lee, H S</creatorcontrib><creatorcontrib>Mheen, T I</creatorcontrib><creatorcontrib>Ahn, J S</creatorcontrib><title>pp60v-src reactivation inhibits serum-induced accumulation of inositol phosphates and phosphatidylethanol in tsNRK</title><title>IUBMB life</title><addtitle>IUBMB Life</addtitle><description>In tsRSV-infected NRK (tsNRK) cells, pp60(v-src) reactivation by temperature-shift from a nonpermissive temperature, 39 C, to a permissive one, 32 degrees C, induced the production of inositol phosphates (IPt) and phosphatidylethanol (PEt). This was accompanied by an increase in membrane-associated protein kinase C (PKC) activity in the absence of exogenous growth factors. However, with serum-stimulation, the amounts of IPt and PEt at 32 degrees C were less than those at 39 degrees C. Pretreatment with PKC inhibitors, Ro-31-8220 and staurosporine, enhanced the accumulation of IPt but not of PEt at 32 degrees C. The tyrosine phosphorylation of phospholipase Cgamma1 (PLCgamma1) was increased either by serum or by pp60(v-src) reactivation. These results suggest that serum transduces its signal through PLCgamma1 mediation, and that pp60(v-src), possibly through the PKC mediation, negatively affects serum-induced PLCgamma1 activation.</description><subject>Animals</subject><subject>Benzoquinones</subject><subject>Cell Line, Transformed</subject><subject>Culture Media</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Genes, src</subject><subject>Glycerophospholipids - metabolism</subject><subject>Indoles - pharmacology</subject><subject>Inositol Phosphates - metabolism</subject><subject>Isoenzymes - metabolism</subject><subject>Kidney</subject><subject>Kinetics</subject><subject>Lactams, Macrocyclic</subject><subject>Oncogene Protein pp60(v-src) - metabolism</subject><subject>Phospholipase C gamma</subject><subject>Phosphotyrosine - metabolism</subject><subject>Protein Kinase C - antagonists & inhibitors</subject><subject>Protein Kinase C - metabolism</subject><subject>Quinones - pharmacology</subject><subject>Rats</subject><subject>Rifabutin - analogs & derivatives</subject><subject>Staurosporine - pharmacology</subject><subject>Temperature</subject><subject>Type C Phospholipases - metabolism</subject><issn>1521-6543</issn><issn>1521-6551</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkM1LxDAQxYMo7rp69iY9eaubtGmbHGXxCxcF2XvJx5RG2qYm6cL-97Z0WcS5zLzhNw_mIXRL8APBDK9JlpA8o5ynuKA5O0PLaRPnWUbOTzNNF-jK-288VoH5JVoQXHDCE7xEru9zvI-9U5EDoYLZi2BsF5muNtIEH3lwQxubTg8KdCSUGtqhmRlbjZj1Jtgm6mvr-1oE8JHo9EkafWgg1KIbEdNFwX98vV-ji0o0Hm6OfYV2z0-7zWu8_Xx52zxuY8Upnl5gSgLTssBYySSrtE6prDSrlFScyYpJIkWaMQIUp6BHUmhK8oQIUAlJV-h-tu2d_RnAh7I1XkHTiA7s4Muc0yKjmI_gegaVs947qMremVa4Q0lwOaVc_kt5vLg7Wg-yBf2Hn2NNfwH6y3rZ</recordid><startdate>199907</startdate><enddate>199907</enddate><creator>Kim, B Y</creator><creator>Kim, J H</creator><creator>Han, Y J</creator><creator>Ahn, S C</creator><creator>Kang, D O</creator><creator>Oh, W K</creator><creator>Ko, H R</creator><creator>Lee, H S</creator><creator>Mheen, T I</creator><creator>Ahn, J S</creator><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>199907</creationdate><title>pp60v-src reactivation inhibits serum-induced accumulation of inositol phosphates and phosphatidylethanol in tsNRK</title><author>Kim, B Y ; Kim, J H ; Han, Y J ; Ahn, S C ; Kang, D O ; Oh, W K ; Ko, H R ; Lee, H S ; Mheen, T I ; Ahn, J S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c940-6558cbe8db700cb25fdd34bfd8fcbc98bf8b1ba3581e403ed8dbad41621aec213</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Animals</topic><topic>Benzoquinones</topic><topic>Cell Line, Transformed</topic><topic>Culture Media</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Genes, src</topic><topic>Glycerophospholipids - metabolism</topic><topic>Indoles - pharmacology</topic><topic>Inositol Phosphates - metabolism</topic><topic>Isoenzymes - metabolism</topic><topic>Kidney</topic><topic>Kinetics</topic><topic>Lactams, Macrocyclic</topic><topic>Oncogene Protein pp60(v-src) - metabolism</topic><topic>Phospholipase C gamma</topic><topic>Phosphotyrosine - metabolism</topic><topic>Protein Kinase C - antagonists & inhibitors</topic><topic>Protein Kinase C - metabolism</topic><topic>Quinones - pharmacology</topic><topic>Rats</topic><topic>Rifabutin - analogs & derivatives</topic><topic>Staurosporine - pharmacology</topic><topic>Temperature</topic><topic>Type C Phospholipases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kim, B Y</creatorcontrib><creatorcontrib>Kim, J H</creatorcontrib><creatorcontrib>Han, Y J</creatorcontrib><creatorcontrib>Ahn, S C</creatorcontrib><creatorcontrib>Kang, D O</creatorcontrib><creatorcontrib>Oh, W K</creatorcontrib><creatorcontrib>Ko, H R</creatorcontrib><creatorcontrib>Lee, H S</creatorcontrib><creatorcontrib>Mheen, T I</creatorcontrib><creatorcontrib>Ahn, J S</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>IUBMB life</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kim, B Y</au><au>Kim, J H</au><au>Han, Y J</au><au>Ahn, S C</au><au>Kang, D O</au><au>Oh, W K</au><au>Ko, H R</au><au>Lee, H S</au><au>Mheen, T I</au><au>Ahn, J S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>pp60v-src reactivation inhibits serum-induced accumulation of inositol phosphates and phosphatidylethanol in tsNRK</atitle><jtitle>IUBMB life</jtitle><addtitle>IUBMB Life</addtitle><date>1999-07</date><risdate>1999</risdate><volume>48</volume><issue>1</issue><spage>85</spage><epage>89</epage><pages>85-89</pages><issn>1521-6543</issn><eissn>1521-6551</eissn><abstract>In tsRSV-infected NRK (tsNRK) cells, pp60(v-src) reactivation by temperature-shift from a nonpermissive temperature, 39 C, to a permissive one, 32 degrees C, induced the production of inositol phosphates (IPt) and phosphatidylethanol (PEt). This was accompanied by an increase in membrane-associated protein kinase C (PKC) activity in the absence of exogenous growth factors. However, with serum-stimulation, the amounts of IPt and PEt at 32 degrees C were less than those at 39 degrees C. Pretreatment with PKC inhibitors, Ro-31-8220 and staurosporine, enhanced the accumulation of IPt but not of PEt at 32 degrees C. The tyrosine phosphorylation of phospholipase Cgamma1 (PLCgamma1) was increased either by serum or by pp60(v-src) reactivation. These results suggest that serum transduces its signal through PLCgamma1 mediation, and that pp60(v-src), possibly through the PKC mediation, negatively affects serum-induced PLCgamma1 activation.</abstract><cop>England</cop><pmid>10791920</pmid><doi>10.1080/152165499307468</doi><tpages>5</tpages></addata></record> |
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| subjects | Animals Benzoquinones Cell Line, Transformed Culture Media Enzyme Inhibitors - pharmacology Genes, src Glycerophospholipids - metabolism Indoles - pharmacology Inositol Phosphates - metabolism Isoenzymes - metabolism Kidney Kinetics Lactams, Macrocyclic Oncogene Protein pp60(v-src) - metabolism Phospholipase C gamma Phosphotyrosine - metabolism Protein Kinase C - antagonists & inhibitors Protein Kinase C - metabolism Quinones - pharmacology Rats Rifabutin - analogs & derivatives Staurosporine - pharmacology Temperature Type C Phospholipases - metabolism |
| title | pp60v-src reactivation inhibits serum-induced accumulation of inositol phosphates and phosphatidylethanol in tsNRK |
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