Endogenous Phosphoinositide Precursors of Inositol Phosphates in Rat Brain Cortical Membranes
The appearance of Ins1P as an index of direct PtdIns breakdown by phospholipase C was examined in rat brain cortical membranes using either exogenous [3H]PtdIns substrate or [3H]inositol-prelabeled endogenous phosphoinositide substrates. Production of [3H]Ins1P was observed using exogenous [3H]PtdIn...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1993-06, Vol.193 (3), p.1061-1067 |
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| creator | Claro, E. Sarri, E. Picatoste, F. |
| description | The appearance of Ins1P as an index of direct PtdIns breakdown by phospholipase C was examined in rat brain cortical membranes using either exogenous [3H]PtdIns substrate or [3H]inositol-prelabeled endogenous phosphoinositide substrates. Production of [3H]Ins1P was observed using exogenous [3H]PtdIns but not with endogenous substrate over the physiological range of calcium concentrations. [3H]Ins1,4P2 and [3H]Ins4P, derived from phospholipase C breakdown of polyphosphoinositides, were formed by membranes from both exogenous [3H]PtdIns and endogenous 3H-phosphoinositides, in the presence of ATP. The contribution of endogenous PtdInsP2 and PtdInsP to the generation of inositol phosphates was examined in membranes from [3H]inositol-prelabeled brain slices by adding unlabeled Ins1,4,5P3 to trap [3H]Ins1,4,5P3 generated upon breakdown of [3H]PtdInsP2. The maximal rate of [3H]Ins1,4,5P3 appearance was attained in the presence of 150-200 μM added Ins1,4,5P3 and represented 12.5% of the combined rates of formation of [3H]Ins1,4,5P3 and [3H]Ins1,4P2, similar to the content of [3H]PtdInsP2 relative to total 3H-polyphosphoinositides. The results show that, while endogenous PtdIns is not degraded by phospholipase C, the enzyme appears to be equally effective to cleave endogenous PtdInsP2 and PtdInsP. |
| doi_str_mv | 10.1006/bbrc.1993.1733 |
| format | Article |
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Production of [3H]Ins1P was observed using exogenous [3H]PtdIns but not with endogenous substrate over the physiological range of calcium concentrations. [3H]Ins1,4P2 and [3H]Ins4P, derived from phospholipase C breakdown of polyphosphoinositides, were formed by membranes from both exogenous [3H]PtdIns and endogenous 3H-phosphoinositides, in the presence of ATP. The contribution of endogenous PtdInsP2 and PtdInsP to the generation of inositol phosphates was examined in membranes from [3H]inositol-prelabeled brain slices by adding unlabeled Ins1,4,5P3 to trap [3H]Ins1,4,5P3 generated upon breakdown of [3H]PtdInsP2. The maximal rate of [3H]Ins1,4,5P3 appearance was attained in the presence of 150-200 μM added Ins1,4,5P3 and represented 12.5% of the combined rates of formation of [3H]Ins1,4,5P3 and [3H]Ins1,4P2, similar to the content of [3H]PtdInsP2 relative to total 3H-polyphosphoinositides. The results show that, while endogenous PtdIns is not degraded by phospholipase C, the enzyme appears to be equally effective to cleave endogenous PtdInsP2 and PtdInsP.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.1993.1733</identifier><identifier>PMID: 8391798</identifier><identifier>CODEN: BBRCA9</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Calcium - pharmacology ; Cell Membrane - metabolism ; Cerebral Cortex - metabolism ; Fundamental and applied biological sciences. Psychology ; In Vitro Techniques ; Inositol - metabolism ; Inositol Phosphates - metabolism ; Intermediary metabolites. Miscellaneous ; Kinetics ; Membrane Proteins - analysis ; Membrane Proteins - metabolism ; Other biological molecules ; Phosphatidylinositols - analysis ; Phosphatidylinositols - metabolism ; Rats ; Tritium ; Type C Phospholipases - metabolism</subject><ispartof>Biochemical and biophysical research communications, 1993-06, Vol.193 (3), p.1061-1067</ispartof><rights>1993 Academic Press</rights><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c368t-b2f44a82fbafef0028373612b3116dace41f9343ae50209e00219809538462913</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X8371733X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4827792$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8391798$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Claro, E.</creatorcontrib><creatorcontrib>Sarri, E.</creatorcontrib><creatorcontrib>Picatoste, F.</creatorcontrib><title>Endogenous Phosphoinositide Precursors of Inositol Phosphates in Rat Brain Cortical Membranes</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The appearance of Ins1P as an index of direct PtdIns breakdown by phospholipase C was examined in rat brain cortical membranes using either exogenous [3H]PtdIns substrate or [3H]inositol-prelabeled endogenous phosphoinositide substrates. Production of [3H]Ins1P was observed using exogenous [3H]PtdIns but not with endogenous substrate over the physiological range of calcium concentrations. [3H]Ins1,4P2 and [3H]Ins4P, derived from phospholipase C breakdown of polyphosphoinositides, were formed by membranes from both exogenous [3H]PtdIns and endogenous 3H-phosphoinositides, in the presence of ATP. The contribution of endogenous PtdInsP2 and PtdInsP to the generation of inositol phosphates was examined in membranes from [3H]inositol-prelabeled brain slices by adding unlabeled Ins1,4,5P3 to trap [3H]Ins1,4,5P3 generated upon breakdown of [3H]PtdInsP2. The maximal rate of [3H]Ins1,4,5P3 appearance was attained in the presence of 150-200 μM added Ins1,4,5P3 and represented 12.5% of the combined rates of formation of [3H]Ins1,4,5P3 and [3H]Ins1,4P2, similar to the content of [3H]PtdInsP2 relative to total 3H-polyphosphoinositides. The results show that, while endogenous PtdIns is not degraded by phospholipase C, the enzyme appears to be equally effective to cleave endogenous PtdInsP2 and PtdInsP.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Calcium - pharmacology</subject><subject>Cell Membrane - metabolism</subject><subject>Cerebral Cortex - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>In Vitro Techniques</subject><subject>Inositol - metabolism</subject><subject>Inositol Phosphates - metabolism</subject><subject>Intermediary metabolites. Miscellaneous</subject><subject>Kinetics</subject><subject>Membrane Proteins - analysis</subject><subject>Membrane Proteins - metabolism</subject><subject>Other biological molecules</subject><subject>Phosphatidylinositols - analysis</subject><subject>Phosphatidylinositols - metabolism</subject><subject>Rats</subject><subject>Tritium</subject><subject>Type C Phospholipases - metabolism</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kEtLLDEQRoNc8Y6PrbsLvbi46zGv6U6WOvgCRREFNxLS6YpGejpjqkfw35txGneuUqROFfUdQg4ZnTJKq-OmSW7KtBZTVguxRSaMalpyRuUfMqGZKLlmT3_JLuIbpYzJSu-QHSU0q7WakOezvo0v0McVFnevEZevMfQRwxBaKO4SuFXCmLCIvrj6_o_dyNkBsAh9cW-H4jTZXM1jGoKzXXEDiybZHnCfbHvbIRyM7x55PD97mF-W17cXV_OT69KJSg1lw72UVnHfWA-eUq5ELSrGG8FY1VoHknktpLAwo5xqyATTiuqZULLK8cQeOdrsXab4vgIczCKgg67LR-Rkpp6pPM5lBqcb0KWImMCbZQoLmz4No2bt06x9mrVPs_aZB_6Nm1fNAtoffBSY-__HvsUc3efYLuAPJhWva80zpjYYZAsfAZJBF6B30IbseDBtDL9d8AXBQpDv</recordid><startdate>19930630</startdate><enddate>19930630</enddate><creator>Claro, E.</creator><creator>Sarri, E.</creator><creator>Picatoste, F.</creator><general>Elsevier Inc</general><general>Elsevier</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>7X8</scope></search><sort><creationdate>19930630</creationdate><title>Endogenous Phosphoinositide Precursors of Inositol Phosphates in Rat Brain Cortical Membranes</title><author>Claro, E. ; Sarri, E. ; Picatoste, F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c368t-b2f44a82fbafef0028373612b3116dace41f9343ae50209e00219809538462913</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Calcium - pharmacology</topic><topic>Cell Membrane - metabolism</topic><topic>Cerebral Cortex - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>In Vitro Techniques</topic><topic>Inositol - metabolism</topic><topic>Inositol Phosphates - metabolism</topic><topic>Intermediary metabolites. Miscellaneous</topic><topic>Kinetics</topic><topic>Membrane Proteins - analysis</topic><topic>Membrane Proteins - metabolism</topic><topic>Other biological molecules</topic><topic>Phosphatidylinositols - analysis</topic><topic>Phosphatidylinositols - metabolism</topic><topic>Rats</topic><topic>Tritium</topic><topic>Type C Phospholipases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Claro, E.</creatorcontrib><creatorcontrib>Sarri, E.</creatorcontrib><creatorcontrib>Picatoste, F.</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>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Claro, E.</au><au>Sarri, E.</au><au>Picatoste, F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Endogenous Phosphoinositide Precursors of Inositol Phosphates in Rat Brain Cortical Membranes</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1993-06-30</date><risdate>1993</risdate><volume>193</volume><issue>3</issue><spage>1061</spage><epage>1067</epage><pages>1061-1067</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>The appearance of Ins1P as an index of direct PtdIns breakdown by phospholipase C was examined in rat brain cortical membranes using either exogenous [3H]PtdIns substrate or [3H]inositol-prelabeled endogenous phosphoinositide substrates. Production of [3H]Ins1P was observed using exogenous [3H]PtdIns but not with endogenous substrate over the physiological range of calcium concentrations. [3H]Ins1,4P2 and [3H]Ins4P, derived from phospholipase C breakdown of polyphosphoinositides, were formed by membranes from both exogenous [3H]PtdIns and endogenous 3H-phosphoinositides, in the presence of ATP. The contribution of endogenous PtdInsP2 and PtdInsP to the generation of inositol phosphates was examined in membranes from [3H]inositol-prelabeled brain slices by adding unlabeled Ins1,4,5P3 to trap [3H]Ins1,4,5P3 generated upon breakdown of [3H]PtdInsP2. The maximal rate of [3H]Ins1,4,5P3 appearance was attained in the presence of 150-200 μM added Ins1,4,5P3 and represented 12.5% of the combined rates of formation of [3H]Ins1,4,5P3 and [3H]Ins1,4P2, similar to the content of [3H]PtdInsP2 relative to total 3H-polyphosphoinositides. The results show that, while endogenous PtdIns is not degraded by phospholipase C, the enzyme appears to be equally effective to cleave endogenous PtdInsP2 and PtdInsP.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>8391798</pmid><doi>10.1006/bbrc.1993.1733</doi><tpages>7</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1993-06, Vol.193 (3), p.1061-1067 |
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| subjects | Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Calcium - pharmacology Cell Membrane - metabolism Cerebral Cortex - metabolism Fundamental and applied biological sciences. Psychology In Vitro Techniques Inositol - metabolism Inositol Phosphates - metabolism Intermediary metabolites. Miscellaneous Kinetics Membrane Proteins - analysis Membrane Proteins - metabolism Other biological molecules Phosphatidylinositols - analysis Phosphatidylinositols - metabolism Rats Tritium Type C Phospholipases - metabolism |
| title | Endogenous Phosphoinositide Precursors of Inositol Phosphates in Rat Brain Cortical Membranes |
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