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CALCIUM-SENSITIVITY OF INOSITOL 1,4,5-TRISPHOSPHATE METABOLISM IN EXOCRINE CELLS FROM THE AVIAN SALT-GLAND
The generation of inositol phosphates upon muscarinic-receptor activation was studied in [H-3]inositol-loaded exocrine cells from the nasal salt glands of the duck Anas platyrhynchos, and the metabolism of different inositol phosphates in vitro was studied in tissue homogenates, with particular refe...
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| Published in: | Biochemical journal 1992-03, Vol.282 (3), p.703-710 |
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| creator | HILDEBRANDT, JP SHUTTLEWORTH, TJ |
| description | The generation of inositol phosphates upon muscarinic-receptor activation was studied in [H-3]inositol-loaded exocrine cells from the nasal salt glands of the duck Anas platyrhynchos, and the metabolism of different inositol phosphates in vitro was studied in tissue homogenates, with particular reference to the possible interaction of changes in intracellular [Ca2+] ([Ca2+]i) with the metabolic processes. In intact cells, there was a rapid (within 15 s) generation of Ins(1,4,5)P3 and Ins(1,3,4,5)P4, followed by an accumulation of their breakdown products, Ins(1,3,4)P3 and inositol bis- and mono-phosphates. Ca2+-sensitivity of the Ins(1,4,5)P3 3-kinase was demonstrated in tissue homogenates, with the rate of phosphorylation increasing 2-fold at free Ca2+ concentrations > 1-mu-M. However, addition of calmodulin or the presence of the calmodulin inhibitor W-7 (up to 100-mu-M) had no effect. 3-Kinase activity increased proportionally with the initial Ins(1,4,5)P3 concentration up to 1-mu-M, but a 10-fold higher substrate concentration produced only a doubling in the phosphorylation rate. Ins(1,3,4,5)P4 was dephosphorylated to Ins(1,3,4)P3, which accumulated in the homogenate assays as well as in intact cells. Depending on its concentration, Ins(1,3,4)P3 was phosphorylated [in part to Ins(1,3,4,6)P4] or dephosphorylated. To investigate the Ca2+-sensitivity of the 3-kinase in intact cells, excess quin2 was used to buffer the receptor-mediated transient changes in [Ca2+]i in [H-3]inositol-loaded cells. These experiments revealed that increasing [Ca2+]i, from < 100 to approx. 400 nM (i.e. within the physiological range) has no effect on the partitioning of Ins(1,4,5)P3 metabolism (phosphorylation versus dephosphorylation) and on the accumulation of Ins(1,4,5)P3 and Ins(1,3,4,5)P4. This indicates that activation of the 3-kinase by physiologically relevant Ca2+ concentrations may not play a major role in the generation of Ins(1,3,4,5)P4 signals upon receptor activation in these cells. The latter are mainly achieved by the receptor-mediated increase in Ins(1,4,5)P3 in the cell and its phosphorylation by the 3-kinase in a substrate-concentration-dependent manner. |
| doi_str_mv | 10.1042/bj2820703 |
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In intact cells, there was a rapid (within 15 s) generation of Ins(1,4,5)P3 and Ins(1,3,4,5)P4, followed by an accumulation of their breakdown products, Ins(1,3,4)P3 and inositol bis- and mono-phosphates. Ca2+-sensitivity of the Ins(1,4,5)P3 3-kinase was demonstrated in tissue homogenates, with the rate of phosphorylation increasing 2-fold at free Ca2+ concentrations > 1-mu-M. However, addition of calmodulin or the presence of the calmodulin inhibitor W-7 (up to 100-mu-M) had no effect. 3-Kinase activity increased proportionally with the initial Ins(1,4,5)P3 concentration up to 1-mu-M, but a 10-fold higher substrate concentration produced only a doubling in the phosphorylation rate. Ins(1,3,4,5)P4 was dephosphorylated to Ins(1,3,4)P3, which accumulated in the homogenate assays as well as in intact cells. Depending on its concentration, Ins(1,3,4)P3 was phosphorylated [in part to Ins(1,3,4,6)P4] or dephosphorylated. To investigate the Ca2+-sensitivity of the 3-kinase in intact cells, excess quin2 was used to buffer the receptor-mediated transient changes in [Ca2+]i in [H-3]inositol-loaded cells. These experiments revealed that increasing [Ca2+]i, from < 100 to approx. 400 nM (i.e. within the physiological range) has no effect on the partitioning of Ins(1,4,5)P3 metabolism (phosphorylation versus dephosphorylation) and on the accumulation of Ins(1,4,5)P3 and Ins(1,3,4,5)P4. This indicates that activation of the 3-kinase by physiologically relevant Ca2+ concentrations may not play a major role in the generation of Ins(1,3,4,5)P4 signals upon receptor activation in these cells. The latter are mainly achieved by the receptor-mediated increase in Ins(1,4,5)P3 in the cell and its phosphorylation by the 3-kinase in a substrate-concentration-dependent manner.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj2820703</identifier><identifier>PMID: 1313230</identifier><language>eng</language><publisher>LONDON: PORTLAND PRESS</publisher><subject>Analytical, structural and metabolic biochemistry ; Anas platyrhynchos ; Animals ; Biochemistry & Molecular Biology ; Biological and medical sciences ; Calcium - pharmacology ; Calcium - physiology ; Ducks ; Fundamental and applied biological sciences. Psychology ; In Vitro Techniques ; Inositol - pharmacokinetics ; Inositol 1,4,5-Trisphosphate - metabolism ; Inositol 1,4,5-Trisphosphate - pharmacokinetics ; Inositol Phosphates - metabolism ; Intermediary metabolites. Miscellaneous ; Life Sciences & Biomedicine ; Other biological molecules ; Phosphotransferases (Alcohol Group Acceptor) ; Phosphotransferases - physiology ; Salt Gland - cytology ; Salt Gland - metabolism ; Science & Technology ; Signal Transduction - physiology ; Tritium</subject><ispartof>Biochemical journal, 1992-03, Vol.282 (3), p.703-710</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>13</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wosA1992HK34200014</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c430t-4b0ca0a511e26c0dccf28ff714843d99a923b11551b5b70c5bb4c4ce6b2a24483</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1130844/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1130844/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,315,733,786,790,891,27225,27957,27958,53827,53829</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5251275$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1313230$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>HILDEBRANDT, JP</creatorcontrib><creatorcontrib>SHUTTLEWORTH, TJ</creatorcontrib><title>CALCIUM-SENSITIVITY OF INOSITOL 1,4,5-TRISPHOSPHATE METABOLISM IN EXOCRINE CELLS FROM THE AVIAN SALT-GLAND</title><title>Biochemical journal</title><addtitle>BIOCHEM J</addtitle><addtitle>Biochem J</addtitle><description>The generation of inositol phosphates upon muscarinic-receptor activation was studied in [H-3]inositol-loaded exocrine cells from the nasal salt glands of the duck Anas platyrhynchos, and the metabolism of different inositol phosphates in vitro was studied in tissue homogenates, with particular reference to the possible interaction of changes in intracellular [Ca2+] ([Ca2+]i) with the metabolic processes. In intact cells, there was a rapid (within 15 s) generation of Ins(1,4,5)P3 and Ins(1,3,4,5)P4, followed by an accumulation of their breakdown products, Ins(1,3,4)P3 and inositol bis- and mono-phosphates. Ca2+-sensitivity of the Ins(1,4,5)P3 3-kinase was demonstrated in tissue homogenates, with the rate of phosphorylation increasing 2-fold at free Ca2+ concentrations > 1-mu-M. However, addition of calmodulin or the presence of the calmodulin inhibitor W-7 (up to 100-mu-M) had no effect. 3-Kinase activity increased proportionally with the initial Ins(1,4,5)P3 concentration up to 1-mu-M, but a 10-fold higher substrate concentration produced only a doubling in the phosphorylation rate. Ins(1,3,4,5)P4 was dephosphorylated to Ins(1,3,4)P3, which accumulated in the homogenate assays as well as in intact cells. Depending on its concentration, Ins(1,3,4)P3 was phosphorylated [in part to Ins(1,3,4,6)P4] or dephosphorylated. To investigate the Ca2+-sensitivity of the 3-kinase in intact cells, excess quin2 was used to buffer the receptor-mediated transient changes in [Ca2+]i in [H-3]inositol-loaded cells. These experiments revealed that increasing [Ca2+]i, from < 100 to approx. 400 nM (i.e. within the physiological range) has no effect on the partitioning of Ins(1,4,5)P3 metabolism (phosphorylation versus dephosphorylation) and on the accumulation of Ins(1,4,5)P3 and Ins(1,3,4,5)P4. This indicates that activation of the 3-kinase by physiologically relevant Ca2+ concentrations may not play a major role in the generation of Ins(1,3,4,5)P4 signals upon receptor activation in these cells. The latter are mainly achieved by the receptor-mediated increase in Ins(1,4,5)P3 in the cell and its phosphorylation by the 3-kinase in a substrate-concentration-dependent manner.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Anas platyrhynchos</subject><subject>Animals</subject><subject>Biochemistry & Molecular Biology</subject><subject>Biological and medical sciences</subject><subject>Calcium - pharmacology</subject><subject>Calcium - physiology</subject><subject>Ducks</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>In Vitro Techniques</subject><subject>Inositol - pharmacokinetics</subject><subject>Inositol 1,4,5-Trisphosphate - metabolism</subject><subject>Inositol 1,4,5-Trisphosphate - pharmacokinetics</subject><subject>Inositol Phosphates - metabolism</subject><subject>Intermediary metabolites. Miscellaneous</subject><subject>Life Sciences & Biomedicine</subject><subject>Other biological molecules</subject><subject>Phosphotransferases (Alcohol Group Acceptor)</subject><subject>Phosphotransferases - physiology</subject><subject>Salt Gland - cytology</subject><subject>Salt Gland - metabolism</subject><subject>Science & Technology</subject><subject>Signal Transduction - physiology</subject><subject>Tritium</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EZCTM</sourceid><recordid>eNqNkl-L1DAUxYso67j64AcQ-iCCuNV7k_Tfi1C7nZ1gp5Vpd9GnkmRS7TDT7jYdxW9vlhlGfdKHEML53cPhnjjOc4S3CIy8kxsSEQiBPnBmyELwopBED50ZkIB5ARB87DwxZgOADBicOWdIkRIKM2eTJnnKr5delRUVr_kNr7-45dzlRWmfZe7iBbvwvXrFq0-L0p6kztxlVicfypxXS8u52ecyXfEic9Mszyt3viqXbr3I3OSGJ4VbJXntXeVJcfnUedSKrdHPjve5cz3P6nTh5eUVtzE8xShMHpOgBAgfUZNAwVqplkRtGyKLGF3HsYgJlYi-j9KXIShfSqaY0oEkgjAW0XPn_cH3di93eq10P41i29yO3U6MP5tBdM3fSt99a74O3xtEChFj1uDV0WAc7vbaTM2uM0pvt6LXw940drcBAxr-E8SAIA18sODrA6jGwZhRt6c0CM19g82pQcu--DP-b_JQmdVfHnVhlNi2o-hVZ06YT3wkoW-x6ID90HJojep0r_SJSjCOyeIjZQTuP0XaTWLqhj4d9v1kR9_8_yj9BfC3urw</recordid><startdate>19920315</startdate><enddate>19920315</enddate><creator>HILDEBRANDT, JP</creator><creator>SHUTTLEWORTH, TJ</creator><general>PORTLAND PRESS</general><general>Portland Press</general><scope>BLEPL</scope><scope>DTL</scope><scope>EZCTM</scope><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>7QP</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19920315</creationdate><title>CALCIUM-SENSITIVITY OF INOSITOL 1,4,5-TRISPHOSPHATE METABOLISM IN EXOCRINE CELLS FROM THE AVIAN SALT-GLAND</title><author>HILDEBRANDT, JP ; SHUTTLEWORTH, TJ</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c430t-4b0ca0a511e26c0dccf28ff714843d99a923b11551b5b70c5bb4c4ce6b2a24483</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Anas platyrhynchos</topic><topic>Animals</topic><topic>Biochemistry & Molecular Biology</topic><topic>Biological and medical sciences</topic><topic>Calcium - pharmacology</topic><topic>Calcium - physiology</topic><topic>Ducks</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>In Vitro Techniques</topic><topic>Inositol - pharmacokinetics</topic><topic>Inositol 1,4,5-Trisphosphate - metabolism</topic><topic>Inositol 1,4,5-Trisphosphate - pharmacokinetics</topic><topic>Inositol Phosphates - metabolism</topic><topic>Intermediary metabolites. Miscellaneous</topic><topic>Life Sciences & Biomedicine</topic><topic>Other biological molecules</topic><topic>Phosphotransferases (Alcohol Group Acceptor)</topic><topic>Phosphotransferases - physiology</topic><topic>Salt Gland - cytology</topic><topic>Salt Gland - metabolism</topic><topic>Science & Technology</topic><topic>Signal Transduction - physiology</topic><topic>Tritium</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>HILDEBRANDT, JP</creatorcontrib><creatorcontrib>SHUTTLEWORTH, TJ</creatorcontrib><collection>Web of Science Core Collection</collection><collection>Science Citation Index Expanded</collection><collection>Web of Science - Science Citation Index Expanded - 1992</collection><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>Calcium & Calcified Tissue Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>HILDEBRANDT, JP</au><au>SHUTTLEWORTH, TJ</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>CALCIUM-SENSITIVITY OF INOSITOL 1,4,5-TRISPHOSPHATE METABOLISM IN EXOCRINE CELLS FROM THE AVIAN SALT-GLAND</atitle><jtitle>Biochemical journal</jtitle><stitle>BIOCHEM J</stitle><addtitle>Biochem J</addtitle><date>1992-03-15</date><risdate>1992</risdate><volume>282</volume><issue>3</issue><spage>703</spage><epage>710</epage><pages>703-710</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><notes>Medline</notes><notes>ObjectType-Article-2</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-1</notes><notes>content type line 23</notes><notes>ObjectType-Article-1</notes><notes>ObjectType-Feature-2</notes><abstract>The generation of inositol phosphates upon muscarinic-receptor activation was studied in [H-3]inositol-loaded exocrine cells from the nasal salt glands of the duck Anas platyrhynchos, and the metabolism of different inositol phosphates in vitro was studied in tissue homogenates, with particular reference to the possible interaction of changes in intracellular [Ca2+] ([Ca2+]i) with the metabolic processes. In intact cells, there was a rapid (within 15 s) generation of Ins(1,4,5)P3 and Ins(1,3,4,5)P4, followed by an accumulation of their breakdown products, Ins(1,3,4)P3 and inositol bis- and mono-phosphates. Ca2+-sensitivity of the Ins(1,4,5)P3 3-kinase was demonstrated in tissue homogenates, with the rate of phosphorylation increasing 2-fold at free Ca2+ concentrations > 1-mu-M. However, addition of calmodulin or the presence of the calmodulin inhibitor W-7 (up to 100-mu-M) had no effect. 3-Kinase activity increased proportionally with the initial Ins(1,4,5)P3 concentration up to 1-mu-M, but a 10-fold higher substrate concentration produced only a doubling in the phosphorylation rate. Ins(1,3,4,5)P4 was dephosphorylated to Ins(1,3,4)P3, which accumulated in the homogenate assays as well as in intact cells. Depending on its concentration, Ins(1,3,4)P3 was phosphorylated [in part to Ins(1,3,4,6)P4] or dephosphorylated. To investigate the Ca2+-sensitivity of the 3-kinase in intact cells, excess quin2 was used to buffer the receptor-mediated transient changes in [Ca2+]i in [H-3]inositol-loaded cells. These experiments revealed that increasing [Ca2+]i, from < 100 to approx. 400 nM (i.e. within the physiological range) has no effect on the partitioning of Ins(1,4,5)P3 metabolism (phosphorylation versus dephosphorylation) and on the accumulation of Ins(1,4,5)P3 and Ins(1,3,4,5)P4. This indicates that activation of the 3-kinase by physiologically relevant Ca2+ concentrations may not play a major role in the generation of Ins(1,3,4,5)P4 signals upon receptor activation in these cells. The latter are mainly achieved by the receptor-mediated increase in Ins(1,4,5)P3 in the cell and its phosphorylation by the 3-kinase in a substrate-concentration-dependent manner.</abstract><cop>LONDON</cop><pub>PORTLAND PRESS</pub><pmid>1313230</pmid><doi>10.1042/bj2820703</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Biochemical journal, 1992-03, Vol.282 (3), p.703-710 |
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| source | Web of Science - Science Citation Index Expanded - 1992<img src="https://exlibris-pub.s3.amazonaws.com/fromwos-v2.jpg" />; PubMed Central |
| subjects | Analytical, structural and metabolic biochemistry Anas platyrhynchos Animals Biochemistry & Molecular Biology Biological and medical sciences Calcium - pharmacology Calcium - physiology Ducks Fundamental and applied biological sciences. Psychology In Vitro Techniques Inositol - pharmacokinetics Inositol 1,4,5-Trisphosphate - metabolism Inositol 1,4,5-Trisphosphate - pharmacokinetics Inositol Phosphates - metabolism Intermediary metabolites. Miscellaneous Life Sciences & Biomedicine Other biological molecules Phosphotransferases (Alcohol Group Acceptor) Phosphotransferases - physiology Salt Gland - cytology Salt Gland - metabolism Science & Technology Signal Transduction - physiology Tritium |
| title | CALCIUM-SENSITIVITY OF INOSITOL 1,4,5-TRISPHOSPHATE METABOLISM IN EXOCRINE CELLS FROM THE AVIAN SALT-GLAND |
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