Phosphorylation of B‐50 Protein by Calcium‐Activated, Phospholipid‐Dependent Protein Kinase and B‐50 Protein Kinase
: B‐50 is a brain‐specific phosphoprotein, the phosphorylation state of which may play a role in the regulation of (poly)phosphoinositide metabolism. Several kinases were tested for their ability to phosphorylate purified B‐50 protein. Only calcium‐activated, phospholipid‐dependent protein kinase (k...
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| Veröffentlicht in: | Journal of neurochemistry 1983-01, Vol.41 (3), p.649-653 |
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| container_title | Journal of neurochemistry |
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| creator | Aloyo, Vincent J. Zwiers, Henk Gispen, Willem Hendrik |
| description | : B‐50 is a brain‐specific phosphoprotein, the phosphorylation state of which may play a role in the regulation of (poly)phosphoinositide metabolism. Several kinases were tested for their ability to phosphorylate purified B‐50 protein. Only calcium‐activated, phospholipid‐dependent protein kinase (kinase C) and B‐50 protein kinase were able to use B‐50 protein as a substrate. Furthermore, kinase C specifically phosphorylates B‐50 when added to synaptic plasma membranes. We further characterized the sensitivity of kinase C and B‐50 kinase to ACTH (and various fragments), phospholipids, chlorpromazine, and proteolytic activation. Since the sensitivities of both kinases were similar, we conclude that B‐50 protein kinase is a calcium‐dependent, phospholipidstimulated protein kinase of the same type as kinase C. |
| doi_str_mv | 10.1111/j.1471-4159.1983.tb04790.x |
| format | Article |
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Several kinases were tested for their ability to phosphorylate purified B‐50 protein. Only calcium‐activated, phospholipid‐dependent protein kinase (kinase C) and B‐50 protein kinase were able to use B‐50 protein as a substrate. Furthermore, kinase C specifically phosphorylates B‐50 when added to synaptic plasma membranes. We further characterized the sensitivity of kinase C and B‐50 kinase to ACTH (and various fragments), phospholipids, chlorpromazine, and proteolytic activation. Since the sensitivities of both kinases were similar, we conclude that B‐50 protein kinase is a calcium‐dependent, phospholipidstimulated protein kinase of the same type as kinase C.</description><identifier>ISSN: 0022-3042</identifier><identifier>EISSN: 1471-4159</identifier><identifier>DOI: 10.1111/j.1471-4159.1983.tb04790.x</identifier><identifier>PMID: 6308167</identifier><identifier>CODEN: JONRA9</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>ACTH ; Adrenocorticotropic Hormone - pharmacology ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Calcium - pharmacology ; Chlorpromazine ; Enzymes and enzyme inhibitors ; Female ; Fundamental and applied biological sciences. Psychology ; GAP-43 Protein ; Kinase C ; Molecular Weight ; Phospholipids ; Phospholipids - metabolism ; Phosphoprotein B‐50 ; Phosphoproteins - metabolism ; Phosphorylation ; protein kinase ; Protein Kinases - metabolism ; Rats ; Rats, Inbred Strains ; synaptic membranes ; Transferases</subject><ispartof>Journal of neurochemistry, 1983-01, Vol.41 (3), p.649-653</ispartof><rights>1984 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5129-4616288fe665c1def08f92bbc6b1dd653eb6dc1555cddb1e73b1b0f64b0181833</citedby><cites>FETCH-LOGICAL-c5129-4616288fe665c1def08f92bbc6b1dd653eb6dc1555cddb1e73b1b0f64b0181833</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1471-4159.1983.tb04790.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1471-4159.1983.tb04790.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27903,27904,45553,45554</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=9380969$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6308167$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Aloyo, Vincent J.</creatorcontrib><creatorcontrib>Zwiers, Henk</creatorcontrib><creatorcontrib>Gispen, Willem Hendrik</creatorcontrib><title>Phosphorylation of B‐50 Protein by Calcium‐Activated, Phospholipid‐Dependent Protein Kinase and B‐50 Protein Kinase</title><title>Journal of neurochemistry</title><addtitle>J Neurochem</addtitle><description>: B‐50 is a brain‐specific phosphoprotein, the phosphorylation state of which may play a role in the regulation of (poly)phosphoinositide metabolism. Several kinases were tested for their ability to phosphorylate purified B‐50 protein. Only calcium‐activated, phospholipid‐dependent protein kinase (kinase C) and B‐50 protein kinase were able to use B‐50 protein as a substrate. Furthermore, kinase C specifically phosphorylates B‐50 when added to synaptic plasma membranes. We further characterized the sensitivity of kinase C and B‐50 kinase to ACTH (and various fragments), phospholipids, chlorpromazine, and proteolytic activation. Since the sensitivities of both kinases were similar, we conclude that B‐50 protein kinase is a calcium‐dependent, phospholipidstimulated protein kinase of the same type as kinase C.</description><subject>ACTH</subject><subject>Adrenocorticotropic Hormone - pharmacology</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Calcium - pharmacology</subject><subject>Chlorpromazine</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GAP-43 Protein</subject><subject>Kinase C</subject><subject>Molecular Weight</subject><subject>Phospholipids</subject><subject>Phospholipids - metabolism</subject><subject>Phosphoprotein B‐50</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation</subject><subject>protein kinase</subject><subject>Protein Kinases - metabolism</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>synaptic membranes</subject><subject>Transferases</subject><issn>0022-3042</issn><issn>1471-4159</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkctu1DAUhi0EKtPCIyBFCHXVhHPiy9gskNoByqWCLmBt-RbVo0wS4gx0xIZH4Bl5kiaaaBZsAG8s-b_4lz5CniIUOJ7n6wLZEnOGXBWoJC0GC2ypoLi9RxYH6T5ZAJRlToGVD8lxSmsAFEzgETkSFCSK5YL8uL5pU3fT9rvaDLFtsrbKLn7__MUhu-7bIcQms7tsZWoXt5vx_dwN8ZsZgj_L5mQdu-hH5VXoQuNDMxyCH2JjUshM4_-s3CuPyIPK1Ck8nu8T8uXN68-rt_nVp8t3q_Or3HEsVT4uFqWUVRCCO_ShAlmp0lonLHovOA1WeIecc-e9xbCkFi1UgllAiZLSE3K67-369us2pEFvYnKhrk0T2m3SErjknLG_GpEqBFDqH4xibMSp8cXe6Po2pT5UuuvjxvQ7jaAnlnqtJ2B6AqYnlnpmqW_H8JP5l63dBH-IzvBG_dmsm-RMXfWmcTEdbIpKUGIa-3Jv-x7rsPuPAfr9x5Vgit4Broy_Mg</recordid><startdate>19830101</startdate><enddate>19830101</enddate><creator>Aloyo, Vincent J.</creator><creator>Zwiers, Henk</creator><creator>Gispen, Willem Hendrik</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</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>7QL</scope><scope>7TK</scope><scope>C1K</scope><scope>7QP</scope><scope>7X8</scope></search><sort><creationdate>19830101</creationdate><title>Phosphorylation of B‐50 Protein by Calcium‐Activated, Phospholipid‐Dependent Protein Kinase and B‐50 Protein Kinase</title><author>Aloyo, Vincent J. ; Zwiers, Henk ; Gispen, Willem Hendrik</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5129-4616288fe665c1def08f92bbc6b1dd653eb6dc1555cddb1e73b1b0f64b0181833</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>ACTH</topic><topic>Adrenocorticotropic Hormone - pharmacology</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Calcium - pharmacology</topic><topic>Chlorpromazine</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GAP-43 Protein</topic><topic>Kinase C</topic><topic>Molecular Weight</topic><topic>Phospholipids</topic><topic>Phospholipids - metabolism</topic><topic>Phosphoprotein B‐50</topic><topic>Phosphoproteins - metabolism</topic><topic>Phosphorylation</topic><topic>protein kinase</topic><topic>Protein Kinases - metabolism</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>synaptic membranes</topic><topic>Transferases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Aloyo, Vincent J.</creatorcontrib><creatorcontrib>Zwiers, Henk</creatorcontrib><creatorcontrib>Gispen, Willem Hendrik</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Neurosciences Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of neurochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Aloyo, Vincent J.</au><au>Zwiers, Henk</au><au>Gispen, Willem Hendrik</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphorylation of B‐50 Protein by Calcium‐Activated, Phospholipid‐Dependent Protein Kinase and B‐50 Protein Kinase</atitle><jtitle>Journal of neurochemistry</jtitle><addtitle>J Neurochem</addtitle><date>1983-01-01</date><risdate>1983</risdate><volume>41</volume><issue>3</issue><spage>649</spage><epage>653</epage><pages>649-653</pages><issn>0022-3042</issn><eissn>1471-4159</eissn><coden>JONRA9</coden><abstract>: B‐50 is a brain‐specific phosphoprotein, the phosphorylation state of which may play a role in the regulation of (poly)phosphoinositide metabolism. Several kinases were tested for their ability to phosphorylate purified B‐50 protein. Only calcium‐activated, phospholipid‐dependent protein kinase (kinase C) and B‐50 protein kinase were able to use B‐50 protein as a substrate. Furthermore, kinase C specifically phosphorylates B‐50 when added to synaptic plasma membranes. We further characterized the sensitivity of kinase C and B‐50 kinase to ACTH (and various fragments), phospholipids, chlorpromazine, and proteolytic activation. Since the sensitivities of both kinases were similar, we conclude that B‐50 protein kinase is a calcium‐dependent, phospholipidstimulated protein kinase of the same type as kinase C.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>6308167</pmid><doi>10.1111/j.1471-4159.1983.tb04790.x</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0022-3042 |
| ispartof | Journal of neurochemistry, 1983-01, Vol.41 (3), p.649-653 |
| issn | 0022-3042 1471-4159 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | ACTH Adrenocorticotropic Hormone - pharmacology Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Calcium - pharmacology Chlorpromazine Enzymes and enzyme inhibitors Female Fundamental and applied biological sciences. Psychology GAP-43 Protein Kinase C Molecular Weight Phospholipids Phospholipids - metabolism Phosphoprotein B‐50 Phosphoproteins - metabolism Phosphorylation protein kinase Protein Kinases - metabolism Rats Rats, Inbred Strains synaptic membranes Transferases |
| title | Phosphorylation of B‐50 Protein by Calcium‐Activated, Phospholipid‐Dependent Protein Kinase and B‐50 Protein Kinase |
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