Phosphorylation of Tyrosine Hydroxylase by Cyclic GMP‐Dependent Protein Kinase
: Tyrosine hydroxylase purified from rat pheochro‐mocytoma was phosphorylated and activated by purified cyclic GMP‐dependent protein kinase as well as by cyclic AMP‐dependent protein kinase catalytic subunit. The extent of activation was correlated with the degree of phosphate incorporated into the...
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| Veröffentlicht in: | Journal of neurochemistry 1987-03, Vol.48 (3), p.840-845 |
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| container_title | Journal of neurochemistry |
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| creator | Roskoski, Robert Vulliet, P. Richard Glass, David B. |
| description | : Tyrosine hydroxylase purified from rat pheochro‐mocytoma was phosphorylated and activated by purified cyclic GMP‐dependent protein kinase as well as by cyclic AMP‐dependent protein kinase catalytic subunit. The extent of activation was correlated with the degree of phosphate incorporated into the enzyme. Comparable stoichio‐metric ratios (0.6 mol phosphate/mol tyrosine hydroxylase subunit) were obtained at maximal concentrations of either cyclic AMP‐dependent or cyclic GMP‐dependent protein kinases. The enzymes appeared to mediate the phosphorylation of the same residue based on the observation that incorporation was not increased when both enzymes were present. The major tryptic phosphopeptide obtained from tyrosine hydroxylase phosphorylated by each protein kinase exhibited an identical retention time following HPLC. The purified phosphopeptides also exhibited identical isoelectric points. These data provide support for the notion that the protein kinases are phosphorylating the same residue of tyrosine hydroxylase. |
| doi_str_mv | 10.1111/j.1471-4159.1987.tb05593.x |
| format | Article |
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Richard ; Glass, David B.</creator><creatorcontrib>Roskoski, Robert ; Vulliet, P. Richard ; Glass, David B.</creatorcontrib><description>: Tyrosine hydroxylase purified from rat pheochro‐mocytoma was phosphorylated and activated by purified cyclic GMP‐dependent protein kinase as well as by cyclic AMP‐dependent protein kinase catalytic subunit. The extent of activation was correlated with the degree of phosphate incorporated into the enzyme. Comparable stoichio‐metric ratios (0.6 mol phosphate/mol tyrosine hydroxylase subunit) were obtained at maximal concentrations of either cyclic AMP‐dependent or cyclic GMP‐dependent protein kinases. The enzymes appeared to mediate the phosphorylation of the same residue based on the observation that incorporation was not increased when both enzymes were present. The major tryptic phosphopeptide obtained from tyrosine hydroxylase phosphorylated by each protein kinase exhibited an identical retention time following HPLC. The purified phosphopeptides also exhibited identical isoelectric points. These data provide support for the notion that the protein kinases are phosphorylating the same residue of tyrosine hydroxylase.</description><identifier>ISSN: 0022-3042</identifier><identifier>EISSN: 1471-4159</identifier><identifier>DOI: 10.1111/j.1471-4159.1987.tb05593.x</identifier><identifier>PMID: 2879892</identifier><identifier>CODEN: JONRA9</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Cell Line ; Chromatography, High Pressure Liquid ; Cyclic AMP - pharmacology ; Cyclic AMP‐dependent protein kinase ; Cyclic GMP - pharmacology ; Cyclic GMP‐dependent protein kinase ; Enzyme Activation - drug effects ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Isoelectric Point ; Oxidoreductases ; Peptide Fragments ; Pheochromocytoma - enzymology ; Phosphorylation ; Protein Kinases - metabolism ; Pterins - pharmacology ; Rat pheo‐chromocytoma ; Rats ; Trypsin - metabolism ; Tyrosine 3-Monooxygenase - metabolism ; Tyrosine hydroxylase</subject><ispartof>Journal of neurochemistry, 1987-03, Vol.48 (3), p.840-845</ispartof><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4950-3b9a3725137561be243e2de2b81080adff75d12bd64622b153ed26d3657ef7a23</citedby><cites>FETCH-LOGICAL-c4950-3b9a3725137561be243e2de2b81080adff75d12bd64622b153ed26d3657ef7a23</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.1471-4159.1987.tb05593.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1471-4159.1987.tb05593.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8271885$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2879892$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Roskoski, Robert</creatorcontrib><creatorcontrib>Vulliet, P. Richard</creatorcontrib><creatorcontrib>Glass, David B.</creatorcontrib><title>Phosphorylation of Tyrosine Hydroxylase by Cyclic GMP‐Dependent Protein Kinase</title><title>Journal of neurochemistry</title><addtitle>J Neurochem</addtitle><description>: Tyrosine hydroxylase purified from rat pheochro‐mocytoma was phosphorylated and activated by purified cyclic GMP‐dependent protein kinase as well as by cyclic AMP‐dependent protein kinase catalytic subunit. The extent of activation was correlated with the degree of phosphate incorporated into the enzyme. Comparable stoichio‐metric ratios (0.6 mol phosphate/mol tyrosine hydroxylase subunit) were obtained at maximal concentrations of either cyclic AMP‐dependent or cyclic GMP‐dependent protein kinases. The enzymes appeared to mediate the phosphorylation of the same residue based on the observation that incorporation was not increased when both enzymes were present. The major tryptic phosphopeptide obtained from tyrosine hydroxylase phosphorylated by each protein kinase exhibited an identical retention time following HPLC. The purified phosphopeptides also exhibited identical isoelectric points. These data provide support for the notion that the protein kinases are phosphorylating the same residue of tyrosine hydroxylase.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cell Line</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Cyclic AMP - pharmacology</subject><subject>Cyclic AMP‐dependent protein kinase</subject><subject>Cyclic GMP - pharmacology</subject><subject>Cyclic GMP‐dependent protein kinase</subject><subject>Enzyme Activation - drug effects</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Isoelectric Point</subject><subject>Oxidoreductases</subject><subject>Peptide Fragments</subject><subject>Pheochromocytoma - enzymology</subject><subject>Phosphorylation</subject><subject>Protein Kinases - metabolism</subject><subject>Pterins - pharmacology</subject><subject>Rat pheo‐chromocytoma</subject><subject>Rats</subject><subject>Trypsin - metabolism</subject><subject>Tyrosine 3-Monooxygenase - metabolism</subject><subject>Tyrosine hydroxylase</subject><issn>0022-3042</issn><issn>1471-4159</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkM9O3DAQh60KBFvaR0CKEOotqf_GDgekattCKW33QM-WE0-EV9l4sbPq5tZH4Bn7JPVqo70ifJnD75vxzIfQBcEFSe_jsiBckpwTURWkUrIYaixExYrtGzQ7REdohjGlOcOcnqK3MS4xJiUvyQk6oUpWqqIztFg8-rh-9GHszOB8n_k2exiDj66H7Ha0wW9TEiGrx2w-Np1rspsfi39_nz_DGnoL_ZAtgh_A9dl31yfwHTpuTRfh_VTP0O-vXx7mt_n9r5tv80_3ecMrgXNWV4ZJKgiToiQ1UM6AWqC1IlhhY9tWCktobdPClNZEMLC0tKwUElppKDtDH_Zz18E_bSAOeuViA11nevCbqKVkijLyMkh4yblQOIFXe7BJ58cArV4HtzJh1ATrnXe91Du5eidX77zrybvepubz6ZdNvQJ7aJ1Ep_xyyk1sTNcG0zcuHjBFJVFKJOx6j_1xHYyvWEDf_Zwrjtl_3bef1w</recordid><startdate>198703</startdate><enddate>198703</enddate><creator>Roskoski, Robert</creator><creator>Vulliet, P. Richard</creator><creator>Glass, David B.</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>7TK</scope><scope>7X8</scope></search><sort><creationdate>198703</creationdate><title>Phosphorylation of Tyrosine Hydroxylase by Cyclic GMP‐Dependent Protein Kinase</title><author>Roskoski, Robert ; Vulliet, P. Richard ; Glass, David B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4950-3b9a3725137561be243e2de2b81080adff75d12bd64622b153ed26d3657ef7a23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cell Line</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Cyclic AMP - pharmacology</topic><topic>Cyclic AMP‐dependent protein kinase</topic><topic>Cyclic GMP - pharmacology</topic><topic>Cyclic GMP‐dependent protein kinase</topic><topic>Enzyme Activation - drug effects</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Isoelectric Point</topic><topic>Oxidoreductases</topic><topic>Peptide Fragments</topic><topic>Pheochromocytoma - enzymology</topic><topic>Phosphorylation</topic><topic>Protein Kinases - metabolism</topic><topic>Pterins - pharmacology</topic><topic>Rat pheo‐chromocytoma</topic><topic>Rats</topic><topic>Trypsin - metabolism</topic><topic>Tyrosine 3-Monooxygenase - metabolism</topic><topic>Tyrosine hydroxylase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Roskoski, Robert</creatorcontrib><creatorcontrib>Vulliet, P. Richard</creatorcontrib><creatorcontrib>Glass, David B.</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>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of neurochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Roskoski, Robert</au><au>Vulliet, P. Richard</au><au>Glass, David B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphorylation of Tyrosine Hydroxylase by Cyclic GMP‐Dependent Protein Kinase</atitle><jtitle>Journal of neurochemistry</jtitle><addtitle>J Neurochem</addtitle><date>1987-03</date><risdate>1987</risdate><volume>48</volume><issue>3</issue><spage>840</spage><epage>845</epage><pages>840-845</pages><issn>0022-3042</issn><eissn>1471-4159</eissn><coden>JONRA9</coden><abstract>: Tyrosine hydroxylase purified from rat pheochro‐mocytoma was phosphorylated and activated by purified cyclic GMP‐dependent protein kinase as well as by cyclic AMP‐dependent protein kinase catalytic subunit. The extent of activation was correlated with the degree of phosphate incorporated into the enzyme. Comparable stoichio‐metric ratios (0.6 mol phosphate/mol tyrosine hydroxylase subunit) were obtained at maximal concentrations of either cyclic AMP‐dependent or cyclic GMP‐dependent protein kinases. The enzymes appeared to mediate the phosphorylation of the same residue based on the observation that incorporation was not increased when both enzymes were present. The major tryptic phosphopeptide obtained from tyrosine hydroxylase phosphorylated by each protein kinase exhibited an identical retention time following HPLC. The purified phosphopeptides also exhibited identical isoelectric points. These data provide support for the notion that the protein kinases are phosphorylating the same residue of tyrosine hydroxylase.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>2879892</pmid><doi>10.1111/j.1471-4159.1987.tb05593.x</doi><tpages>6</tpages></addata></record> |
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| ispartof | Journal of neurochemistry, 1987-03, Vol.48 (3), p.840-845 |
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| language | eng |
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| source | MEDLINE; Access via Wiley Online Library |
| subjects | Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cell Line Chromatography, High Pressure Liquid Cyclic AMP - pharmacology Cyclic AMP‐dependent protein kinase Cyclic GMP - pharmacology Cyclic GMP‐dependent protein kinase Enzyme Activation - drug effects Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Isoelectric Point Oxidoreductases Peptide Fragments Pheochromocytoma - enzymology Phosphorylation Protein Kinases - metabolism Pterins - pharmacology Rat pheo‐chromocytoma Rats Trypsin - metabolism Tyrosine 3-Monooxygenase - metabolism Tyrosine hydroxylase |
| title | Phosphorylation of Tyrosine Hydroxylase by Cyclic GMP‐Dependent Protein Kinase |
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