Stimulation of protein phosphorylations in frog rod outer segments by protein kinase activators. Suppression of light-induced changes in membrane current and cGMP by protein kinase C activators

Addition of protein kinase C activators to electropermeabilized frog rod photoreceptors enhances the phosphorylation of proteins with molecular masses of 54, 24, 19, 17, 12, and 11 kDa. The latter two correspond to components I and II, which are also phosphorylated by cyclic nucleotide-dependent pro...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:The Journal of biological chemistry 1989-05, Vol.264 (15), p.8857-8864
Hauptverfasser: BINDER, B. M, BREWER, E, BOWNDS, M. D
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 8864
container_issue 15
container_start_page 8857
container_title The Journal of biological chemistry
container_volume 264
creator BINDER, B. M
BREWER, E
BOWNDS, M. D
description Addition of protein kinase C activators to electropermeabilized frog rod photoreceptors enhances the phosphorylation of proteins with molecular masses of 54, 24, 19, 17, 12, and 11 kDa. The latter two correspond to components I and II, which are also phosphorylated by cyclic nucleotide-dependent protein kinase. Stimulation of phosphorylation by the protein kinase C activator oleoylacetylglycerol (OAG) is half-maximal at 7.7 microM OAG and is reduced by the protein kinase C inhibitor H-7. In contrast with earlier observations, no effects of calcium, calmodulin, or insulin on protein phosphorylations are observed. We find evidence for only three protein kinases in rod outer segments: a protein kinase C-like activity, cAMP-dependent protein kinase, and rhodopsin kinase. With the exception of components I and II, the substrate proteins for each kinase are distinct. Treatment of intact rods with OAG decreases the amplitude of the photoresponse and dark levels of cGMP up to 40%, as well as depressing the light-stimulated decrease in cGMP levels. These effects are observed between 0.1 and 1 microM OAG. The data suggest that OAG-sensitive reactions may modulate pathways that support the light response.
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_15308141</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>15308141</sourcerecordid><originalsourceid>FETCH-LOGICAL-h294t-8c8e071e23c1ab76b781730cd5ef3b8d2a24d3b62444808c5c9ccfcae4f423363</originalsourceid><addsrcrecordid>eNptkN9KwzAUxosoc04fQQgo3lXyr2t6KUOnMFGYgnclTU_XaNvUJFX2eL6ZwRXxwsAhkO93vu_k7EVTggWLWUJe9qMpxpTEGU3EYXTk3CsOh2dkEk1owinN2DT6WnvdDo302nTIVKi3xoPuUF8bF8pud5JD4a2yZoOsKZEZPFjkYNNC5x0qtr9tb7qTDpBUXn9Ib6y7ROuh7y04NwY0elP7WHfloKBEqpbdBn7cW2gLKztAarA2-CLZBX15__iP_-JPwnF0UMnGwcl4z6Lnm-unxW28eljeLa5WcU0z7mOhBOCUAGWKyCKdF6kgKcOqTKBihSippLxkxZxyzgUWKlGZUpWSwCtOGZuzWXSx8w2zvA_gfN5qp6BpwsxmcDlJGBaEkwCejuBQtFDmvdWttNt83HnQz0ddOiWbKnxaafeLpYxQgZOAne2wOmzsU1vIC21UDW1O5zyk5UIkKfsGDLScOA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15308141</pqid></control><display><type>article</type><title>Stimulation of protein phosphorylations in frog rod outer segments by protein kinase activators. Suppression of light-induced changes in membrane current and cGMP by protein kinase C activators</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>BINDER, B. M ; BREWER, E ; BOWNDS, M. D</creator><creatorcontrib>BINDER, B. M ; BREWER, E ; BOWNDS, M. D</creatorcontrib><description>Addition of protein kinase C activators to electropermeabilized frog rod photoreceptors enhances the phosphorylation of proteins with molecular masses of 54, 24, 19, 17, 12, and 11 kDa. The latter two correspond to components I and II, which are also phosphorylated by cyclic nucleotide-dependent protein kinase. Stimulation of phosphorylation by the protein kinase C activator oleoylacetylglycerol (OAG) is half-maximal at 7.7 microM OAG and is reduced by the protein kinase C inhibitor H-7. In contrast with earlier observations, no effects of calcium, calmodulin, or insulin on protein phosphorylations are observed. We find evidence for only three protein kinases in rod outer segments: a protein kinase C-like activity, cAMP-dependent protein kinase, and rhodopsin kinase. With the exception of components I and II, the substrate proteins for each kinase are distinct. Treatment of intact rods with OAG decreases the amplitude of the photoresponse and dark levels of cGMP up to 40%, as well as depressing the light-stimulated decrease in cGMP levels. These effects are observed between 0.1 and 1 microM OAG. The data suggest that OAG-sensitive reactions may modulate pathways that support the light response.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>PMID: 2542293</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>8-Bromo Cyclic Adenosine Monophosphate - pharmacology ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Cell Membrane - physiology ; Cyclic GMP - analogs &amp; derivatives ; Cyclic GMP - metabolism ; Cyclic GMP - pharmacology ; Diglycerides - pharmacology ; Enzyme Activation ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Glycerides - pharmacology ; Kinetics ; Light ; Membrane Potentials ; Molecular Weight ; Oleic Acid ; Oleic Acids - pharmacology ; Phosphoproteins - isolation &amp; purification ; Phosphorylation ; Photoreceptor Cells - metabolism ; photoreceptors ; protein kinase ; protein kinase C ; Protein Kinase C - metabolism ; Protein Kinases - metabolism ; Proteins - metabolism ; Rana catesbeiana ; rhodopsin kinase ; Rod Cell Outer Segment - metabolism ; Tetradecanoylphorbol Acetate - pharmacology ; Transferases</subject><ispartof>The Journal of biological chemistry, 1989-05, Vol.264 (15), p.8857-8864</ispartof><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=7312805$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2542293$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>BINDER, B. M</creatorcontrib><creatorcontrib>BREWER, E</creatorcontrib><creatorcontrib>BOWNDS, M. D</creatorcontrib><title>Stimulation of protein phosphorylations in frog rod outer segments by protein kinase activators. Suppression of light-induced changes in membrane current and cGMP by protein kinase C activators</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Addition of protein kinase C activators to electropermeabilized frog rod photoreceptors enhances the phosphorylation of proteins with molecular masses of 54, 24, 19, 17, 12, and 11 kDa. The latter two correspond to components I and II, which are also phosphorylated by cyclic nucleotide-dependent protein kinase. Stimulation of phosphorylation by the protein kinase C activator oleoylacetylglycerol (OAG) is half-maximal at 7.7 microM OAG and is reduced by the protein kinase C inhibitor H-7. In contrast with earlier observations, no effects of calcium, calmodulin, or insulin on protein phosphorylations are observed. We find evidence for only three protein kinases in rod outer segments: a protein kinase C-like activity, cAMP-dependent protein kinase, and rhodopsin kinase. With the exception of components I and II, the substrate proteins for each kinase are distinct. Treatment of intact rods with OAG decreases the amplitude of the photoresponse and dark levels of cGMP up to 40%, as well as depressing the light-stimulated decrease in cGMP levels. These effects are observed between 0.1 and 1 microM OAG. The data suggest that OAG-sensitive reactions may modulate pathways that support the light response.</description><subject>8-Bromo Cyclic Adenosine Monophosphate - pharmacology</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cell Membrane - physiology</subject><subject>Cyclic GMP - analogs &amp; derivatives</subject><subject>Cyclic GMP - metabolism</subject><subject>Cyclic GMP - pharmacology</subject><subject>Diglycerides - pharmacology</subject><subject>Enzyme Activation</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycerides - pharmacology</subject><subject>Kinetics</subject><subject>Light</subject><subject>Membrane Potentials</subject><subject>Molecular Weight</subject><subject>Oleic Acid</subject><subject>Oleic Acids - pharmacology</subject><subject>Phosphoproteins - isolation &amp; purification</subject><subject>Phosphorylation</subject><subject>Photoreceptor Cells - metabolism</subject><subject>photoreceptors</subject><subject>protein kinase</subject><subject>protein kinase C</subject><subject>Protein Kinase C - metabolism</subject><subject>Protein Kinases - metabolism</subject><subject>Proteins - metabolism</subject><subject>Rana catesbeiana</subject><subject>rhodopsin kinase</subject><subject>Rod Cell Outer Segment - metabolism</subject><subject>Tetradecanoylphorbol Acetate - pharmacology</subject><subject>Transferases</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkN9KwzAUxosoc04fQQgo3lXyr2t6KUOnMFGYgnclTU_XaNvUJFX2eL6ZwRXxwsAhkO93vu_k7EVTggWLWUJe9qMpxpTEGU3EYXTk3CsOh2dkEk1owinN2DT6WnvdDo302nTIVKi3xoPuUF8bF8pud5JD4a2yZoOsKZEZPFjkYNNC5x0qtr9tb7qTDpBUXn9Ib6y7ROuh7y04NwY0elP7WHfloKBEqpbdBn7cW2gLKztAarA2-CLZBX15__iP_-JPwnF0UMnGwcl4z6Lnm-unxW28eljeLa5WcU0z7mOhBOCUAGWKyCKdF6kgKcOqTKBihSippLxkxZxyzgUWKlGZUpWSwCtOGZuzWXSx8w2zvA_gfN5qp6BpwsxmcDlJGBaEkwCejuBQtFDmvdWttNt83HnQz0ddOiWbKnxaafeLpYxQgZOAne2wOmzsU1vIC21UDW1O5zyk5UIkKfsGDLScOA</recordid><startdate>19890525</startdate><enddate>19890525</enddate><creator>BINDER, B. M</creator><creator>BREWER, E</creator><creator>BOWNDS, M. D</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope></search><sort><creationdate>19890525</creationdate><title>Stimulation of protein phosphorylations in frog rod outer segments by protein kinase activators. Suppression of light-induced changes in membrane current and cGMP by protein kinase C activators</title><author>BINDER, B. M ; BREWER, E ; BOWNDS, M. D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h294t-8c8e071e23c1ab76b781730cd5ef3b8d2a24d3b62444808c5c9ccfcae4f423363</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>8-Bromo Cyclic Adenosine Monophosphate - pharmacology</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cell Membrane - physiology</topic><topic>Cyclic GMP - analogs &amp; derivatives</topic><topic>Cyclic GMP - metabolism</topic><topic>Cyclic GMP - pharmacology</topic><topic>Diglycerides - pharmacology</topic><topic>Enzyme Activation</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycerides - pharmacology</topic><topic>Kinetics</topic><topic>Light</topic><topic>Membrane Potentials</topic><topic>Molecular Weight</topic><topic>Oleic Acid</topic><topic>Oleic Acids - pharmacology</topic><topic>Phosphoproteins - isolation &amp; purification</topic><topic>Phosphorylation</topic><topic>Photoreceptor Cells - metabolism</topic><topic>photoreceptors</topic><topic>protein kinase</topic><topic>protein kinase C</topic><topic>Protein Kinase C - metabolism</topic><topic>Protein Kinases - metabolism</topic><topic>Proteins - metabolism</topic><topic>Rana catesbeiana</topic><topic>rhodopsin kinase</topic><topic>Rod Cell Outer Segment - metabolism</topic><topic>Tetradecanoylphorbol Acetate - pharmacology</topic><topic>Transferases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>BINDER, B. M</creatorcontrib><creatorcontrib>BREWER, E</creatorcontrib><creatorcontrib>BOWNDS, M. D</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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>BINDER, B. M</au><au>BREWER, E</au><au>BOWNDS, M. D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Stimulation of protein phosphorylations in frog rod outer segments by protein kinase activators. Suppression of light-induced changes in membrane current and cGMP by protein kinase C activators</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1989-05-25</date><risdate>1989</risdate><volume>264</volume><issue>15</issue><spage>8857</spage><epage>8864</epage><pages>8857-8864</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Addition of protein kinase C activators to electropermeabilized frog rod photoreceptors enhances the phosphorylation of proteins with molecular masses of 54, 24, 19, 17, 12, and 11 kDa. The latter two correspond to components I and II, which are also phosphorylated by cyclic nucleotide-dependent protein kinase. Stimulation of phosphorylation by the protein kinase C activator oleoylacetylglycerol (OAG) is half-maximal at 7.7 microM OAG and is reduced by the protein kinase C inhibitor H-7. In contrast with earlier observations, no effects of calcium, calmodulin, or insulin on protein phosphorylations are observed. We find evidence for only three protein kinases in rod outer segments: a protein kinase C-like activity, cAMP-dependent protein kinase, and rhodopsin kinase. With the exception of components I and II, the substrate proteins for each kinase are distinct. Treatment of intact rods with OAG decreases the amplitude of the photoresponse and dark levels of cGMP up to 40%, as well as depressing the light-stimulated decrease in cGMP levels. These effects are observed between 0.1 and 1 microM OAG. The data suggest that OAG-sensitive reactions may modulate pathways that support the light response.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>2542293</pmid><tpages>8</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0021-9258
ispartof The Journal of biological chemistry, 1989-05, Vol.264 (15), p.8857-8864
issn 0021-9258
1083-351X
language eng
recordid cdi_proquest_miscellaneous_15308141
source MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection
subjects 8-Bromo Cyclic Adenosine Monophosphate - pharmacology
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Cell Membrane - physiology
Cyclic GMP - analogs & derivatives
Cyclic GMP - metabolism
Cyclic GMP - pharmacology
Diglycerides - pharmacology
Enzyme Activation
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Glycerides - pharmacology
Kinetics
Light
Membrane Potentials
Molecular Weight
Oleic Acid
Oleic Acids - pharmacology
Phosphoproteins - isolation & purification
Phosphorylation
Photoreceptor Cells - metabolism
photoreceptors
protein kinase
protein kinase C
Protein Kinase C - metabolism
Protein Kinases - metabolism
Proteins - metabolism
Rana catesbeiana
rhodopsin kinase
Rod Cell Outer Segment - metabolism
Tetradecanoylphorbol Acetate - pharmacology
Transferases
title Stimulation of protein phosphorylations in frog rod outer segments by protein kinase activators. Suppression of light-induced changes in membrane current and cGMP by protein kinase C activators
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-16T15%3A32%3A10IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Stimulation%20of%20protein%20phosphorylations%20in%20frog%20rod%20outer%20segments%20by%20protein%20kinase%20activators.%20Suppression%20of%20light-induced%20changes%20in%20membrane%20current%20and%20cGMP%20by%20protein%20kinase%20C%20activators&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=BINDER,%20B.%20M&rft.date=1989-05-25&rft.volume=264&rft.issue=15&rft.spage=8857&rft.epage=8864&rft.pages=8857-8864&rft.issn=0021-9258&rft.eissn=1083-351X&rft.coden=JBCHA3&rft_id=info:doi/&rft_dat=%3Cproquest_pubme%3E15308141%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=15308141&rft_id=info:pmid/2542293&rfr_iscdi=true