Regulation of Cyclic Nucleotide Concentrations in Photoreceptors: An ATP-Dependent Stimulation of Cyclic Nucleotide Phosphodiesterase by Light
Regulation of cyclic nucleotide concentrations in rod outer segments (Rana pipiens) has been further examined. The present studies show that illumination markedly diminishes the concentration of cyclic nucleotides in suspensions of photoreceptor membranes, but the locus of regulation is cyclic nucle...
Gespeichert in:
Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1973-12, Vol.70 (12), p.3820-3824 |
---|---|
Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 3824 |
---|---|
container_issue | 12 |
container_start_page | 3820 |
container_title | Proceedings of the National Academy of Sciences - PNAS |
container_volume | 70 |
creator | Miki, Naomasa Keirns, James J. Marcus, Frederick R. Freeman, Jenny Bitensky, Mark W. |
description | Regulation of cyclic nucleotide concentrations in rod outer segments (Rana pipiens) has been further examined. The present studies show that illumination markedly diminishes the concentration of cyclic nucleotides in suspensions of photoreceptor membranes, but the locus of regulation is cyclic nucleotide phosphodiesterase (EC 3.1.4.c) (light-stimulated) and not adenylate cyclase. There is a marked disproportionality between bleaching of rhodopsin and stimulation of phosphodiesterase. Bleaching only 0.6% of the rhodopsin produces half the stimulation produced by bleaching 100% of the rhodopsin. The process of activation of phosphodiesterase by light is in two steps, a light-dependent step followed by an ATP-dependent step. Illumination (in the absence of ATP) produces a trypsin-resistant, heat-labile, macromolecular stimulator. In the presence of 0.75 mM ATP (GTP or ITP) this stimulator produces a greater than 5-fold increase in the Vmaxof photoreceptor phosphodiesterase without changing the Km. At physiological substrate concentrations (10-7M) the rate of hydrolysis of cyclic GMP is 23 times greater than that of cyclic AMP. The light-produced stimulator appears unique to the photoreceptor membranes and does not activate phosphodiesterase in other tissues. |
doi_str_mv | 10.1073/pnas.70.12.3820 |
format | Article |
fullrecord | <record><control><sourceid>jstor_pubme</sourceid><recordid>TN_cdi_pubmed_primary_4359491</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>62657</jstor_id><sourcerecordid>62657</sourcerecordid><originalsourceid>FETCH-LOGICAL-c461t-26610c9b6009283b491956d838771742c9485c0d0b656629d1f0b81d07c7b81c3</originalsourceid><addsrcrecordid>eNp9kUtvEzEUhS0EKqGwRkICeQWrSf0aP5BYRCkvKYIKytqa8XgSV449jD2o-RP8ZhwSAmy6urq63zn20QHgKUZzjAS9GEKT5qIsZE4lQffADCOFK84Uug9mCBFRSUbYQ_AopRuEkKolOgNnjNaKKTwDP7_Y9eSb7GKAsYfLnfHOwE-T8TZm11m4jMHYkMffSIIuwKtNzHG0xg5lpNdwEeDi-qq6tIMNXUHh1-y2d3oWhzRsYudsynZskoXtDq7cepMfgwd945N9cpzn4Nu7t9fLD9Xq8_uPy8WqMozjXBHOMTKq5SUQkbQtUVTNO0mlEFgwYhSTtUEdannNOVEd7lErcYeEEWUaeg7eHHyHqd3a7pDQ62F022bc6dg4_f8luI1exx-aEUEpL_qXR_0Yv08lht66ZKz3TbBxSloSzBlHpIAXB9CMMaXR9qc3MNL7BvW-QS3KQvS-waJ4_u_XTvyxsnJ_dbzvhX-ufw10P3mf7W0u5Is7yQI8OwA3qVR5IjjhtaC_AO0xuso</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>82164602</pqid></control><display><type>article</type><title>Regulation of Cyclic Nucleotide Concentrations in Photoreceptors: An ATP-Dependent Stimulation of Cyclic Nucleotide Phosphodiesterase by Light</title><source>Jstor Complete Legacy</source><source>MEDLINE</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Miki, Naomasa ; Keirns, James J. ; Marcus, Frederick R. ; Freeman, Jenny ; Bitensky, Mark W.</creator><creatorcontrib>Miki, Naomasa ; Keirns, James J. ; Marcus, Frederick R. ; Freeman, Jenny ; Bitensky, Mark W.</creatorcontrib><description>Regulation of cyclic nucleotide concentrations in rod outer segments (Rana pipiens) has been further examined. The present studies show that illumination markedly diminishes the concentration of cyclic nucleotides in suspensions of photoreceptor membranes, but the locus of regulation is cyclic nucleotide phosphodiesterase (EC 3.1.4.c) (light-stimulated) and not adenylate cyclase. There is a marked disproportionality between bleaching of rhodopsin and stimulation of phosphodiesterase. Bleaching only 0.6% of the rhodopsin produces half the stimulation produced by bleaching 100% of the rhodopsin. The process of activation of phosphodiesterase by light is in two steps, a light-dependent step followed by an ATP-dependent step. Illumination (in the absence of ATP) produces a trypsin-resistant, heat-labile, macromolecular stimulator. In the presence of 0.75 mM ATP (GTP or ITP) this stimulator produces a greater than 5-fold increase in the Vmaxof photoreceptor phosphodiesterase without changing the Km. At physiological substrate concentrations (10-7M) the rate of hydrolysis of cyclic GMP is 23 times greater than that of cyclic AMP. The light-produced stimulator appears unique to the photoreceptor membranes and does not activate phosphodiesterase in other tissues.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.70.12.3820</identifier><identifier>PMID: 4359491</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Adenosine Triphosphate ; Adenylyl Cyclases - metabolism ; Animals ; Anura ; Biochemistry ; Biological Sciences: Biochemistry ; Bleaching ; Calcium ; Calcium - pharmacology ; Cell Fractionation ; Cell Membrane - enzymology ; Cyclic AMP - metabolism ; Cyclic GMP - metabolism ; Cyclic nucleotides ; Darkness ; Enzyme Activation ; Homogenization ; In Vitro Techniques ; Kinetics ; Light ; Mercuribenzoates - pharmacology ; Nuclear membrane ; P branes ; Phosphodiesterase Inhibitors ; Phosphoric Diester Hydrolases - metabolism ; Photoreceptor Cells - cytology ; Photoreceptor Cells - enzymology ; Photoreceptors ; Physiological regulation ; Protein Kinases - pharmacology ; Rana pipiens ; Receptors ; Time Factors</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1973-12, Vol.70 (12), p.3820-3824</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c461t-26610c9b6009283b491956d838771742c9485c0d0b656629d1f0b81d07c7b81c3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/70/12.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/62657$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/62657$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4359491$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Miki, Naomasa</creatorcontrib><creatorcontrib>Keirns, James J.</creatorcontrib><creatorcontrib>Marcus, Frederick R.</creatorcontrib><creatorcontrib>Freeman, Jenny</creatorcontrib><creatorcontrib>Bitensky, Mark W.</creatorcontrib><title>Regulation of Cyclic Nucleotide Concentrations in Photoreceptors: An ATP-Dependent Stimulation of Cyclic Nucleotide Phosphodiesterase by Light</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Regulation of cyclic nucleotide concentrations in rod outer segments (Rana pipiens) has been further examined. The present studies show that illumination markedly diminishes the concentration of cyclic nucleotides in suspensions of photoreceptor membranes, but the locus of regulation is cyclic nucleotide phosphodiesterase (EC 3.1.4.c) (light-stimulated) and not adenylate cyclase. There is a marked disproportionality between bleaching of rhodopsin and stimulation of phosphodiesterase. Bleaching only 0.6% of the rhodopsin produces half the stimulation produced by bleaching 100% of the rhodopsin. The process of activation of phosphodiesterase by light is in two steps, a light-dependent step followed by an ATP-dependent step. Illumination (in the absence of ATP) produces a trypsin-resistant, heat-labile, macromolecular stimulator. In the presence of 0.75 mM ATP (GTP or ITP) this stimulator produces a greater than 5-fold increase in the Vmaxof photoreceptor phosphodiesterase without changing the Km. At physiological substrate concentrations (10-7M) the rate of hydrolysis of cyclic GMP is 23 times greater than that of cyclic AMP. The light-produced stimulator appears unique to the photoreceptor membranes and does not activate phosphodiesterase in other tissues.</description><subject>Adenosine Triphosphate</subject><subject>Adenylyl Cyclases - metabolism</subject><subject>Animals</subject><subject>Anura</subject><subject>Biochemistry</subject><subject>Biological Sciences: Biochemistry</subject><subject>Bleaching</subject><subject>Calcium</subject><subject>Calcium - pharmacology</subject><subject>Cell Fractionation</subject><subject>Cell Membrane - enzymology</subject><subject>Cyclic AMP - metabolism</subject><subject>Cyclic GMP - metabolism</subject><subject>Cyclic nucleotides</subject><subject>Darkness</subject><subject>Enzyme Activation</subject><subject>Homogenization</subject><subject>In Vitro Techniques</subject><subject>Kinetics</subject><subject>Light</subject><subject>Mercuribenzoates - pharmacology</subject><subject>Nuclear membrane</subject><subject>P branes</subject><subject>Phosphodiesterase Inhibitors</subject><subject>Phosphoric Diester Hydrolases - metabolism</subject><subject>Photoreceptor Cells - cytology</subject><subject>Photoreceptor Cells - enzymology</subject><subject>Photoreceptors</subject><subject>Physiological regulation</subject><subject>Protein Kinases - pharmacology</subject><subject>Rana pipiens</subject><subject>Receptors</subject><subject>Time Factors</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1973</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUtvEzEUhS0EKqGwRkICeQWrSf0aP5BYRCkvKYIKytqa8XgSV449jD2o-RP8ZhwSAmy6urq63zn20QHgKUZzjAS9GEKT5qIsZE4lQffADCOFK84Uug9mCBFRSUbYQ_AopRuEkKolOgNnjNaKKTwDP7_Y9eSb7GKAsYfLnfHOwE-T8TZm11m4jMHYkMffSIIuwKtNzHG0xg5lpNdwEeDi-qq6tIMNXUHh1-y2d3oWhzRsYudsynZskoXtDq7cepMfgwd945N9cpzn4Nu7t9fLD9Xq8_uPy8WqMozjXBHOMTKq5SUQkbQtUVTNO0mlEFgwYhSTtUEdannNOVEd7lErcYeEEWUaeg7eHHyHqd3a7pDQ62F022bc6dg4_f8luI1exx-aEUEpL_qXR_0Yv08lht66ZKz3TbBxSloSzBlHpIAXB9CMMaXR9qc3MNL7BvW-QS3KQvS-waJ4_u_XTvyxsnJ_dbzvhX-ufw10P3mf7W0u5Is7yQI8OwA3qVR5IjjhtaC_AO0xuso</recordid><startdate>19731201</startdate><enddate>19731201</enddate><creator>Miki, Naomasa</creator><creator>Keirns, James J.</creator><creator>Marcus, Frederick R.</creator><creator>Freeman, Jenny</creator><creator>Bitensky, Mark W.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><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><scope>5PM</scope></search><sort><creationdate>19731201</creationdate><title>Regulation of Cyclic Nucleotide Concentrations in Photoreceptors: An ATP-Dependent Stimulation of Cyclic Nucleotide Phosphodiesterase by Light</title><author>Miki, Naomasa ; Keirns, James J. ; Marcus, Frederick R. ; Freeman, Jenny ; Bitensky, Mark W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c461t-26610c9b6009283b491956d838771742c9485c0d0b656629d1f0b81d07c7b81c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1973</creationdate><topic>Adenosine Triphosphate</topic><topic>Adenylyl Cyclases - metabolism</topic><topic>Animals</topic><topic>Anura</topic><topic>Biochemistry</topic><topic>Biological Sciences: Biochemistry</topic><topic>Bleaching</topic><topic>Calcium</topic><topic>Calcium - pharmacology</topic><topic>Cell Fractionation</topic><topic>Cell Membrane - enzymology</topic><topic>Cyclic AMP - metabolism</topic><topic>Cyclic GMP - metabolism</topic><topic>Cyclic nucleotides</topic><topic>Darkness</topic><topic>Enzyme Activation</topic><topic>Homogenization</topic><topic>In Vitro Techniques</topic><topic>Kinetics</topic><topic>Light</topic><topic>Mercuribenzoates - pharmacology</topic><topic>Nuclear membrane</topic><topic>P branes</topic><topic>Phosphodiesterase Inhibitors</topic><topic>Phosphoric Diester Hydrolases - metabolism</topic><topic>Photoreceptor Cells - cytology</topic><topic>Photoreceptor Cells - enzymology</topic><topic>Photoreceptors</topic><topic>Physiological regulation</topic><topic>Protein Kinases - pharmacology</topic><topic>Rana pipiens</topic><topic>Receptors</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Miki, Naomasa</creatorcontrib><creatorcontrib>Keirns, James J.</creatorcontrib><creatorcontrib>Marcus, Frederick R.</creatorcontrib><creatorcontrib>Freeman, Jenny</creatorcontrib><creatorcontrib>Bitensky, Mark W.</creatorcontrib><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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Miki, Naomasa</au><au>Keirns, James J.</au><au>Marcus, Frederick R.</au><au>Freeman, Jenny</au><au>Bitensky, Mark W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of Cyclic Nucleotide Concentrations in Photoreceptors: An ATP-Dependent Stimulation of Cyclic Nucleotide Phosphodiesterase by Light</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1973-12-01</date><risdate>1973</risdate><volume>70</volume><issue>12</issue><spage>3820</spage><epage>3824</epage><pages>3820-3824</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Regulation of cyclic nucleotide concentrations in rod outer segments (Rana pipiens) has been further examined. The present studies show that illumination markedly diminishes the concentration of cyclic nucleotides in suspensions of photoreceptor membranes, but the locus of regulation is cyclic nucleotide phosphodiesterase (EC 3.1.4.c) (light-stimulated) and not adenylate cyclase. There is a marked disproportionality between bleaching of rhodopsin and stimulation of phosphodiesterase. Bleaching only 0.6% of the rhodopsin produces half the stimulation produced by bleaching 100% of the rhodopsin. The process of activation of phosphodiesterase by light is in two steps, a light-dependent step followed by an ATP-dependent step. Illumination (in the absence of ATP) produces a trypsin-resistant, heat-labile, macromolecular stimulator. In the presence of 0.75 mM ATP (GTP or ITP) this stimulator produces a greater than 5-fold increase in the Vmaxof photoreceptor phosphodiesterase without changing the Km. At physiological substrate concentrations (10-7M) the rate of hydrolysis of cyclic GMP is 23 times greater than that of cyclic AMP. The light-produced stimulator appears unique to the photoreceptor membranes and does not activate phosphodiesterase in other tissues.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>4359491</pmid><doi>10.1073/pnas.70.12.3820</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0027-8424 |
ispartof | Proceedings of the National Academy of Sciences - PNAS, 1973-12, Vol.70 (12), p.3820-3824 |
issn | 0027-8424 1091-6490 |
language | eng |
recordid | cdi_pubmed_primary_4359491 |
source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
subjects | Adenosine Triphosphate Adenylyl Cyclases - metabolism Animals Anura Biochemistry Biological Sciences: Biochemistry Bleaching Calcium Calcium - pharmacology Cell Fractionation Cell Membrane - enzymology Cyclic AMP - metabolism Cyclic GMP - metabolism Cyclic nucleotides Darkness Enzyme Activation Homogenization In Vitro Techniques Kinetics Light Mercuribenzoates - pharmacology Nuclear membrane P branes Phosphodiesterase Inhibitors Phosphoric Diester Hydrolases - metabolism Photoreceptor Cells - cytology Photoreceptor Cells - enzymology Photoreceptors Physiological regulation Protein Kinases - pharmacology Rana pipiens Receptors Time Factors |
title | Regulation of Cyclic Nucleotide Concentrations in Photoreceptors: An ATP-Dependent Stimulation of Cyclic Nucleotide Phosphodiesterase by Light |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-02T05%3A38%3A21IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Regulation%20of%20Cyclic%20Nucleotide%20Concentrations%20in%20Photoreceptors:%20An%20ATP-Dependent%20Stimulation%20of%20Cyclic%20Nucleotide%20Phosphodiesterase%20by%20Light&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Miki,%20Naomasa&rft.date=1973-12-01&rft.volume=70&rft.issue=12&rft.spage=3820&rft.epage=3824&rft.pages=3820-3824&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.70.12.3820&rft_dat=%3Cjstor_pubme%3E62657%3C/jstor_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=82164602&rft_id=info:pmid/4359491&rft_jstor_id=62657&rfr_iscdi=true |