Localization of HRG4, a photoreceptor protein homologous to Unc-119, in ribbon synapse
To characterize further HRG4, a novel photoreceptor protein recently identified by subtractive cDNA cloning, by sequence analysis and immunolocalization. The rat homolog of HRG4, RRG4 was expressed and used to prepare an antibody. The antibody was used in Western blot analysis, and immunofluorescent...
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| Veröffentlicht in: | Investigative ophthalmology & visual science 1998-04, Vol.39 (5), p.690-698 |
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| creator | Higashide, T McLaren, MJ Inana, G |
| description | To characterize further HRG4, a novel photoreceptor protein recently identified by subtractive cDNA cloning, by sequence analysis and immunolocalization.
The rat homolog of HRG4, RRG4 was expressed and used to prepare an antibody. The antibody was used in Western blot analysis, and immunofluorescent localization at the light and electron microscopic levels of HRG4-RRG4 protein. The HRG4-RRG4 sequence was also analyzed for homologies.
HRG4-RRG4 showed 57% homology with unc-119, a Caenorhabditis elegans neuroprotein causing defects in locomotion, feeding, and chemosensation when mutated. By Western blot analysis, the HRG4-RRG4 protein was demonstrable only in retina and was soluble in nature. Immunofluorescence microscopic study of human and rat retinas, using the HRG4-RRG4 antibody, and other rod and cone photoreceptor-specific antibodies showed that the HRG4-RRG4 protein is localized in the outer plexiform layer of the retina in the synaptic termini of rod and cone photoreceptors. Electron microscopic immunolocalization showed the protein in the cytoplasm and on the presynaptic membranes of the photoreceptor synapses.
The homology to unc-119 and localization to the photoreceptor synapse are suggestive of a function for HRG4-RRG4 in photoreceptor neurotransmission. HRG4 is the first photoreceptor-enriched synaptic protein to be reported, suggesting that its function may be unique to the specialized ribbon synapses formed between photoreceptors and the horizontal and bipolar cells of the retina. |
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The rat homolog of HRG4, RRG4 was expressed and used to prepare an antibody. The antibody was used in Western blot analysis, and immunofluorescent localization at the light and electron microscopic levels of HRG4-RRG4 protein. The HRG4-RRG4 sequence was also analyzed for homologies.
HRG4-RRG4 showed 57% homology with unc-119, a Caenorhabditis elegans neuroprotein causing defects in locomotion, feeding, and chemosensation when mutated. By Western blot analysis, the HRG4-RRG4 protein was demonstrable only in retina and was soluble in nature. Immunofluorescence microscopic study of human and rat retinas, using the HRG4-RRG4 antibody, and other rod and cone photoreceptor-specific antibodies showed that the HRG4-RRG4 protein is localized in the outer plexiform layer of the retina in the synaptic termini of rod and cone photoreceptors. Electron microscopic immunolocalization showed the protein in the cytoplasm and on the presynaptic membranes of the photoreceptor synapses.
The homology to unc-119 and localization to the photoreceptor synapse are suggestive of a function for HRG4-RRG4 in photoreceptor neurotransmission. HRG4 is the first photoreceptor-enriched synaptic protein to be reported, suggesting that its function may be unique to the specialized ribbon synapses formed between photoreceptors and the horizontal and bipolar cells of the retina.</description><identifier>ISSN: 0146-0404</identifier><identifier>EISSN: 1552-5783</identifier><identifier>PMID: 9538874</identifier><identifier>CODEN: IOVSDA</identifier><language>eng</language><publisher>Rockville, MD: ARVO</publisher><subject>Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Biological and medical sciences ; Blotting, Western ; Caenorhabditis elegans Proteins ; Consensus Sequence ; DNA Primers - chemistry ; Electrophoresis, Polyacrylamide Gel ; Eye and associated structures. Visual pathways and centers. Vision ; Eye Proteins - analysis ; Eye Proteins - genetics ; Eye Proteins - immunology ; Fluorescent Antibody Technique, Indirect ; Fundamental and applied biological sciences. Psychology ; Helminth Proteins - analysis ; Helminth Proteins - genetics ; Humans ; Microscopy, Immunoelectron ; Molecular Sequence Data ; Nerve Tissue Proteins - analysis ; Nerve Tissue Proteins - genetics ; Photoreceptor Cells - chemistry ; Presynaptic Terminals - chemistry ; Rabbits ; Rats ; Recombinant Proteins ; Sequence Homology, Amino Acid ; Vertebrates: nervous system and sense organs</subject><ispartof>Investigative ophthalmology & visual science, 1998-04, Vol.39 (5), p.690-698</ispartof><rights>1998 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2225364$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9538874$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Higashide, T</creatorcontrib><creatorcontrib>McLaren, MJ</creatorcontrib><creatorcontrib>Inana, G</creatorcontrib><title>Localization of HRG4, a photoreceptor protein homologous to Unc-119, in ribbon synapse</title><title>Investigative ophthalmology & visual science</title><addtitle>Invest Ophthalmol Vis Sci</addtitle><description>To characterize further HRG4, a novel photoreceptor protein recently identified by subtractive cDNA cloning, by sequence analysis and immunolocalization.
The rat homolog of HRG4, RRG4 was expressed and used to prepare an antibody. The antibody was used in Western blot analysis, and immunofluorescent localization at the light and electron microscopic levels of HRG4-RRG4 protein. The HRG4-RRG4 sequence was also analyzed for homologies.
HRG4-RRG4 showed 57% homology with unc-119, a Caenorhabditis elegans neuroprotein causing defects in locomotion, feeding, and chemosensation when mutated. By Western blot analysis, the HRG4-RRG4 protein was demonstrable only in retina and was soluble in nature. Immunofluorescence microscopic study of human and rat retinas, using the HRG4-RRG4 antibody, and other rod and cone photoreceptor-specific antibodies showed that the HRG4-RRG4 protein is localized in the outer plexiform layer of the retina in the synaptic termini of rod and cone photoreceptors. Electron microscopic immunolocalization showed the protein in the cytoplasm and on the presynaptic membranes of the photoreceptor synapses.
The homology to unc-119 and localization to the photoreceptor synapse are suggestive of a function for HRG4-RRG4 in photoreceptor neurotransmission. HRG4 is the first photoreceptor-enriched synaptic protein to be reported, suggesting that its function may be unique to the specialized ribbon synapses formed between photoreceptors and the horizontal and bipolar cells of the retina.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Caenorhabditis elegans Proteins</subject><subject>Consensus Sequence</subject><subject>DNA Primers - chemistry</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Eye and associated structures. Visual pathways and centers. Vision</subject><subject>Eye Proteins - analysis</subject><subject>Eye Proteins - genetics</subject><subject>Eye Proteins - immunology</subject><subject>Fluorescent Antibody Technique, Indirect</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Helminth Proteins - analysis</subject><subject>Helminth Proteins - genetics</subject><subject>Humans</subject><subject>Microscopy, Immunoelectron</subject><subject>Molecular Sequence Data</subject><subject>Nerve Tissue Proteins - analysis</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Photoreceptor Cells - chemistry</subject><subject>Presynaptic Terminals - chemistry</subject><subject>Rabbits</subject><subject>Rats</subject><subject>Recombinant Proteins</subject><subject>Sequence Homology, Amino Acid</subject><subject>Vertebrates: nervous system and sense organs</subject><issn>0146-0404</issn><issn>1552-5783</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kM9LwzAAhYMoc07_BCEH9bRCfjc5iugmDARxXkOapWukbWrTUeZfb2TF0zu8j4_HOwNzzDnJeC7pOZgjzESGGGKX4CrGL4QIxgTNwExxKmXO5uBzE6yp_Y8ZfGhhKOH6fcWW0MCuCkPonXVdCtj1YXC-hVVoQh324RDhEOC2tRnGaglT0_uiSIZ4bE0X3TW4KE0d3c2UC7B9ef54Wmebt9Xr0-Mmq4jgQ-akRBYbrqxSlinKBaJYMSOlo5gXeS5dLmwuVEFEUVBXMkvLXGCLEZF8Z-gCPJy8aeD3wcVBNz5aV9emdWmkzlVycEUSeDuBh6JxO931vjH9UU9HpP5u6k1Mh5S9aa2P_xghhFPxh92fsMrvq9H3TsfG1HWSYj2OI1Waa6EQ_QUGtnLd</recordid><startdate>19980401</startdate><enddate>19980401</enddate><creator>Higashide, T</creator><creator>McLaren, MJ</creator><creator>Inana, G</creator><general>ARVO</general><general>Association for Research in Vision and Ophtalmology</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19980401</creationdate><title>Localization of HRG4, a photoreceptor protein homologous to Unc-119, in ribbon synapse</title><author>Higashide, T ; McLaren, MJ ; Inana, G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h265t-e880c1a59c99c4935603194a88e315b778e76c769b26bb3ef4c3f761c10285da3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Adaptor Proteins, Signal Transducing</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Caenorhabditis elegans Proteins</topic><topic>Consensus Sequence</topic><topic>DNA Primers - chemistry</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Eye and associated structures. Visual pathways and centers. Vision</topic><topic>Eye Proteins - analysis</topic><topic>Eye Proteins - genetics</topic><topic>Eye Proteins - immunology</topic><topic>Fluorescent Antibody Technique, Indirect</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Helminth Proteins - analysis</topic><topic>Helminth Proteins - genetics</topic><topic>Humans</topic><topic>Microscopy, Immunoelectron</topic><topic>Molecular Sequence Data</topic><topic>Nerve Tissue Proteins - analysis</topic><topic>Nerve Tissue Proteins - genetics</topic><topic>Photoreceptor Cells - chemistry</topic><topic>Presynaptic Terminals - chemistry</topic><topic>Rabbits</topic><topic>Rats</topic><topic>Recombinant Proteins</topic><topic>Sequence Homology, Amino Acid</topic><topic>Vertebrates: nervous system and sense organs</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Higashide, T</creatorcontrib><creatorcontrib>McLaren, MJ</creatorcontrib><creatorcontrib>Inana, G</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>MEDLINE - Academic</collection><jtitle>Investigative ophthalmology & visual science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Higashide, T</au><au>McLaren, MJ</au><au>Inana, G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Localization of HRG4, a photoreceptor protein homologous to Unc-119, in ribbon synapse</atitle><jtitle>Investigative ophthalmology & visual science</jtitle><addtitle>Invest Ophthalmol Vis Sci</addtitle><date>1998-04-01</date><risdate>1998</risdate><volume>39</volume><issue>5</issue><spage>690</spage><epage>698</epage><pages>690-698</pages><issn>0146-0404</issn><eissn>1552-5783</eissn><coden>IOVSDA</coden><abstract>To characterize further HRG4, a novel photoreceptor protein recently identified by subtractive cDNA cloning, by sequence analysis and immunolocalization.
The rat homolog of HRG4, RRG4 was expressed and used to prepare an antibody. The antibody was used in Western blot analysis, and immunofluorescent localization at the light and electron microscopic levels of HRG4-RRG4 protein. The HRG4-RRG4 sequence was also analyzed for homologies.
HRG4-RRG4 showed 57% homology with unc-119, a Caenorhabditis elegans neuroprotein causing defects in locomotion, feeding, and chemosensation when mutated. By Western blot analysis, the HRG4-RRG4 protein was demonstrable only in retina and was soluble in nature. Immunofluorescence microscopic study of human and rat retinas, using the HRG4-RRG4 antibody, and other rod and cone photoreceptor-specific antibodies showed that the HRG4-RRG4 protein is localized in the outer plexiform layer of the retina in the synaptic termini of rod and cone photoreceptors. Electron microscopic immunolocalization showed the protein in the cytoplasm and on the presynaptic membranes of the photoreceptor synapses.
The homology to unc-119 and localization to the photoreceptor synapse are suggestive of a function for HRG4-RRG4 in photoreceptor neurotransmission. HRG4 is the first photoreceptor-enriched synaptic protein to be reported, suggesting that its function may be unique to the specialized ribbon synapses formed between photoreceptors and the horizontal and bipolar cells of the retina.</abstract><cop>Rockville, MD</cop><pub>ARVO</pub><pmid>9538874</pmid><tpages>9</tpages></addata></record> |
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| subjects | Adaptor Proteins, Signal Transducing Amino Acid Sequence Animals Biological and medical sciences Blotting, Western Caenorhabditis elegans Proteins Consensus Sequence DNA Primers - chemistry Electrophoresis, Polyacrylamide Gel Eye and associated structures. Visual pathways and centers. Vision Eye Proteins - analysis Eye Proteins - genetics Eye Proteins - immunology Fluorescent Antibody Technique, Indirect Fundamental and applied biological sciences. Psychology Helminth Proteins - analysis Helminth Proteins - genetics Humans Microscopy, Immunoelectron Molecular Sequence Data Nerve Tissue Proteins - analysis Nerve Tissue Proteins - genetics Photoreceptor Cells - chemistry Presynaptic Terminals - chemistry Rabbits Rats Recombinant Proteins Sequence Homology, Amino Acid Vertebrates: nervous system and sense organs |
| title | Localization of HRG4, a photoreceptor protein homologous to Unc-119, in ribbon synapse |
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