d-[ 3H]galactose incorporation into glycogen in retinal cone cells
Previous studies have shown that bovine retinas incubated with [ 3H]galactose incorporated it, unmodified, into large molecules. Light and electron microscope autoradiography showed a significant proportion of the label to be in cone inner segments, and pulse-chase studies showed it was subsequently...
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Veröffentlicht in: | Experimental eye research 1990-03, Vol.50 (3), p.281-288 |
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creator | Shallal, Asaad McKechnie, Nicol M. Converse, Carolyna Foulds, Wallace S. |
description | Previous studies have shown that bovine retinas incubated with [
3H]galactose incorporated it, unmodified, into large molecules. Light and electron microscope autoradiography showed a significant proportion of the label to be in cone inner segments, and pulse-chase studies showed it was subsequently transported to the synaptic pedicles. In this report, evidence is presented to show that the galactose-labelled macromolecules are resistant to hydrolysis by proteolytic enzymes, testicular hyaluronidase, chondroitinase ABC, β-glucosidase and β-glucuronidase, but are readily degraded by α-amylase and β-galactosidase, and to a lesser extent by β-amylase. Treatment with α-amylase also leads to specific removal of radioactivity from cone inner segments and pedicles, as judged by light-microscopic autoradiography. These studies appear to indicate that the cone-specific galactose label is in glycogen or glycogen-like molecules. |
doi_str_mv | 10.1016/0014-4835(90)90212-D |
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3H]galactose incorporated it, unmodified, into large molecules. Light and electron microscope autoradiography showed a significant proportion of the label to be in cone inner segments, and pulse-chase studies showed it was subsequently transported to the synaptic pedicles. In this report, evidence is presented to show that the galactose-labelled macromolecules are resistant to hydrolysis by proteolytic enzymes, testicular hyaluronidase, chondroitinase ABC, β-glucosidase and β-glucuronidase, but are readily degraded by α-amylase and β-galactosidase, and to a lesser extent by β-amylase. Treatment with α-amylase also leads to specific removal of radioactivity from cone inner segments and pedicles, as judged by light-microscopic autoradiography. These studies appear to indicate that the cone-specific galactose label is in glycogen or glycogen-like molecules.</description><identifier>ISSN: 0014-4835</identifier><identifier>EISSN: 1096-0007</identifier><identifier>DOI: 10.1016/0014-4835(90)90212-D</identifier><identifier>PMID: 2318272</identifier><identifier>CODEN: EXERA6</identifier><language>eng</language><publisher>London: Elsevier Ltd</publisher><subject>Animals ; Autoradiography ; axonal transport ; Biological and medical sciences ; Cattle ; Chromatography, Gel ; Chromatography, Ion Exchange ; cone cells ; Electrophoresis, Polyacrylamide Gel ; Eye and associated structures. Visual pathways and centers. Vision ; Fundamental and applied biological sciences. Psychology ; Galactose - metabolism ; galactosylation ; glycogen ; Glycogen - metabolism ; Hydrolysis ; Photoreceptor Cells - metabolism ; photoreceptors ; retina ; Vertebrates: nervous system and sense organs</subject><ispartof>Experimental eye research, 1990-03, Vol.50 (3), p.281-288</ispartof><rights>1990</rights><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-7fc55bed9273ff03d4d4481b2525495922abcf0451fd8b17cfad0a4e18f61bc3</citedby><cites>FETCH-LOGICAL-c386t-7fc55bed9273ff03d4d4481b2525495922abcf0451fd8b17cfad0a4e18f61bc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-4835(90)90212-D$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6913807$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2318272$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shallal, Asaad</creatorcontrib><creatorcontrib>McKechnie, Nicol M.</creatorcontrib><creatorcontrib>Converse, Carolyna</creatorcontrib><creatorcontrib>Foulds, Wallace S.</creatorcontrib><title>d-[ 3H]galactose incorporation into glycogen in retinal cone cells</title><title>Experimental eye research</title><addtitle>Exp Eye Res</addtitle><description>Previous studies have shown that bovine retinas incubated with [
3H]galactose incorporated it, unmodified, into large molecules. Light and electron microscope autoradiography showed a significant proportion of the label to be in cone inner segments, and pulse-chase studies showed it was subsequently transported to the synaptic pedicles. In this report, evidence is presented to show that the galactose-labelled macromolecules are resistant to hydrolysis by proteolytic enzymes, testicular hyaluronidase, chondroitinase ABC, β-glucosidase and β-glucuronidase, but are readily degraded by α-amylase and β-galactosidase, and to a lesser extent by β-amylase. Treatment with α-amylase also leads to specific removal of radioactivity from cone inner segments and pedicles, as judged by light-microscopic autoradiography. These studies appear to indicate that the cone-specific galactose label is in glycogen or glycogen-like molecules.</description><subject>Animals</subject><subject>Autoradiography</subject><subject>axonal transport</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>Chromatography, Gel</subject><subject>Chromatography, Ion Exchange</subject><subject>cone cells</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Eye and associated structures. Visual pathways and centers. Vision</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Galactose - metabolism</subject><subject>galactosylation</subject><subject>glycogen</subject><subject>Glycogen - metabolism</subject><subject>Hydrolysis</subject><subject>Photoreceptor Cells - metabolism</subject><subject>photoreceptors</subject><subject>retina</subject><subject>Vertebrates: nervous system and sense organs</subject><issn>0014-4835</issn><issn>1096-0007</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LJDEQhoO46Kj7DxT6IKKH3q18dKdzEXT8WhD24k2WkE4qQ6SnMyY9gv9-u51hjp6KqvepongIOaXwiwKtfwNQUYqGV5cKrhQwysq7PTKjoOoSAOQ-me2QQ3KU89s45UKKA3LAOG2YZDNy68rXgj_9W5jO2CFmLEJvY1rFZIYQ-7EbYrHoPm1c4NQVCYfQm66wscfCYtflE_LDmy7jz209Ji8P9y_zp_L57-Of-c1zaXlTD6X0tqpadIpJ7j1wJ5wQDW1ZxSqhKsWYaa0HUVHvmpZK640DI5A2vqat5cfkYnN2leL7GvOglyFPD5ge4zprqeqmAqlGUGxAm2LOCb1epbA06VNT0JM5PWnRkxatQH-Z03fj2tn2_rpdotstbVWN-fk2N9mazifT25B3WK0ob0CO2PUGw1HFR8Cksw3YW3QhoR20i-H7P_4DZDSJRQ</recordid><startdate>19900301</startdate><enddate>19900301</enddate><creator>Shallal, Asaad</creator><creator>McKechnie, Nicol M.</creator><creator>Converse, Carolyna</creator><creator>Foulds, Wallace S.</creator><general>Elsevier Ltd</general><general>Elsevier</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>7X8</scope></search><sort><creationdate>19900301</creationdate><title>d-[ 3H]galactose incorporation into glycogen in retinal cone cells</title><author>Shallal, Asaad ; McKechnie, Nicol M. ; Converse, Carolyna ; Foulds, Wallace S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-7fc55bed9273ff03d4d4481b2525495922abcf0451fd8b17cfad0a4e18f61bc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Animals</topic><topic>Autoradiography</topic><topic>axonal transport</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>Chromatography, Gel</topic><topic>Chromatography, Ion Exchange</topic><topic>cone cells</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Eye and associated structures. Visual pathways and centers. Vision</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Galactose - metabolism</topic><topic>galactosylation</topic><topic>glycogen</topic><topic>Glycogen - metabolism</topic><topic>Hydrolysis</topic><topic>Photoreceptor Cells - metabolism</topic><topic>photoreceptors</topic><topic>retina</topic><topic>Vertebrates: nervous system and sense organs</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shallal, Asaad</creatorcontrib><creatorcontrib>McKechnie, Nicol M.</creatorcontrib><creatorcontrib>Converse, Carolyna</creatorcontrib><creatorcontrib>Foulds, Wallace S.</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>MEDLINE - Academic</collection><jtitle>Experimental eye research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shallal, Asaad</au><au>McKechnie, Nicol M.</au><au>Converse, Carolyna</au><au>Foulds, Wallace S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>d-[ 3H]galactose incorporation into glycogen in retinal cone cells</atitle><jtitle>Experimental eye research</jtitle><addtitle>Exp Eye Res</addtitle><date>1990-03-01</date><risdate>1990</risdate><volume>50</volume><issue>3</issue><spage>281</spage><epage>288</epage><pages>281-288</pages><issn>0014-4835</issn><eissn>1096-0007</eissn><coden>EXERA6</coden><abstract>Previous studies have shown that bovine retinas incubated with [
3H]galactose incorporated it, unmodified, into large molecules. Light and electron microscope autoradiography showed a significant proportion of the label to be in cone inner segments, and pulse-chase studies showed it was subsequently transported to the synaptic pedicles. In this report, evidence is presented to show that the galactose-labelled macromolecules are resistant to hydrolysis by proteolytic enzymes, testicular hyaluronidase, chondroitinase ABC, β-glucosidase and β-glucuronidase, but are readily degraded by α-amylase and β-galactosidase, and to a lesser extent by β-amylase. Treatment with α-amylase also leads to specific removal of radioactivity from cone inner segments and pedicles, as judged by light-microscopic autoradiography. These studies appear to indicate that the cone-specific galactose label is in glycogen or glycogen-like molecules.</abstract><cop>London</cop><pub>Elsevier Ltd</pub><pmid>2318272</pmid><doi>10.1016/0014-4835(90)90212-D</doi><tpages>8</tpages></addata></record> |
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subjects | Animals Autoradiography axonal transport Biological and medical sciences Cattle Chromatography, Gel Chromatography, Ion Exchange cone cells Electrophoresis, Polyacrylamide Gel Eye and associated structures. Visual pathways and centers. Vision Fundamental and applied biological sciences. Psychology Galactose - metabolism galactosylation glycogen Glycogen - metabolism Hydrolysis Photoreceptor Cells - metabolism photoreceptors retina Vertebrates: nervous system and sense organs |
title | d-[ 3H]galactose incorporation into glycogen in retinal cone cells |
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