Effect of tunicamycin on the glycosylation of rhodopsin
The incorporation of [ 3H]glucosamine, [ 3H]mannose, and [ 35S]methionine into rhodopsin was investigated in retinas which had been incubated in the presence and absence of the antibiotic, tunicamycin. In its presence, the incorporation of glucosamine was inhibited 70% and mannose, 96% compared to c...
Gespeichert in:
| Veröffentlicht in: | Archives of biochemistry and biophysics 1980-05, Vol.201 (2), p.527-532 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 532 |
|---|---|
| container_issue | 2 |
| container_start_page | 527 |
| container_title | Archives of biochemistry and biophysics |
| container_volume | 201 |
| creator | Plantner, James J. Poncz, Louis Kean, Edward L. |
| description | The incorporation of [
3H]glucosamine, [
3H]mannose, and [
35S]methionine into rhodopsin was investigated in retinas which had been incubated in the presence and absence of the antibiotic, tunicamycin. In its presence, the incorporation of glucosamine was inhibited 70% and mannose, 96% compared to controls. In the presence of tunicamycin the attachment of glucosamine to core-region sites was virtually eliminated. The formation of unglycosylated rhodopsin was also indicated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and concanavalin A-Sepharose chromatography. These findings are consistent with the participation of the lipid-linked pathway in the glycosylation of this well-characterized intrinsic glycoprotein of the membranes of the disk of the rod outer segment. As indicated by the incorporation of [
35S]methionine, the synthesis of rhodopsin apoprotein was inhibited by a much lesser amount. This suggests that the glycosylation of rhodopsin is not required for its insertion into the disk membrane. |
| doi_str_mv | 10.1016/0003-9861(80)90541-X |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_75181274</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>000398618090541X</els_id><sourcerecordid>75181274</sourcerecordid><originalsourceid>FETCH-LOGICAL-c357t-ada3f320f4ed95cac1db547db6bc9573537b69164a54fd678818f1957bc83dfd3</originalsourceid><addsrcrecordid>eNp9kMtKw0AUhgdRaq2-gUJWoovoTOaajSClXqDgRqG7YTIXO5Jk6kwi5O1NbenS1YHzXw7nA-ASwTsEEbuHEOK8FAzdCHhbQkpQvjoCUwRLlkMsyDGYHiyn4CylLwgRIqyYgAnHJaMFnAK-cM7qLgsu6_rWa9UM2rdZaLNubbPPetAhDbXq_LgZPXEdTNgk356DE6fqZC_2cwY-nhbv85d8-fb8On9c5hpT3uXKKOxwAR2xpqRaaWQqSripWKVLyjHFvGIlYkRR4gzjQiDh0KhUWmDjDJ6B613vJobv3qZONj5pW9eqtaFPklMkUMHJaCQ7o44hpWid3ETfqDhIBOWWl9zCkFsYUkD5x0uuxtjVvr-vGmsOoT2gUX_Y6XZ88sfbKJP2ttXW-Dhykyb4_w_8AmdYecc</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>75181274</pqid></control><display><type>article</type><title>Effect of tunicamycin on the glycosylation of rhodopsin</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Plantner, James J. ; Poncz, Louis ; Kean, Edward L.</creator><creatorcontrib>Plantner, James J. ; Poncz, Louis ; Kean, Edward L.</creatorcontrib><description>The incorporation of [
3H]glucosamine, [
3H]mannose, and [
35S]methionine into rhodopsin was investigated in retinas which had been incubated in the presence and absence of the antibiotic, tunicamycin. In its presence, the incorporation of glucosamine was inhibited 70% and mannose, 96% compared to controls. In the presence of tunicamycin the attachment of glucosamine to core-region sites was virtually eliminated. The formation of unglycosylated rhodopsin was also indicated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and concanavalin A-Sepharose chromatography. These findings are consistent with the participation of the lipid-linked pathway in the glycosylation of this well-characterized intrinsic glycoprotein of the membranes of the disk of the rod outer segment. As indicated by the incorporation of [
35S]methionine, the synthesis of rhodopsin apoprotein was inhibited by a much lesser amount. This suggests that the glycosylation of rhodopsin is not required for its insertion into the disk membrane.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(80)90541-X</identifier><identifier>PMID: 7396520</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Cattle ; Culture Techniques ; Electrophoresis, Polyacrylamide Gel ; Glucosamine - analogs & derivatives ; Glucosamine - metabolism ; Glycoproteins - biosynthesis ; Mannose - metabolism ; Membrane Proteins - biosynthesis ; Methionine - metabolism ; Retinal Pigments - metabolism ; Rhodopsin - metabolism ; Tunicamycin - pharmacology</subject><ispartof>Archives of biochemistry and biophysics, 1980-05, Vol.201 (2), p.527-532</ispartof><rights>1980</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-ada3f320f4ed95cac1db547db6bc9573537b69164a54fd678818f1957bc83dfd3</citedby><cites>FETCH-LOGICAL-c357t-ada3f320f4ed95cac1db547db6bc9573537b69164a54fd678818f1957bc83dfd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/000398618090541X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27902,27903,65308</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7396520$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Plantner, James J.</creatorcontrib><creatorcontrib>Poncz, Louis</creatorcontrib><creatorcontrib>Kean, Edward L.</creatorcontrib><title>Effect of tunicamycin on the glycosylation of rhodopsin</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The incorporation of [
3H]glucosamine, [
3H]mannose, and [
35S]methionine into rhodopsin was investigated in retinas which had been incubated in the presence and absence of the antibiotic, tunicamycin. In its presence, the incorporation of glucosamine was inhibited 70% and mannose, 96% compared to controls. In the presence of tunicamycin the attachment of glucosamine to core-region sites was virtually eliminated. The formation of unglycosylated rhodopsin was also indicated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and concanavalin A-Sepharose chromatography. These findings are consistent with the participation of the lipid-linked pathway in the glycosylation of this well-characterized intrinsic glycoprotein of the membranes of the disk of the rod outer segment. As indicated by the incorporation of [
35S]methionine, the synthesis of rhodopsin apoprotein was inhibited by a much lesser amount. This suggests that the glycosylation of rhodopsin is not required for its insertion into the disk membrane.</description><subject>Animals</subject><subject>Cattle</subject><subject>Culture Techniques</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Glucosamine - analogs & derivatives</subject><subject>Glucosamine - metabolism</subject><subject>Glycoproteins - biosynthesis</subject><subject>Mannose - metabolism</subject><subject>Membrane Proteins - biosynthesis</subject><subject>Methionine - metabolism</subject><subject>Retinal Pigments - metabolism</subject><subject>Rhodopsin - metabolism</subject><subject>Tunicamycin - pharmacology</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtKw0AUhgdRaq2-gUJWoovoTOaajSClXqDgRqG7YTIXO5Jk6kwi5O1NbenS1YHzXw7nA-ASwTsEEbuHEOK8FAzdCHhbQkpQvjoCUwRLlkMsyDGYHiyn4CylLwgRIqyYgAnHJaMFnAK-cM7qLgsu6_rWa9UM2rdZaLNubbPPetAhDbXq_LgZPXEdTNgk356DE6fqZC_2cwY-nhbv85d8-fb8On9c5hpT3uXKKOxwAR2xpqRaaWQqSripWKVLyjHFvGIlYkRR4gzjQiDh0KhUWmDjDJ6B613vJobv3qZONj5pW9eqtaFPklMkUMHJaCQ7o44hpWid3ETfqDhIBOWWl9zCkFsYUkD5x0uuxtjVvr-vGmsOoT2gUX_Y6XZ88sfbKJP2ttXW-Dhykyb4_w_8AmdYecc</recordid><startdate>198005</startdate><enddate>198005</enddate><creator>Plantner, James J.</creator><creator>Poncz, Louis</creator><creator>Kean, Edward L.</creator><general>Elsevier Inc</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></search><sort><creationdate>198005</creationdate><title>Effect of tunicamycin on the glycosylation of rhodopsin</title><author>Plantner, James J. ; Poncz, Louis ; Kean, Edward L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-ada3f320f4ed95cac1db547db6bc9573537b69164a54fd678818f1957bc83dfd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1980</creationdate><topic>Animals</topic><topic>Cattle</topic><topic>Culture Techniques</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Glucosamine - analogs & derivatives</topic><topic>Glucosamine - metabolism</topic><topic>Glycoproteins - biosynthesis</topic><topic>Mannose - metabolism</topic><topic>Membrane Proteins - biosynthesis</topic><topic>Methionine - metabolism</topic><topic>Retinal Pigments - metabolism</topic><topic>Rhodopsin - metabolism</topic><topic>Tunicamycin - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Plantner, James J.</creatorcontrib><creatorcontrib>Poncz, Louis</creatorcontrib><creatorcontrib>Kean, Edward L.</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><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Plantner, James J.</au><au>Poncz, Louis</au><au>Kean, Edward L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effect of tunicamycin on the glycosylation of rhodopsin</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1980-05</date><risdate>1980</risdate><volume>201</volume><issue>2</issue><spage>527</spage><epage>532</epage><pages>527-532</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>The incorporation of [
3H]glucosamine, [
3H]mannose, and [
35S]methionine into rhodopsin was investigated in retinas which had been incubated in the presence and absence of the antibiotic, tunicamycin. In its presence, the incorporation of glucosamine was inhibited 70% and mannose, 96% compared to controls. In the presence of tunicamycin the attachment of glucosamine to core-region sites was virtually eliminated. The formation of unglycosylated rhodopsin was also indicated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and concanavalin A-Sepharose chromatography. These findings are consistent with the participation of the lipid-linked pathway in the glycosylation of this well-characterized intrinsic glycoprotein of the membranes of the disk of the rod outer segment. As indicated by the incorporation of [
35S]methionine, the synthesis of rhodopsin apoprotein was inhibited by a much lesser amount. This suggests that the glycosylation of rhodopsin is not required for its insertion into the disk membrane.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7396520</pmid><doi>10.1016/0003-9861(80)90541-X</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-9861 |
| ispartof | Archives of biochemistry and biophysics, 1980-05, Vol.201 (2), p.527-532 |
| issn | 0003-9861 1096-0384 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_75181274 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Animals Cattle Culture Techniques Electrophoresis, Polyacrylamide Gel Glucosamine - analogs & derivatives Glucosamine - metabolism Glycoproteins - biosynthesis Mannose - metabolism Membrane Proteins - biosynthesis Methionine - metabolism Retinal Pigments - metabolism Rhodopsin - metabolism Tunicamycin - pharmacology |
| title | Effect of tunicamycin on the glycosylation of rhodopsin |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-27T09%3A15%3A17IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Effect%20of%20tunicamycin%20on%20the%20glycosylation%20of%20rhodopsin&rft.jtitle=Archives%20of%20biochemistry%20and%20biophysics&rft.au=Plantner,%20James%20J.&rft.date=1980-05&rft.volume=201&rft.issue=2&rft.spage=527&rft.epage=532&rft.pages=527-532&rft.issn=0003-9861&rft.eissn=1096-0384&rft_id=info:doi/10.1016/0003-9861(80)90541-X&rft_dat=%3Cproquest_cross%3E75181274%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=75181274&rft_id=info:pmid/7396520&rft_els_id=000398618090541X&rfr_iscdi=true |