A UDP-glucose:Glycoprotein glucose-1-phosphotransferase in embryonic chicken neural retina
A subclass of cell-surface glycoproteins from embryonic chicken neural retina contains a high mannose-type oligosaccharide that terminates with glucose linked via a phosphodiester bond to penultimate mannose. This unusual oligosaccharide seems responsible for the glycoprotein attachments to the cell...
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| Veröffentlicht in: | Cell 1982-12, Vol.31 (3), p.739-748 |
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| creator | Koro, Lillian A. Marchase, Richard B. |
| description | A subclass of cell-surface glycoproteins from embryonic chicken neural retina contains a high mannose-type oligosaccharide that terminates with glucose linked via a phosphodiester bond to penultimate mannose. This unusual oligosaccharide seems responsible for the glycoprotein attachments to the cell-surface baseplate ligatin. Using β-
32PUDP-
3H-glucose, we demonstrate in retinal homogenates the existence of a UDP-glucose:glyco-protein glucose-1-phosphotransferase (GIcPTase) that catalyzes the synthesis of such a linkage. Characterization of the doubly labeled product resulting from activity of the transferase reveals a family of endoglycosidase H-sensitive oligosaccharides displaying a cation-exchange profile similar to that of oligosaccharides derived from ligatin-associated proteins synthesized in vivo. Further analysis confirms that the incorporation of label is due to a terminal
3H-glucose joined via a
32P-phosphodiester linkage to carbon 6 of a penultimate mannose. We propose that GIcPTase may be a controlling enzyme for the targeting of certain newly synthesized proteins to the cell surface. |
| doi_str_mv | 10.1016/0092-8674(82)90328-2 |
| format | Article |
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32PUDP-
3H-glucose, we demonstrate in retinal homogenates the existence of a UDP-glucose:glyco-protein glucose-1-phosphotransferase (GIcPTase) that catalyzes the synthesis of such a linkage. Characterization of the doubly labeled product resulting from activity of the transferase reveals a family of endoglycosidase H-sensitive oligosaccharides displaying a cation-exchange profile similar to that of oligosaccharides derived from ligatin-associated proteins synthesized in vivo. Further analysis confirms that the incorporation of label is due to a terminal
3H-glucose joined via a
32P-phosphodiester linkage to carbon 6 of a penultimate mannose. We propose that GIcPTase may be a controlling enzyme for the targeting of certain newly synthesized proteins to the cell surface.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/0092-8674(82)90328-2</identifier><identifier>PMID: 6297779</identifier><identifier>CODEN: CELLB5</identifier><language>eng</language><publisher>Cambridge, MA: Elsevier Inc</publisher><subject>550201 - Biochemistry- Tracer Techniques ; Analytical, structural and metabolic biochemistry ; ANIMAL CELLS ; ANIMALS ; BASIC BIOLOGICAL SCIENCES ; BETA DECAY RADIOISOTOPES ; BETA-MINUS DECAY RADIOISOTOPES ; BIOCHEMISTRY ; Biological and medical sciences ; BIRDS ; BODY ; BODY AREAS ; CARBOHYDRATES ; CHEMISTRY ; Chick Embryo ; CHICKENS ; DAYS LIVING RADIOISOTOPES ; EMBRYOS ; ENZYME ACTIVITY ; ENZYMES ; Enzymes and enzyme inhibitors ; EYES ; FACE ; FOWL ; Fundamental and applied biological sciences. Psychology ; HEAD ; ISOTOPE APPLICATIONS ; ISOTOPES ; Kinetics ; LABELLED COMPOUNDS ; LIGHT NUCLEI ; NERVE CELLS ; Neurons - enzymology ; NUCLEI ; ODD-ODD NUCLEI ; OLIGOSACCHARIDES ; Oligosaccharides - biosynthesis ; ORGANIC COMPOUNDS ; ORGANS ; PHOSPHORUS 32 ; PHOSPHORUS ISOTOPES ; Phosphorus Radioisotopes ; PHOSPHORUS-GROUP TRANSFERASES ; PHOSPHOTRANSFERASES ; Phosphotransferases - metabolism ; RADIOISOTOPES ; RETINA ; Retina - enzymology ; SACCHARIDES ; SENSE ORGANS ; SOMATIC CELLS ; STRUCTURAL CHEMICAL ANALYSIS ; Substrate Specificity ; TRACER TECHNIQUES ; TRANSFERASES ; Transferases (Other Substituted Phosphate Groups) ; Tritium ; TRITIUM COMPOUNDS ; Uridine Diphosphate Glucose ; VERTEBRATES</subject><ispartof>Cell, 1982-12, Vol.31 (3), p.739-748</ispartof><rights>1982</rights><rights>1984 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c463t-c9bc36769cdbd8c4452fa049c40990b93b07497f0dfe0b8720958ad4f718b0803</citedby><cites>FETCH-LOGICAL-c463t-c9bc36769cdbd8c4452fa049c40990b93b07497f0dfe0b8720958ad4f718b0803</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0092867482903282$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,881,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=9366268$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6297779$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/6225819$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Koro, Lillian A.</creatorcontrib><creatorcontrib>Marchase, Richard B.</creatorcontrib><creatorcontrib>Department of Anatomy, Duke University Medical Center, Durham, North Carolina</creatorcontrib><title>A UDP-glucose:Glycoprotein glucose-1-phosphotransferase in embryonic chicken neural retina</title><title>Cell</title><addtitle>Cell</addtitle><description>A subclass of cell-surface glycoproteins from embryonic chicken neural retina contains a high mannose-type oligosaccharide that terminates with glucose linked via a phosphodiester bond to penultimate mannose. This unusual oligosaccharide seems responsible for the glycoprotein attachments to the cell-surface baseplate ligatin. Using β-
32PUDP-
3H-glucose, we demonstrate in retinal homogenates the existence of a UDP-glucose:glyco-protein glucose-1-phosphotransferase (GIcPTase) that catalyzes the synthesis of such a linkage. Characterization of the doubly labeled product resulting from activity of the transferase reveals a family of endoglycosidase H-sensitive oligosaccharides displaying a cation-exchange profile similar to that of oligosaccharides derived from ligatin-associated proteins synthesized in vivo. Further analysis confirms that the incorporation of label is due to a terminal
3H-glucose joined via a
32P-phosphodiester linkage to carbon 6 of a penultimate mannose. We propose that GIcPTase may be a controlling enzyme for the targeting of certain newly synthesized proteins to the cell surface.</description><subject>550201 - Biochemistry- Tracer Techniques</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>ANIMAL CELLS</subject><subject>ANIMALS</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>BETA DECAY RADIOISOTOPES</subject><subject>BETA-MINUS DECAY RADIOISOTOPES</subject><subject>BIOCHEMISTRY</subject><subject>Biological and medical sciences</subject><subject>BIRDS</subject><subject>BODY</subject><subject>BODY AREAS</subject><subject>CARBOHYDRATES</subject><subject>CHEMISTRY</subject><subject>Chick Embryo</subject><subject>CHICKENS</subject><subject>DAYS LIVING RADIOISOTOPES</subject><subject>EMBRYOS</subject><subject>ENZYME ACTIVITY</subject><subject>ENZYMES</subject><subject>Enzymes and enzyme inhibitors</subject><subject>EYES</subject><subject>FACE</subject><subject>FOWL</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>HEAD</subject><subject>ISOTOPE APPLICATIONS</subject><subject>ISOTOPES</subject><subject>Kinetics</subject><subject>LABELLED COMPOUNDS</subject><subject>LIGHT NUCLEI</subject><subject>NERVE CELLS</subject><subject>Neurons - enzymology</subject><subject>NUCLEI</subject><subject>ODD-ODD NUCLEI</subject><subject>OLIGOSACCHARIDES</subject><subject>Oligosaccharides - biosynthesis</subject><subject>ORGANIC COMPOUNDS</subject><subject>ORGANS</subject><subject>PHOSPHORUS 32</subject><subject>PHOSPHORUS ISOTOPES</subject><subject>Phosphorus Radioisotopes</subject><subject>PHOSPHORUS-GROUP TRANSFERASES</subject><subject>PHOSPHOTRANSFERASES</subject><subject>Phosphotransferases - metabolism</subject><subject>RADIOISOTOPES</subject><subject>RETINA</subject><subject>Retina - enzymology</subject><subject>SACCHARIDES</subject><subject>SENSE ORGANS</subject><subject>SOMATIC CELLS</subject><subject>STRUCTURAL CHEMICAL ANALYSIS</subject><subject>Substrate Specificity</subject><subject>TRACER TECHNIQUES</subject><subject>TRANSFERASES</subject><subject>Transferases (Other Substituted Phosphate Groups)</subject><subject>Tritium</subject><subject>TRITIUM COMPOUNDS</subject><subject>Uridine Diphosphate Glucose</subject><subject>VERTEBRATES</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkV-L1DAUxYso67j6BUShLCL6UL1J89cHYVl1FRYUdF58CWl6uxPtJGPSCvPtbW2ZR30IgZxfzk3OKYonBF4RIOI1gKaVEpK9UPSlhpqqit4pNgS0rBiR9G6xOSH3iwc5_wAAxTk_K84E1VJKvSm-X5bbd1-q2350MeOb6_7o4iHFAX0o18OKVIddzNMakg25w2QzlpOO-yYdY_CudDvvfmIoA47J9mXCwQf7sLjX2T7jo3U_L7Yf3n-7-ljdfL7-dHV5Uzkm6qFyunG1kEK7tmmVY4zTzgLTjoHW0Oi6Acm07KDtEBolKWiubMs6SVQDCurz4mLxjXnwJjs_oNu5GAK6wQhKuSJ6gp4v0PS5XyPmwex9dtj3NmAcs1FApVKC_hcknDOuxDyWLaBLMeeEnTkkv7fpaAiYuSAzp2_m9I2i5m9BZvZ_uvqPzR7b06W1kUl_tuo2O9t3U-TO5xOmayGoUBP2eME6G429TROy_aooZ4LP4ttFxCn23x7TnAoGh61Pcyht9P9-5B9br7O1</recordid><startdate>198212</startdate><enddate>198212</enddate><creator>Koro, Lillian A.</creator><creator>Marchase, Richard B.</creator><general>Elsevier Inc</general><general>Cell Press</general><scope>FBQ</scope><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>7TK</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>198212</creationdate><title>A UDP-glucose:Glycoprotein glucose-1-phosphotransferase in embryonic chicken neural retina</title><author>Koro, Lillian A. ; Marchase, Richard B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c463t-c9bc36769cdbd8c4452fa049c40990b93b07497f0dfe0b8720958ad4f718b0803</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>550201 - Biochemistry- Tracer Techniques</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>ANIMAL CELLS</topic><topic>ANIMALS</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>BETA DECAY RADIOISOTOPES</topic><topic>BETA-MINUS DECAY RADIOISOTOPES</topic><topic>BIOCHEMISTRY</topic><topic>Biological and medical sciences</topic><topic>BIRDS</topic><topic>BODY</topic><topic>BODY AREAS</topic><topic>CARBOHYDRATES</topic><topic>CHEMISTRY</topic><topic>Chick Embryo</topic><topic>CHICKENS</topic><topic>DAYS LIVING RADIOISOTOPES</topic><topic>EMBRYOS</topic><topic>ENZYME ACTIVITY</topic><topic>ENZYMES</topic><topic>Enzymes and enzyme inhibitors</topic><topic>EYES</topic><topic>FACE</topic><topic>FOWL</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>HEAD</topic><topic>ISOTOPE APPLICATIONS</topic><topic>ISOTOPES</topic><topic>Kinetics</topic><topic>LABELLED COMPOUNDS</topic><topic>LIGHT NUCLEI</topic><topic>NERVE CELLS</topic><topic>Neurons - enzymology</topic><topic>NUCLEI</topic><topic>ODD-ODD NUCLEI</topic><topic>OLIGOSACCHARIDES</topic><topic>Oligosaccharides - biosynthesis</topic><topic>ORGANIC COMPOUNDS</topic><topic>ORGANS</topic><topic>PHOSPHORUS 32</topic><topic>PHOSPHORUS ISOTOPES</topic><topic>Phosphorus Radioisotopes</topic><topic>PHOSPHORUS-GROUP TRANSFERASES</topic><topic>PHOSPHOTRANSFERASES</topic><topic>Phosphotransferases - metabolism</topic><topic>RADIOISOTOPES</topic><topic>RETINA</topic><topic>Retina - enzymology</topic><topic>SACCHARIDES</topic><topic>SENSE ORGANS</topic><topic>SOMATIC CELLS</topic><topic>STRUCTURAL CHEMICAL ANALYSIS</topic><topic>Substrate Specificity</topic><topic>TRACER TECHNIQUES</topic><topic>TRANSFERASES</topic><topic>Transferases (Other Substituted Phosphate Groups)</topic><topic>Tritium</topic><topic>TRITIUM COMPOUNDS</topic><topic>Uridine Diphosphate Glucose</topic><topic>VERTEBRATES</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Koro, Lillian A.</creatorcontrib><creatorcontrib>Marchase, Richard B.</creatorcontrib><creatorcontrib>Department of Anatomy, Duke University Medical Center, Durham, North Carolina</creatorcontrib><collection>AGRIS</collection><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>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Koro, Lillian A.</au><au>Marchase, Richard B.</au><aucorp>Department of Anatomy, Duke University Medical Center, Durham, North Carolina</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A UDP-glucose:Glycoprotein glucose-1-phosphotransferase in embryonic chicken neural retina</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1982-12</date><risdate>1982</risdate><volume>31</volume><issue>3</issue><spage>739</spage><epage>748</epage><pages>739-748</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><coden>CELLB5</coden><abstract>A subclass of cell-surface glycoproteins from embryonic chicken neural retina contains a high mannose-type oligosaccharide that terminates with glucose linked via a phosphodiester bond to penultimate mannose. This unusual oligosaccharide seems responsible for the glycoprotein attachments to the cell-surface baseplate ligatin. Using β-
32PUDP-
3H-glucose, we demonstrate in retinal homogenates the existence of a UDP-glucose:glyco-protein glucose-1-phosphotransferase (GIcPTase) that catalyzes the synthesis of such a linkage. Characterization of the doubly labeled product resulting from activity of the transferase reveals a family of endoglycosidase H-sensitive oligosaccharides displaying a cation-exchange profile similar to that of oligosaccharides derived from ligatin-associated proteins synthesized in vivo. Further analysis confirms that the incorporation of label is due to a terminal
3H-glucose joined via a
32P-phosphodiester linkage to carbon 6 of a penultimate mannose. We propose that GIcPTase may be a controlling enzyme for the targeting of certain newly synthesized proteins to the cell surface.</abstract><cop>Cambridge, MA</cop><pub>Elsevier Inc</pub><pmid>6297779</pmid><doi>10.1016/0092-8674(82)90328-2</doi><tpages>10</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0092-8674 |
| ispartof | Cell, 1982-12, Vol.31 (3), p.739-748 |
| issn | 0092-8674 1097-4172 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80278862 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | 550201 - Biochemistry- Tracer Techniques Analytical, structural and metabolic biochemistry ANIMAL CELLS ANIMALS BASIC BIOLOGICAL SCIENCES BETA DECAY RADIOISOTOPES BETA-MINUS DECAY RADIOISOTOPES BIOCHEMISTRY Biological and medical sciences BIRDS BODY BODY AREAS CARBOHYDRATES CHEMISTRY Chick Embryo CHICKENS DAYS LIVING RADIOISOTOPES EMBRYOS ENZYME ACTIVITY ENZYMES Enzymes and enzyme inhibitors EYES FACE FOWL Fundamental and applied biological sciences. Psychology HEAD ISOTOPE APPLICATIONS ISOTOPES Kinetics LABELLED COMPOUNDS LIGHT NUCLEI NERVE CELLS Neurons - enzymology NUCLEI ODD-ODD NUCLEI OLIGOSACCHARIDES Oligosaccharides - biosynthesis ORGANIC COMPOUNDS ORGANS PHOSPHORUS 32 PHOSPHORUS ISOTOPES Phosphorus Radioisotopes PHOSPHORUS-GROUP TRANSFERASES PHOSPHOTRANSFERASES Phosphotransferases - metabolism RADIOISOTOPES RETINA Retina - enzymology SACCHARIDES SENSE ORGANS SOMATIC CELLS STRUCTURAL CHEMICAL ANALYSIS Substrate Specificity TRACER TECHNIQUES TRANSFERASES Transferases (Other Substituted Phosphate Groups) Tritium TRITIUM COMPOUNDS Uridine Diphosphate Glucose VERTEBRATES |
| title | A UDP-glucose:Glycoprotein glucose-1-phosphotransferase in embryonic chicken neural retina |
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