Two Isoforms of Trimming Glucosidase II Exist in Mammalian Tissues and Cell Lines but Not in Yeast and Insect Cells
We previously cloned glucosidase II and provided in vivo evidence for its involvement in protein folding quality control. DNA-sequencing of different clones demonstrated the existence of two isoforms of glucosidase II which differed by 66 nucleotides due to alternative splicing. The existence of two...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2001-01, Vol.280 (1), p.363-367 |
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| creator | Ziak, Martin Meier, Mirjam Etter, Kay-Sara Roth, Jürgen |
| description | We previously cloned glucosidase II and provided in vivo evidence for its involvement in protein folding quality control. DNA-sequencing of different clones demonstrated the existence of two isoforms of glucosidase II which differed by 66 nucleotides due to alternative splicing. The existence of two enzyme isoforms in various organs of pig and rat as well as human, bovine, rat, and mouse cell lines could be demonstrated by RT-PCR and Western blotting. Furthermore, the two isoforms of glucosidase II could be detected in embryonic and postnatal rat kidney and liver. In yeast, Saccharomyces cerevisiae, and in insects, Drosophila S2 cells, only one isoforms of the enzyme was detectable. The ubiquitous occurrence of the two glucosidase II isoforms in mammalian tissues and cell lines might be indicative of a special function of each isoform. |
| doi_str_mv | 10.1006/bbrc.2000.4082 |
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DNA-sequencing of different clones demonstrated the existence of two isoforms of glucosidase II which differed by 66 nucleotides due to alternative splicing. The existence of two enzyme isoforms in various organs of pig and rat as well as human, bovine, rat, and mouse cell lines could be demonstrated by RT-PCR and Western blotting. Furthermore, the two isoforms of glucosidase II could be detected in embryonic and postnatal rat kidney and liver. In yeast, Saccharomyces cerevisiae, and in insects, Drosophila S2 cells, only one isoforms of the enzyme was detectable. 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DNA-sequencing of different clones demonstrated the existence of two isoforms of glucosidase II which differed by 66 nucleotides due to alternative splicing. The existence of two enzyme isoforms in various organs of pig and rat as well as human, bovine, rat, and mouse cell lines could be demonstrated by RT-PCR and Western blotting. Furthermore, the two isoforms of glucosidase II could be detected in embryonic and postnatal rat kidney and liver. In yeast, Saccharomyces cerevisiae, and in insects, Drosophila S2 cells, only one isoforms of the enzyme was detectable. The ubiquitous occurrence of the two glucosidase II isoforms in mammalian tissues and cell lines might be indicative of a special function of each isoform.</description><subject>alpha-Glucosidases - genetics</subject><subject>alpha-Glucosidases - metabolism</subject><subject>Animals</subject><subject>Cattle</subject><subject>Cell Line</subject><subject>Drosophila</subject><subject>endoplasmic reticulum</subject><subject>enzyme isoforms</subject><subject>Female</subject><subject>Gene Expression Regulation, Developmental</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>glucosidase II</subject><subject>Humans</subject><subject>insect</subject><subject>Isoenzymes - genetics</subject><subject>Isoenzymes - metabolism</subject><subject>Kidney - embryology</subject><subject>Kidney - enzymology</subject><subject>Kidney - growth & development</subject><subject>Liver - embryology</subject><subject>Liver - enzymology</subject><subject>Liver - growth & development</subject><subject>Male</subject><subject>mammalian tissue</subject><subject>Mammals</subject><subject>Mice</subject><subject>N-glycosylation</subject><subject>Organ Specificity</subject><subject>protein quality control</subject><subject>Rats</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>yeast</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kEGP1CAYhonRuOOsV4_KyVvHD0ppOZrJujYZ9bCziZ4IULrBtGXla9X990t3JvEkFwI838ubh5A3DHYMQH6wNrkdB4CdgIY_IxsGCgrOQDwnm3wtC67Y9wvyCvEnAGNCqpfkgjEmecXFhuDxT6Qtxj6mEWns6TGFcQzTHb0eFhcxdAY9bVt69TfgTMNEv5hxNEMwEz0GxMUjNVNH934Y6CFM-WiXmX6NT-wPb_LQ-t5O6N38hOEledGbAf3r874lt5-ujvvPxeHbdbv_eChcKcVcCMd7U1bKgqhr7-uScdGVsq5q5bkyHKxURlrVWOCy4b4BJpxQxijRGW-h3JL3p9z7FH_lorMeA7rcwEw-LqhrqJQs89qS3Ql0KSIm3-v7bMGkB81Ar5r1qlmvmvWqOQ-8PScvdvTdP_zsNQPvTkBvojZ3KaC-veG5YI6oK8bqTDQnwmcDv4NPGl3wk_NdSNmU7mL43--Pw6KT6Q</recordid><startdate>20010112</startdate><enddate>20010112</enddate><creator>Ziak, Martin</creator><creator>Meier, Mirjam</creator><creator>Etter, Kay-Sara</creator><creator>Roth, Jürgen</creator><general>Elsevier Inc</general><scope>FBQ</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>20010112</creationdate><title>Two Isoforms of Trimming Glucosidase II Exist in Mammalian Tissues and Cell Lines but Not in Yeast and Insect Cells</title><author>Ziak, Martin ; Meier, Mirjam ; Etter, Kay-Sara ; Roth, Jürgen</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c364t-4c2fa359b0477ee73124d367579e29a20b69a6b98b02682e8014c49aa94daeb03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>alpha-Glucosidases - genetics</topic><topic>alpha-Glucosidases - metabolism</topic><topic>Animals</topic><topic>Cattle</topic><topic>Cell Line</topic><topic>Drosophila</topic><topic>endoplasmic reticulum</topic><topic>enzyme isoforms</topic><topic>Female</topic><topic>Gene Expression Regulation, Developmental</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>glucosidase II</topic><topic>Humans</topic><topic>insect</topic><topic>Isoenzymes - genetics</topic><topic>Isoenzymes - metabolism</topic><topic>Kidney - embryology</topic><topic>Kidney - enzymology</topic><topic>Kidney - growth & development</topic><topic>Liver - embryology</topic><topic>Liver - enzymology</topic><topic>Liver - growth & development</topic><topic>Male</topic><topic>mammalian tissue</topic><topic>Mammals</topic><topic>Mice</topic><topic>N-glycosylation</topic><topic>Organ Specificity</topic><topic>protein quality control</topic><topic>Rats</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>yeast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ziak, Martin</creatorcontrib><creatorcontrib>Meier, Mirjam</creatorcontrib><creatorcontrib>Etter, Kay-Sara</creatorcontrib><creatorcontrib>Roth, Jürgen</creatorcontrib><collection>AGRIS</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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ziak, Martin</au><au>Meier, Mirjam</au><au>Etter, Kay-Sara</au><au>Roth, Jürgen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Two Isoforms of Trimming Glucosidase II Exist in Mammalian Tissues and Cell Lines but Not in Yeast and Insect Cells</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2001-01-12</date><risdate>2001</risdate><volume>280</volume><issue>1</issue><spage>363</spage><epage>367</epage><pages>363-367</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>We previously cloned glucosidase II and provided in vivo evidence for its involvement in protein folding quality control. DNA-sequencing of different clones demonstrated the existence of two isoforms of glucosidase II which differed by 66 nucleotides due to alternative splicing. The existence of two enzyme isoforms in various organs of pig and rat as well as human, bovine, rat, and mouse cell lines could be demonstrated by RT-PCR and Western blotting. Furthermore, the two isoforms of glucosidase II could be detected in embryonic and postnatal rat kidney and liver. In yeast, Saccharomyces cerevisiae, and in insects, Drosophila S2 cells, only one isoforms of the enzyme was detectable. The ubiquitous occurrence of the two glucosidase II isoforms in mammalian tissues and cell lines might be indicative of a special function of each isoform.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11162524</pmid><doi>10.1006/bbrc.2000.4082</doi><tpages>5</tpages></addata></record> |
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| subjects | alpha-Glucosidases - genetics alpha-Glucosidases - metabolism Animals Cattle Cell Line Drosophila endoplasmic reticulum enzyme isoforms Female Gene Expression Regulation, Developmental Gene Expression Regulation, Enzymologic glucosidase II Humans insect Isoenzymes - genetics Isoenzymes - metabolism Kidney - embryology Kidney - enzymology Kidney - growth & development Liver - embryology Liver - enzymology Liver - growth & development Male mammalian tissue Mammals Mice N-glycosylation Organ Specificity protein quality control Rats Reverse Transcriptase Polymerase Chain Reaction Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology yeast |
| title | Two Isoforms of Trimming Glucosidase II Exist in Mammalian Tissues and Cell Lines but Not in Yeast and Insect Cells |
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