Transient expression of wild-type and mutant glucocerebrosidases in hybrid vaccinia expression system
Gaucher disease, the most prevalent lysosomal storage disease, is characterised by a significant phenotypic variation caused by more than 150 mutations. In order to verify pathogenicity of mutations found in the Czech Gaucher population, the vaccinia expression system was used. The wild-type human β...
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| Veröffentlicht in: | European journal of human genetics : EJHG 2003-05, Vol.11 (5), p.369-374 |
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| creator | Hodaňová, Kateřina Mělková, Zora Horowitz, Mia Hřebíček, Martin |
| description | Gaucher disease, the most prevalent lysosomal storage disease, is characterised by a significant phenotypic variation caused by more than 150 mutations. In order to verify pathogenicity of mutations found in the Czech Gaucher population, the vaccinia expression system was used. The wild-type human
β
-glucocerebrosidase cDNA and cDNAs carrying the mutations 72delC, 1326insT, 1263del55, S196P, N370S, L444P, G202E, D409H, T369M, L444P+V460V, and D409H+T369M were expressed in Gaucher fibroblast cell line (L444P/S107L), BSC40, and HeLa G cells. The enzymatic activity and immunological reactivity were analysed. Only
β
-glucocerebrosidase-deficient fibroblasts were suitable for expression using plasmid transfection. The expressed
β
-glucosidase activity of mutant glucocerebrosidases was in good correlation with the presumed severity of the mutations. |
| doi_str_mv | 10.1038/sj.ejhg.5200974 |
| format | Article |
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β
-glucocerebrosidase cDNA and cDNAs carrying the mutations 72delC, 1326insT, 1263del55, S196P, N370S, L444P, G202E, D409H, T369M, L444P+V460V, and D409H+T369M were expressed in Gaucher fibroblast cell line (L444P/S107L), BSC40, and HeLa G cells. The enzymatic activity and immunological reactivity were analysed. Only
β
-glucocerebrosidase-deficient fibroblasts were suitable for expression using plasmid transfection. The expressed
β
-glucosidase activity of mutant glucocerebrosidases was in good correlation with the presumed severity of the mutations.</description><identifier>ISSN: 1018-4813</identifier><identifier>EISSN: 1476-5438</identifier><identifier>DOI: 10.1038/sj.ejhg.5200974</identifier><identifier>PMID: 12734541</identifier><language>eng</language><publisher>Cham: Springer International Publishing</publisher><subject>Bioinformatics ; Biological and medical sciences ; Biomedical and Life Sciences ; Biomedicine ; Cloning, Molecular ; Cytogenetics ; Deoxyribonucleic acid ; DNA ; Enzymatic activity ; Errors of metabolism ; Fibroblasts ; Gaucher Disease - enzymology ; Gaucher's disease ; Gene Expression ; Genetic Vectors ; Genomics ; Glucosylceramidase ; Glucosylceramidase - biosynthesis ; Glucosylceramidase - genetics ; HeLa Cells ; Human Genetics ; Humans ; Immunology ; Kinases ; Lipids (lysosomal enzyme disorders, storage diseases) ; Medical sciences ; Metabolic diseases ; Mutagenesis, Site-Directed ; Mutation ; Pathogenicity ; Phenotypic variations ; Proteins ; RNA polymerase ; Transfection ; Vaccinia ; Vaccinia virus ; Viruses</subject><ispartof>European journal of human genetics : EJHG, 2003-05, Vol.11 (5), p.369-374</ispartof><rights>Springer Nature Switzerland AG 2003</rights><rights>2003 INIST-CNRS</rights><rights>Copyright Nature Publishing Group May 2003</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c463t-7ac817ba0089ae734e0ab3bf76ac21479ad2751f866b9aa22b832b224eefed623</citedby><cites>FETCH-LOGICAL-c463t-7ac817ba0089ae734e0ab3bf76ac21479ad2751f866b9aa22b832b224eefed623</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/sj.ejhg.5200974$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/sj.ejhg.5200974$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14793862$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12734541$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hodaňová, Kateřina</creatorcontrib><creatorcontrib>Mělková, Zora</creatorcontrib><creatorcontrib>Horowitz, Mia</creatorcontrib><creatorcontrib>Hřebíček, Martin</creatorcontrib><title>Transient expression of wild-type and mutant glucocerebrosidases in hybrid vaccinia expression system</title><title>European journal of human genetics : EJHG</title><addtitle>Eur J Hum Genet</addtitle><addtitle>Eur J Hum Genet</addtitle><description>Gaucher disease, the most prevalent lysosomal storage disease, is characterised by a significant phenotypic variation caused by more than 150 mutations. In order to verify pathogenicity of mutations found in the Czech Gaucher population, the vaccinia expression system was used. The wild-type human
β
-glucocerebrosidase cDNA and cDNAs carrying the mutations 72delC, 1326insT, 1263del55, S196P, N370S, L444P, G202E, D409H, T369M, L444P+V460V, and D409H+T369M were expressed in Gaucher fibroblast cell line (L444P/S107L), BSC40, and HeLa G cells. The enzymatic activity and immunological reactivity were analysed. Only
β
-glucocerebrosidase-deficient fibroblasts were suitable for expression using plasmid transfection. The expressed
β
-glucosidase activity of mutant glucocerebrosidases was in good correlation with the presumed severity of the mutations.</description><subject>Bioinformatics</subject><subject>Biological and medical sciences</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cloning, Molecular</subject><subject>Cytogenetics</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>Enzymatic activity</subject><subject>Errors of metabolism</subject><subject>Fibroblasts</subject><subject>Gaucher Disease - enzymology</subject><subject>Gaucher's disease</subject><subject>Gene Expression</subject><subject>Genetic Vectors</subject><subject>Genomics</subject><subject>Glucosylceramidase</subject><subject>Glucosylceramidase - biosynthesis</subject><subject>Glucosylceramidase - genetics</subject><subject>HeLa Cells</subject><subject>Human Genetics</subject><subject>Humans</subject><subject>Immunology</subject><subject>Kinases</subject><subject>Lipids (lysosomal enzyme disorders, storage diseases)</subject><subject>Medical sciences</subject><subject>Metabolic diseases</subject><subject>Mutagenesis, Site-Directed</subject><subject>Mutation</subject><subject>Pathogenicity</subject><subject>Phenotypic variations</subject><subject>Proteins</subject><subject>RNA polymerase</subject><subject>Transfection</subject><subject>Vaccinia</subject><subject>Vaccinia virus</subject><subject>Viruses</subject><issn>1018-4813</issn><issn>1476-5438</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp1kM1v1DAQxS0EoqVw5oYiJLhl648kdo6o4kuqxKWcrbEz2TpKnMWTUPa_x2UjLULiNJbm5zfvPcZeC74TXJlrGnY43O93teS81dUTdikq3ZR1pczT_ObClJUR6oK9IBo4z0stnrMLIbWq6kpcMrxLEClgXAr8dUhIFOZYzH3xEMauXI4HLCB2xbQukJH9uPrZY0KXZgodEFIRYnF_dCl0xU_wPsQAfyvRkRacXrJnPYyEr7Z5xb5_-nh386W8_fb5682H29JXjVpKDd4I7YBz0wJmi8jBKdfrBrzM3lvopK5Fb5rGtQBSOqOkk7JC7LFrpLpi70-6hzT_WJEWOwXyOI4QcV7JCmOU0LXJ4Nt_wGFeU8zerBTaKGXaJkPXJ8jntJSwt4cUJkhHK7h9rN_SYB_rt1v9-cebTXZ1E3Znfus7A-82AMjD2OfyfaAzlzMq8ycIP3GUV3GP6ezvf7d_A76foOI</recordid><startdate>20030501</startdate><enddate>20030501</enddate><creator>Hodaňová, Kateřina</creator><creator>Mělková, Zora</creator><creator>Horowitz, Mia</creator><creator>Hřebíček, Martin</creator><general>Springer International Publishing</general><general>Nature Publishing</general><general>Nature Publishing Group</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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>7TM</scope></search><sort><creationdate>20030501</creationdate><title>Transient expression of wild-type and mutant glucocerebrosidases in hybrid vaccinia expression system</title><author>Hodaňová, Kateřina ; Mělková, Zora ; Horowitz, Mia ; Hřebíček, Martin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c463t-7ac817ba0089ae734e0ab3bf76ac21479ad2751f866b9aa22b832b224eefed623</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Bioinformatics</topic><topic>Biological and medical sciences</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Cloning, Molecular</topic><topic>Cytogenetics</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>Enzymatic activity</topic><topic>Errors of metabolism</topic><topic>Fibroblasts</topic><topic>Gaucher Disease - enzymology</topic><topic>Gaucher's disease</topic><topic>Gene Expression</topic><topic>Genetic Vectors</topic><topic>Genomics</topic><topic>Glucosylceramidase</topic><topic>Glucosylceramidase - biosynthesis</topic><topic>Glucosylceramidase - genetics</topic><topic>HeLa Cells</topic><topic>Human Genetics</topic><topic>Humans</topic><topic>Immunology</topic><topic>Kinases</topic><topic>Lipids (lysosomal enzyme disorders, storage diseases)</topic><topic>Medical sciences</topic><topic>Metabolic diseases</topic><topic>Mutagenesis, Site-Directed</topic><topic>Mutation</topic><topic>Pathogenicity</topic><topic>Phenotypic variations</topic><topic>Proteins</topic><topic>RNA polymerase</topic><topic>Transfection</topic><topic>Vaccinia</topic><topic>Vaccinia virus</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hodaňová, Kateřina</creatorcontrib><creatorcontrib>Mělková, Zora</creatorcontrib><creatorcontrib>Horowitz, Mia</creatorcontrib><creatorcontrib>Hřebíček, Martin</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>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Genetics Abstracts</collection><collection>Nucleic Acids Abstracts</collection><jtitle>European journal of human genetics : EJHG</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hodaňová, Kateřina</au><au>Mělková, Zora</au><au>Horowitz, Mia</au><au>Hřebíček, Martin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Transient expression of wild-type and mutant glucocerebrosidases in hybrid vaccinia expression system</atitle><jtitle>European journal of human genetics : EJHG</jtitle><stitle>Eur J Hum Genet</stitle><addtitle>Eur J Hum Genet</addtitle><date>2003-05-01</date><risdate>2003</risdate><volume>11</volume><issue>5</issue><spage>369</spage><epage>374</epage><pages>369-374</pages><issn>1018-4813</issn><eissn>1476-5438</eissn><abstract>Gaucher disease, the most prevalent lysosomal storage disease, is characterised by a significant phenotypic variation caused by more than 150 mutations. In order to verify pathogenicity of mutations found in the Czech Gaucher population, the vaccinia expression system was used. The wild-type human
β
-glucocerebrosidase cDNA and cDNAs carrying the mutations 72delC, 1326insT, 1263del55, S196P, N370S, L444P, G202E, D409H, T369M, L444P+V460V, and D409H+T369M were expressed in Gaucher fibroblast cell line (L444P/S107L), BSC40, and HeLa G cells. The enzymatic activity and immunological reactivity were analysed. Only
β
-glucocerebrosidase-deficient fibroblasts were suitable for expression using plasmid transfection. The expressed
β
-glucosidase activity of mutant glucocerebrosidases was in good correlation with the presumed severity of the mutations.</abstract><cop>Cham</cop><pub>Springer International Publishing</pub><pmid>12734541</pmid><doi>10.1038/sj.ejhg.5200974</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Bioinformatics Biological and medical sciences Biomedical and Life Sciences Biomedicine Cloning, Molecular Cytogenetics Deoxyribonucleic acid DNA Enzymatic activity Errors of metabolism Fibroblasts Gaucher Disease - enzymology Gaucher's disease Gene Expression Genetic Vectors Genomics Glucosylceramidase Glucosylceramidase - biosynthesis Glucosylceramidase - genetics HeLa Cells Human Genetics Humans Immunology Kinases Lipids (lysosomal enzyme disorders, storage diseases) Medical sciences Metabolic diseases Mutagenesis, Site-Directed Mutation Pathogenicity Phenotypic variations Proteins RNA polymerase Transfection Vaccinia Vaccinia virus Viruses |
| title | Transient expression of wild-type and mutant glucocerebrosidases in hybrid vaccinia expression system |
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