Novel induction of alpha-lactalbumin-mediated lacdiNAc-R expression in vivo
alpha-Lactalbumin (alpha-LA) is a regulatory protein by which the mammalian beta1,4-galactosyltransferase (beta1,4-galT) is induced to utilize glucose as an acceptor instead of N-acetylglucosamine (GlcNAc) during lactose synthesis in mammary gland. alpha-LA can also modulate beta1,4-galT to utilize...
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| Veröffentlicht in: | Biochemical journal 2000-05, Vol.348 Pt 1 (1), p.229-234 |
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| creator | Do, S I Lee, K Y Kim, H N |
| description | alpha-Lactalbumin (alpha-LA) is a regulatory protein by which the mammalian beta1,4-galactosyltransferase (beta1,4-galT) is induced to utilize glucose as an acceptor instead of N-acetylglucosamine (GlcNAc) during lactose synthesis in mammary gland. alpha-LA can also modulate beta1,4-galT to utilize UDP-N-acetylgalactosamine (UDP-GalNAc) as a donor towards GlcNAc acceptor substrate with high efficiency in vitro [Do, Do and Cummings (1995) J. Biol. Chem. 270, 18447-18451]. In the present study we transfected cDNA encoding bovine alpha-LA into Lec8 cells and examined whether nucleotide sugar switching of UDP-galactose (UDP-Gal) into UDP-GalNAc occurred in vivo and whether the neo-glycosylation of GalNAcbeta1,4GlcNAc-R structure was synthesized in alpha-LA-stable transfectants. Our studies demonstrate that the stable expression of alpha-LA in Lec8 cells induces the formation of GalNAcbeta1,4GlcNAc-R in vivo through the nucleotide sugar switching of beta1,4-galT. |
| doi_str_mv | 10.1042/0264-6021:3480229 |
| format | Article |
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Biol. Chem. 270, 18447-18451]. In the present study we transfected cDNA encoding bovine alpha-LA into Lec8 cells and examined whether nucleotide sugar switching of UDP-galactose (UDP-Gal) into UDP-GalNAc occurred in vivo and whether the neo-glycosylation of GalNAcbeta1,4GlcNAc-R structure was synthesized in alpha-LA-stable transfectants. Our studies demonstrate that the stable expression of alpha-LA in Lec8 cells induces the formation of GalNAcbeta1,4GlcNAc-R in vivo through the nucleotide sugar switching of beta1,4-galT.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/0264-6021:3480229</identifier><identifier>PMID: 10794736</identifier><language>eng</language><publisher>England</publisher><subject>Amidohydrolases - metabolism ; Animals ; Biomarkers, Tumor - metabolism ; Cattle ; Cells, Cultured ; CHO Cells ; Cricetinae ; Disaccharides - metabolism ; Glucosamine - metabolism ; Glycopeptides - analysis ; Immunoblotting ; Lactalbumin - genetics ; Lactalbumin - metabolism ; Lactose - analogs & derivatives ; Lactose - metabolism ; N-Acetylgalactosaminyltransferases ; Oligopeptides - metabolism ; Oligosaccharides - metabolism ; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase ; Reverse Transcriptase Polymerase Chain Reaction ; Transfection ; Tritium</subject><ispartof>Biochemical journal, 2000-05, Vol.348 Pt 1 (1), p.229-234</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1221058/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1221058/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27923,27924,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10794736$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Do, S I</creatorcontrib><creatorcontrib>Lee, K Y</creatorcontrib><creatorcontrib>Kim, H N</creatorcontrib><title>Novel induction of alpha-lactalbumin-mediated lacdiNAc-R expression in vivo</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>alpha-Lactalbumin (alpha-LA) is a regulatory protein by which the mammalian beta1,4-galactosyltransferase (beta1,4-galT) is induced to utilize glucose as an acceptor instead of N-acetylglucosamine (GlcNAc) during lactose synthesis in mammary gland. alpha-LA can also modulate beta1,4-galT to utilize UDP-N-acetylgalactosamine (UDP-GalNAc) as a donor towards GlcNAc acceptor substrate with high efficiency in vitro [Do, Do and Cummings (1995) J. Biol. Chem. 270, 18447-18451]. In the present study we transfected cDNA encoding bovine alpha-LA into Lec8 cells and examined whether nucleotide sugar switching of UDP-galactose (UDP-Gal) into UDP-GalNAc occurred in vivo and whether the neo-glycosylation of GalNAcbeta1,4GlcNAc-R structure was synthesized in alpha-LA-stable transfectants. Our studies demonstrate that the stable expression of alpha-LA in Lec8 cells induces the formation of GalNAcbeta1,4GlcNAc-R in vivo through the nucleotide sugar switching of beta1,4-galT.</description><subject>Amidohydrolases - metabolism</subject><subject>Animals</subject><subject>Biomarkers, Tumor - metabolism</subject><subject>Cattle</subject><subject>Cells, Cultured</subject><subject>CHO Cells</subject><subject>Cricetinae</subject><subject>Disaccharides - metabolism</subject><subject>Glucosamine - metabolism</subject><subject>Glycopeptides - analysis</subject><subject>Immunoblotting</subject><subject>Lactalbumin - genetics</subject><subject>Lactalbumin - metabolism</subject><subject>Lactose - analogs & derivatives</subject><subject>Lactose - metabolism</subject><subject>N-Acetylgalactosaminyltransferases</subject><subject>Oligopeptides - metabolism</subject><subject>Oligosaccharides - metabolism</subject><subject>Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>Transfection</subject><subject>Tritium</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUU1LxDAUDKK46-oP8CI9eau-fLRJPQjL4hcuK4ieQ5ombqRt1qYt-u9t2WXR04P3ZuYNMwidY7jCwMg1kJTFKRB8Q5kAQrIDNMWMQyw4EYdour9P0EkInwCYAYNjNMHAM8ZpOkXPK9-bMnJ10enW-TryNlLlZq3iUulWlXlXuTquTOFUa4poWBZuNdfxa2S-N40JYeS4Oupd70_RkVVlMGe7OUPv93dvi8d4-fLwtJgvY00Zb-OUWEtNoXnCKOZpAlbodHCsLdOUsKwAwYzFuRYGK8ZYJvJcaZKJgkJiVEFn6Haru-nywZk2dduoUm4aV6nmR3rl5P9L7dbyw_cSE4IhEYPA5U6g8V-dCa2sXNCmLFVtfBckxzD4IWQA4i1QNz6Extj9EwxyrECOEcsxYrmrYOBc_HX3h7HNnP4CkEGCqA</recordid><startdate>20000515</startdate><enddate>20000515</enddate><creator>Do, S I</creator><creator>Lee, K Y</creator><creator>Kim, H N</creator><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><scope>5PM</scope></search><sort><creationdate>20000515</creationdate><title>Novel induction of alpha-lactalbumin-mediated lacdiNAc-R expression in vivo</title><author>Do, S I ; Lee, K Y ; Kim, H N</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c347t-62ff3edc754317650f8c6872cf4c3249d084ef1bc8e1a44498bbac298d305ead3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amidohydrolases - metabolism</topic><topic>Animals</topic><topic>Biomarkers, Tumor - metabolism</topic><topic>Cattle</topic><topic>Cells, Cultured</topic><topic>CHO Cells</topic><topic>Cricetinae</topic><topic>Disaccharides - metabolism</topic><topic>Glucosamine - metabolism</topic><topic>Glycopeptides - analysis</topic><topic>Immunoblotting</topic><topic>Lactalbumin - genetics</topic><topic>Lactalbumin - metabolism</topic><topic>Lactose - analogs & derivatives</topic><topic>Lactose - metabolism</topic><topic>N-Acetylgalactosaminyltransferases</topic><topic>Oligopeptides - metabolism</topic><topic>Oligosaccharides - metabolism</topic><topic>Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>Transfection</topic><topic>Tritium</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Do, S I</creatorcontrib><creatorcontrib>Lee, K Y</creatorcontrib><creatorcontrib>Kim, H N</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Do, S I</au><au>Lee, K Y</au><au>Kim, H N</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Novel induction of alpha-lactalbumin-mediated lacdiNAc-R expression in vivo</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>2000-05-15</date><risdate>2000</risdate><volume>348 Pt 1</volume><issue>1</issue><spage>229</spage><epage>234</epage><pages>229-234</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>alpha-Lactalbumin (alpha-LA) is a regulatory protein by which the mammalian beta1,4-galactosyltransferase (beta1,4-galT) is induced to utilize glucose as an acceptor instead of N-acetylglucosamine (GlcNAc) during lactose synthesis in mammary gland. alpha-LA can also modulate beta1,4-galT to utilize UDP-N-acetylgalactosamine (UDP-GalNAc) as a donor towards GlcNAc acceptor substrate with high efficiency in vitro [Do, Do and Cummings (1995) J. Biol. Chem. 270, 18447-18451]. In the present study we transfected cDNA encoding bovine alpha-LA into Lec8 cells and examined whether nucleotide sugar switching of UDP-galactose (UDP-Gal) into UDP-GalNAc occurred in vivo and whether the neo-glycosylation of GalNAcbeta1,4GlcNAc-R structure was synthesized in alpha-LA-stable transfectants. Our studies demonstrate that the stable expression of alpha-LA in Lec8 cells induces the formation of GalNAcbeta1,4GlcNAc-R in vivo through the nucleotide sugar switching of beta1,4-galT.</abstract><cop>England</cop><pmid>10794736</pmid><doi>10.1042/0264-6021:3480229</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Amidohydrolases - metabolism Animals Biomarkers, Tumor - metabolism Cattle Cells, Cultured CHO Cells Cricetinae Disaccharides - metabolism Glucosamine - metabolism Glycopeptides - analysis Immunoblotting Lactalbumin - genetics Lactalbumin - metabolism Lactose - analogs & derivatives Lactose - metabolism N-Acetylgalactosaminyltransferases Oligopeptides - metabolism Oligosaccharides - metabolism Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Reverse Transcriptase Polymerase Chain Reaction Transfection Tritium |
| title | Novel induction of alpha-lactalbumin-mediated lacdiNAc-R expression in vivo |
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