A novel human UDP- N-acetyl- D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates
A novel member of the human UDP- N-acetyl- D-galactosamine:polypeptide N-acetylgalactosaminyltransferase gene family, designated GalNAc-T7, was cloned and expressed. GalNAc-T7 exhibited different properties compared to other characterized members of this gene family, in showing apparent exclusive sp...
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| Veröffentlicht in: | FEBS letters 1999-10, Vol.460 (2), p.226-230 |
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| creator | Bennett, Eric Paul Hassan, Helle Hollingsworth, Michael A. Clausen, Henrik |
| description | A novel member of the human UDP-
N-acetyl-
D-galactosamine:polypeptide
N-acetylgalactosaminyltransferase gene family, designated GalNAc-T7, was cloned and expressed. GalNAc-T7 exhibited different properties compared to other characterized members of this gene family, in showing apparent exclusive specificity for partially GalNAc-glycosylated acceptor substrates. GalNAc-T7 showed no activity with a large panel of non-glycosylated peptides, but was selectively activated by partial GalNAc glycosylation of peptide substrates derived from the tandem repeats of human MUC2 and rat submaxillary gland mucin. The function of GalNAc-T7 is suggested to be as a follow-up enzyme in the initiation step of
O-glycosylation. |
| doi_str_mv | 10.1016/S0014-5793(99)01268-5 |
| format | Article |
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N-acetyl-
D-galactosamine:polypeptide
N-acetylgalactosaminyltransferase gene family, designated GalNAc-T7, was cloned and expressed. GalNAc-T7 exhibited different properties compared to other characterized members of this gene family, in showing apparent exclusive specificity for partially GalNAc-glycosylated acceptor substrates. GalNAc-T7 showed no activity with a large panel of non-glycosylated peptides, but was selectively activated by partial GalNAc glycosylation of peptide substrates derived from the tandem repeats of human MUC2 and rat submaxillary gland mucin. The function of GalNAc-T7 is suggested to be as a follow-up enzyme in the initiation step of
O-glycosylation.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(99)01268-5</identifier><identifier>PMID: 10544240</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Animals ; Blotting, Northern ; Cloning, Molecular ; DNA, Complementary - metabolism ; EST, expressed sequence tags ; GalNAc, N-acetylgalactosamine ; GalNAc-transferase ; GalNAc-transferase, UDP-GalNAc:polypeptide αGalNAc-transferase (EC 2.4.1.41) ; Glycosylation ; Glycosyltransferase ; Humans ; Isoenzymes ; Kinetics ; Molecular Sequence Data ; Mucin ; N-Acetylgalactosaminyltransferases - isolation & purification ; N-Acetylgalactosaminyltransferases - metabolism ; O-Glycosylation ; Peptides - chemistry ; Peptides - metabolism ; RACE, rapid amplification of cDNA ends ; Rats ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Substrate Specificity ; Tissue Distribution ; Uridine Diphosphate - chemistry ; Uridine Diphosphate - metabolism</subject><ispartof>FEBS letters, 1999-10, Vol.460 (2), p.226-230</ispartof><rights>1999 Federation of European Biochemical Societies</rights><rights>FEBS Letters 460 (1999) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4735-67b70ebb74bfdd7d07bdda9e5cd4e652a393bc481a487fff7d5cba9cf412647b3</citedby><cites>FETCH-LOGICAL-c4735-67b70ebb74bfdd7d07bdda9e5cd4e652a393bc481a487fff7d5cba9cf412647b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2899%2901268-5$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0014-5793(99)01268-5$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1416,1432,3548,27922,27923,45572,45573,45993,46407,46831</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10544240$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bennett, Eric Paul</creatorcontrib><creatorcontrib>Hassan, Helle</creatorcontrib><creatorcontrib>Hollingsworth, Michael A.</creatorcontrib><creatorcontrib>Clausen, Henrik</creatorcontrib><title>A novel human UDP- N-acetyl- D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>A novel member of the human UDP-
N-acetyl-
D-galactosamine:polypeptide
N-acetylgalactosaminyltransferase gene family, designated GalNAc-T7, was cloned and expressed. GalNAc-T7 exhibited different properties compared to other characterized members of this gene family, in showing apparent exclusive specificity for partially GalNAc-glycosylated acceptor substrates. GalNAc-T7 showed no activity with a large panel of non-glycosylated peptides, but was selectively activated by partial GalNAc glycosylation of peptide substrates derived from the tandem repeats of human MUC2 and rat submaxillary gland mucin. The function of GalNAc-T7 is suggested to be as a follow-up enzyme in the initiation step of
O-glycosylation.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Blotting, Northern</subject><subject>Cloning, Molecular</subject><subject>DNA, Complementary - metabolism</subject><subject>EST, expressed sequence tags</subject><subject>GalNAc, N-acetylgalactosamine</subject><subject>GalNAc-transferase</subject><subject>GalNAc-transferase, UDP-GalNAc:polypeptide αGalNAc-transferase (EC 2.4.1.41)</subject><subject>Glycosylation</subject><subject>Glycosyltransferase</subject><subject>Humans</subject><subject>Isoenzymes</subject><subject>Kinetics</subject><subject>Molecular Sequence Data</subject><subject>Mucin</subject><subject>N-Acetylgalactosaminyltransferases - isolation & purification</subject><subject>N-Acetylgalactosaminyltransferases - metabolism</subject><subject>O-Glycosylation</subject><subject>Peptides - chemistry</subject><subject>Peptides - metabolism</subject><subject>RACE, rapid amplification of cDNA ends</subject><subject>Rats</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Substrate Specificity</subject><subject>Tissue Distribution</subject><subject>Uridine Diphosphate - chemistry</subject><subject>Uridine Diphosphate - metabolism</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1u1TAQhS0EopfCI4C8QiDV4CR2HLNBl_4iVQWJdm059rg18k2C7bTKM_GS5N6UqjtYjTzzzTnWHIReF_RDQYv64w9KC0a4kNU7Kd_Toqwbwp-gVdGIilSsbp6i1QOyh16k9JPO76aQz9FeQTljJaMr9HuNu_4WAr4ZN7rDV0ffCb4g2kCeAsFH5FoHbXKf9MZ38GnowzTAkL2FB-oxMYUcdZccRJ3gAJ_qcLE25FIc4Dufb3AawHjnjc8Tdn3Eg47Z6_CXuw6T6dMUdAaLtTGz0QylsU2zaob0Ej1zOiR4dV_30dXJ8eXhGTn_dvr1cH1ODBMVJ7VoBYW2Fax11gpLRWutlsCNZVDzUleyag1rCs0a4ZwTlptWS-PYfEQm2mofvV10h9j_GiFltfHJQAi6g35MqpZlyXhJZ5AvoIl9ShGcGqLf6DipgqptSmqXktpGoKRUu5QUn_fe3BuM7Qbso60llhk4W4A7H2D6P1V1cvyl3E22Ayl37a3X50UK5ovdeogqGQ-dAesjmKxs7__x2z9yMLoO</recordid><startdate>19991029</startdate><enddate>19991029</enddate><creator>Bennett, Eric Paul</creator><creator>Hassan, Helle</creator><creator>Hollingsworth, Michael A.</creator><creator>Clausen, Henrik</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>19991029</creationdate><title>A novel human UDP- N-acetyl- D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates</title><author>Bennett, Eric Paul ; Hassan, Helle ; Hollingsworth, Michael A. ; Clausen, Henrik</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4735-67b70ebb74bfdd7d07bdda9e5cd4e652a393bc481a487fff7d5cba9cf412647b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Blotting, Northern</topic><topic>Cloning, Molecular</topic><topic>DNA, Complementary - metabolism</topic><topic>EST, expressed sequence tags</topic><topic>GalNAc, N-acetylgalactosamine</topic><topic>GalNAc-transferase</topic><topic>GalNAc-transferase, UDP-GalNAc:polypeptide αGalNAc-transferase (EC 2.4.1.41)</topic><topic>Glycosylation</topic><topic>Glycosyltransferase</topic><topic>Humans</topic><topic>Isoenzymes</topic><topic>Kinetics</topic><topic>Molecular Sequence Data</topic><topic>Mucin</topic><topic>N-Acetylgalactosaminyltransferases - isolation & purification</topic><topic>N-Acetylgalactosaminyltransferases - metabolism</topic><topic>O-Glycosylation</topic><topic>Peptides - chemistry</topic><topic>Peptides - metabolism</topic><topic>RACE, rapid amplification of cDNA ends</topic><topic>Rats</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Substrate Specificity</topic><topic>Tissue Distribution</topic><topic>Uridine Diphosphate - chemistry</topic><topic>Uridine Diphosphate - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bennett, Eric Paul</creatorcontrib><creatorcontrib>Hassan, Helle</creatorcontrib><creatorcontrib>Hollingsworth, Michael A.</creatorcontrib><creatorcontrib>Clausen, Henrik</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bennett, Eric Paul</au><au>Hassan, Helle</au><au>Hollingsworth, Michael A.</au><au>Clausen, Henrik</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel human UDP- N-acetyl- D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1999-10-29</date><risdate>1999</risdate><volume>460</volume><issue>2</issue><spage>226</spage><epage>230</epage><pages>226-230</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>A novel member of the human UDP-
N-acetyl-
D-galactosamine:polypeptide
N-acetylgalactosaminyltransferase gene family, designated GalNAc-T7, was cloned and expressed. GalNAc-T7 exhibited different properties compared to other characterized members of this gene family, in showing apparent exclusive specificity for partially GalNAc-glycosylated acceptor substrates. GalNAc-T7 showed no activity with a large panel of non-glycosylated peptides, but was selectively activated by partial GalNAc glycosylation of peptide substrates derived from the tandem repeats of human MUC2 and rat submaxillary gland mucin. The function of GalNAc-T7 is suggested to be as a follow-up enzyme in the initiation step of
O-glycosylation.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>10544240</pmid><doi>10.1016/S0014-5793(99)01268-5</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 1999-10, Vol.460 (2), p.226-230 |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Wiley Free Content; EZB-FREE-00999 freely available EZB journals; Wiley Online Library All Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Blotting, Northern Cloning, Molecular DNA, Complementary - metabolism EST, expressed sequence tags GalNAc, N-acetylgalactosamine GalNAc-transferase GalNAc-transferase, UDP-GalNAc:polypeptide αGalNAc-transferase (EC 2.4.1.41) Glycosylation Glycosyltransferase Humans Isoenzymes Kinetics Molecular Sequence Data Mucin N-Acetylgalactosaminyltransferases - isolation & purification N-Acetylgalactosaminyltransferases - metabolism O-Glycosylation Peptides - chemistry Peptides - metabolism RACE, rapid amplification of cDNA ends Rats Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Substrate Specificity Tissue Distribution Uridine Diphosphate - chemistry Uridine Diphosphate - metabolism |
| title | A novel human UDP- N-acetyl- D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates |
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