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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
1998-4-16
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pubmed:databankReference | |
pubmed:abstractText |
We isolated a cDNA encoding a novel glucuronyltransferase from human placenta cDNA with the use of the degenerate reverse transcriptase-polymerase chain reaction method. Degenerate primers were designed based upon the amino acid sequence alignment of rat glucuronyltransferase (GlcAT-P) involved in the biosynthesis of the carbohydrate epitope HNK-1 with putative proteins in Caenorhabditis elegans and Schistosoma mansoni. The new cDNA sequence revealed an open reading frame coding for a protein of 335 amino acids with a type II transmembrane protein topology. The amino acid sequence displayed 43% identity to the rat GlcAT-P, and the highest sequence identity was found in the COOH-terminal catalytic domain. The expression of a soluble recombinant form of the protein in COS-1 cells produced an active glucuronyltransferase with marked specificity for a glycoserine Galbeta1-3Galbeta1-4Xylbeta1-O-Ser. In contrast, asialoorosomucoid, which contains the Galbeta1-4GlcNAc sequence and is a good acceptor substrate for the GlcAT-P, did not serve as an acceptor. The reaction product was sensitive to beta-glucuronidase digestion and co-chromatographed with authentic GlcAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser in high-performance liquid chromatography, suggesting that the enzyme is a beta1, 3-glucuronyltransferase. These results indicate that this new member of the glucuronyltransferase gene family is the enzyme previously described as glucuronyltransferase I that forms the glycosaminoglycan-protein linkage region, GlcAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser, of proteoglycans.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Glucuronosyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosaminoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Hexosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6615-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9506957-Amino Acid Sequence,
pubmed-meshheading:9506957-Animals,
pubmed-meshheading:9506957-Base Sequence,
pubmed-meshheading:9506957-Binding Sites,
pubmed-meshheading:9506957-Carbohydrate Sequence,
pubmed-meshheading:9506957-Chromatography, High Pressure Liquid,
pubmed-meshheading:9506957-Cloning, Molecular,
pubmed-meshheading:9506957-DNA, Complementary,
pubmed-meshheading:9506957-Glucuronosyltransferase,
pubmed-meshheading:9506957-Glycosaminoglycans,
pubmed-meshheading:9506957-Hexosyltransferases,
pubmed-meshheading:9506957-Humans,
pubmed-meshheading:9506957-Molecular Sequence Data,
pubmed-meshheading:9506957-Polymerase Chain Reaction,
pubmed-meshheading:9506957-Proteoglycans,
pubmed-meshheading:9506957-Rats,
pubmed-meshheading:9506957-Sequence Homology, Amino Acid
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pubmed:year |
1998
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pubmed:articleTitle |
Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans.
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pubmed:affiliation |
Department of Biochemistry, Kobe Pharmaceutical University, Higashinada-ku, Kobe 658, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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