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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
21
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pubmed:dateCreated |
1998-6-25
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pubmed:databankReference | |
pubmed:abstractText |
BLAST analysis of expressed sequence tags (ESTs) using the coding sequence of a human UDP-galactose:beta-N-acetyl-glucosamine beta-1, 3-galactosyltransferase, designated beta3Gal-T1, revealed no ESTs with identical sequences but a large number with similarity. Three different sets of overlapping ESTs with sequence similarities to beta3Gal-T1 were compiled, and complete coding regions of these genes were obtained. Expression of two of these genes in the Baculo virus system showed that one represented a UDP-galactose:beta-N-acetyl-glucosamine beta-1, 3-galactosyltransferase (beta3Gal-T2) with similar kinetic properties as beta3Gal-T1. Another gene represented a UDP-galactose:beta-N-acetyl-galactosamine beta-1, 3-galactosyltransferase (beta3Gal-T4) involved in GM1/GD1 ganglioside synthesis, and this gene was highly similar to a recently reported rat GD1 synthase (Miyazaki, H., Fukumoto, S., Okada, M., Hasegawa, T., and Furukawa, K. (1997) J. Biol. Chem. 272, 24794-24799). Northern analysis of mRNA from human organs with the four homologous cDNA revealed different expression patterns. beta3Gal-T1 mRNA was expressed in brain, beta3Gal-T2 was expressed in brain and heart, and beta3Gal-T3 and -T4 were more widely expressed. The coding regions for each of the four genes were contained in single exons. beta3Gal-T2, -T3, and -T4 were localized to 1q31, 3q25, and 6p21.3, respectively, by EST mapping. The results demonstrate the existence of a family of homologous beta3-galactosyltransferase genes.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author |
pubmed-author:AlmeidaRR,
pubmed-author:AmadoMM,
pubmed-author:BennettE PEP,
pubmed-author:CarneiroFF,
pubmed-author:ClausenHH,
pubmed-author:HassanHH,
pubmed-author:HollingsworthM AMA,
pubmed-author:HolmesE HEH,
pubmed-author:LeveryS BSB,
pubmed-author:NielsenP APA,
pubmed-author:NomotoMM,
pubmed-author:SchwientekTT
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pubmed:issnType |
Print
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pubmed:day |
22
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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 |
12770-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9582303-Amino Acid Sequence,
pubmed-meshheading:9582303-Animals,
pubmed-meshheading:9582303-Carbohydrate Sequence,
pubmed-meshheading:9582303-Cell Line,
pubmed-meshheading:9582303-Chromosome Mapping,
pubmed-meshheading:9582303-Cloning, Molecular,
pubmed-meshheading:9582303-Galactosyltransferases,
pubmed-meshheading:9582303-Humans,
pubmed-meshheading:9582303-Magnetic Resonance Spectroscopy,
pubmed-meshheading:9582303-Molecular Sequence Data,
pubmed-meshheading:9582303-Multigene Family,
pubmed-meshheading:9582303-Rats,
pubmed-meshheading:9582303-Sequence Homology, Amino Acid,
pubmed-meshheading:9582303-Spodoptera
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pubmed:year |
1998
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pubmed:articleTitle |
A family of human beta3-galactosyltransferases. Characterization of four members of a UDP-galactose:beta-N-acetyl-glucosamine/beta-nacetyl-galactosamine beta-1,3-galactosyltransferase family.
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pubmed:affiliation |
School of Dentistry, University of Copenhagen, Norre Allé 20, 2200 Copenhagen N, Denmark.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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