Source:http://linkedlifedata.com/resource/pubmed/id/10101300
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
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| pubmed:dateCreated |
1999-8-5
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| pubmed:databankReference | |
| pubmed:abstractText |
Some alpha(1,3)fucosylated oligosaccharides serve as counter receptors to lectin-like adhesion proteins or are expressed with temporal precision during embryogenesis, and alpha(1, 3)fucosyltransferase is a key enzyme in the production of these oligosaccharides. Two alpha(1,3)-fucosyltransferase genes, designated zFT1 and zFT2, were cloned from zebrafish. Sequence comparisons with other genes indicated that zFT1 and zFT2 share about 30% amino acid sequence identity with human alpha(1, 3)fucosyltransferases. Although the alpha(1,3)fucosyltransferases cloned so far can be classified into three types-myeloid, Lewis, and leukocyte-by virtue of their amino acid sequences, phylogenetic analysis indicated that neither zFT1 nor zFT2 belongs to any of these categories. The expression of zFT1 or zFT2 in mammalian cells induces alpha(1,3)fucosyltransferase activity to synthesize the Lewis x structure from pyridylaminated lacto-N-neotetraose; however, lacto-N-tetraose does not serve as a substrate. Reverse transcriptase-polymerase chain reaction analysis revealed that zFT1 is transcribed during a restricted period before hatching, whereas the mRNA for zFT2 was detected only after hatching.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD15,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Fucosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/galactoside 3-fucosyltransferase
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| pubmed:status |
MEDLINE
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| pubmed:month |
Apr
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| pubmed:issn |
0021-924X
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
125
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
838-45
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| pubmed:dateRevised |
2007-12-19
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| pubmed:meshHeading |
pubmed-meshheading:10101300-Amino Acid Sequence,
pubmed-meshheading:10101300-Animals,
pubmed-meshheading:10101300-Antigens, CD15,
pubmed-meshheading:10101300-Base Sequence,
pubmed-meshheading:10101300-Chromosome Mapping,
pubmed-meshheading:10101300-Cloning, Molecular,
pubmed-meshheading:10101300-DNA,
pubmed-meshheading:10101300-DNA Primers,
pubmed-meshheading:10101300-Fucosyltransferases,
pubmed-meshheading:10101300-Gene Expression Regulation, Developmental,
pubmed-meshheading:10101300-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:10101300-Humans,
pubmed-meshheading:10101300-Molecular Sequence Data,
pubmed-meshheading:10101300-Phylogeny,
pubmed-meshheading:10101300-RNA, Messenger,
pubmed-meshheading:10101300-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:10101300-Sequence Homology, Amino Acid,
pubmed-meshheading:10101300-Species Specificity,
pubmed-meshheading:10101300-Zebrafish
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| pubmed:year |
1999
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| pubmed:articleTitle |
Molecular cloning and characterization of two zebrafish alpha(1,3)fucosyltransferase genes developmentally regulated in embryogenesis.
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| pubmed:affiliation |
Department of Chemistry, Graduate School of Science, Osaka University, Toyonaka, Osaka, 560-0043, Japan.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|