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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1997-9-8
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pubmed:databankReference | |
pubmed:abstractText |
Complementary DNA encoding a human Gal(beta1-3)GalNAc alpha2,3-sialyltransferase type II (hST3Gal II) was cloned from a CEM T-cell cDNA library using a 23-base oligonucleotide probe. The sequence of this probe was established on the basis of a slightly divergent sialylmotif L that was obtained by polymerase chain reaction with degenerate oligonucleotide primers based on the conserved sialylmotif L of mammalian Gal(beta1-3)GalNAc alpha2,3-sialyltransferases. It was thus confirmed that a short oligonucleotide probe may be sensitive and highly specific. The nucleotide and amino acid sequences of hST3Gal II show, respectively, 56.3% and 49.3% similarity to hST3Gal I [Kitagawa, H. & Paulson, J. C. (1994) J. Biol. Chem. 269, 17872-17878] and 88.1% and 93.7% similarity to murine ST3Gal II [Lee, Y. C., Kojima, N., Wada, E., Kurosawa, N., Nakaoka, T., Hamamoto, T. & Tsuji, S. (1994) J. Biol. Chem. 269, 10028-10033]. hST3Gal II mRNA was highly expressed in heart, liver, skeletal muscle and various lymphoid tissues but not in brain and kidney. A soluble form of hST3Gal II expressed in COS-7 cells was tested in vitro for substrate specificity and kinetic properties. Asialofetuin and asialo-bovine submaxillary mucin appeared better substrates for hST3Gal II than for its murine counterpart as previously reported [Kojima, N., Lee, Y.-C., Hamamoto, T., Kurosawa, N. & Tsuji, S. (1994) Biochemistry 33, 5772-5776]. In previous studies, we have shown hyposialylation of O-glycans attached to two major lymphocyte CD43 and CD45 cell surface molecules in human-immunodeficiency-virus-1(HIV-1)-infected T-cell lines. Since comparable levels of hST3Gal I and hST3Gal II mRNA and enzymatic activity were observed in parental and HIV-1-infected CEM T-cell lysates, the sialylation defect associated with HIV infection of this cell line is probably due to a mechanism different from a simple altered catalytic activity of these sialyltransferases.
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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/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/N-acetyllactosaminide...,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sialyltransferases
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
247
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
558-66
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:9266697-Amino Acid Sequence,
pubmed-meshheading:9266697-Animals,
pubmed-meshheading:9266697-Base Sequence,
pubmed-meshheading:9266697-COS Cells,
pubmed-meshheading:9266697-Cell Line,
pubmed-meshheading:9266697-DNA, Complementary,
pubmed-meshheading:9266697-DNA Primers,
pubmed-meshheading:9266697-Humans,
pubmed-meshheading:9266697-Kinetics,
pubmed-meshheading:9266697-Molecular Sequence Data,
pubmed-meshheading:9266697-Organ Specificity,
pubmed-meshheading:9266697-Polymerase Chain Reaction,
pubmed-meshheading:9266697-RNA, Messenger,
pubmed-meshheading:9266697-Recombinant Proteins,
pubmed-meshheading:9266697-Sialyltransferases,
pubmed-meshheading:9266697-T-Lymphocytes,
pubmed-meshheading:9266697-Transfection
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pubmed:year |
1997
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pubmed:articleTitle |
Cloning and expression of cDNA for a human Gal(beta1-3)GalNAc alpha2,3-sialyltransferase from the CEM T-cell line.
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pubmed:affiliation |
Laboratoire de Virologie, Faculté de Médecine, Nice, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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