Source:http://linkedlifedata.com/resource/pubmed/id/12417418
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2002-11-5
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pubmed:abstractText |
Beta1,4-N-acetylgalactosaminyltransferase (GM2/GD2 synthase) is a key enzyme which catalyzes the conversion of GM3, GD3 and lactosylceramide (LacCer) to GM2, GD2 and asialo-GM2 (GA2), respectively. This step is critical for the synthesis of all complex gangliosides enriched in the nervous system of vertebrates. Following the cloning of cDNAs encoding GM2/GD2 synthase by an expression cloning approach, substantial evidence for the roles of complex gangliosides have been obtained. Above all, knock-out mice lacking all complex gangliosides revealed important roles of complex gangliosides in vivo, i.e., in the maintenance and repair of nervous tissues, in the intact differentiation of spermatocytes via the transport of testosterone, and in the regulation of interleukin-2 receptor complex. Molecular mechanisms for these functions of complex gangliosides in vivo remain to be clarified.
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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 |
Dec
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
1573
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
356-62
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pubmed:dateRevised |
2005-11-16
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pubmed:meshHeading |
pubmed-meshheading:12417418-Animals,
pubmed-meshheading:12417418-Brain,
pubmed-meshheading:12417418-Gangliosides,
pubmed-meshheading:12417418-Gene Expression,
pubmed-meshheading:12417418-Humans,
pubmed-meshheading:12417418-Mice,
pubmed-meshheading:12417418-Mice, Mutant Strains,
pubmed-meshheading:12417418-N-Acetylgalactosaminyltransferases,
pubmed-meshheading:12417418-Substrate Specificity
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pubmed:year |
2002
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pubmed:articleTitle |
Beta1,4-N-acetylgalactosaminyltransferase--GM2/GD2 synthase: a key enzyme to control the synthesis of brain-enriched complex gangliosides.
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pubmed:affiliation |
Department of Biochemistry II, Nagoya University School of Medicine, 65 Tsurumai, Showa-ku, Nagoya, Japan. koichi@med.nagoya-u.ac.jp
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pubmed:publicationType |
Journal Article,
Review
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