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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
1980-1-24
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pubmed:abstractText |
Four different glycolipid:glycosyltransferase activities involved in the biosynthesis in vitro of gangliosides and blood group-related glycosphingolipids have been tested in a simian virus 40-transformed glial cell culture derived from the cerebrum of a fetus with Tay-Sachs disease (TSD). The TSD cultured brain cells contained little activity of either UDP-Gal:GM2(beta 1-3)galactosyltransferase (GalT-3; EC 2.4.1.62), which catalyzes the formation of GM1a from GM2 (tay-Sachs) ganglioside, or GDP-Fuc:nLcOse4Cer (alpha 1-2)fucosyltransferase (FucT-2; EC 2.4.1.89), which catalyzes the formation of H1 glycolipid from nLcOse4Cer. These cells contained a potent inhibitor of the second reaction (catalyzed by a Golgi-rich membrane fraction from bovine spleen), whereas no inhibition of the first reaction (catalyzed by a membrane fraction from 14-day-old embryonic chicken brain) was observed. The activity of UDP-Gal:LcOse3Cer(beta 1-4)galactosyltransferase (GalT-4; EC 2.4.1.86) was 30- to 80-fold higher than the activity of GalT-3. The presence of CMP-AcNeu:nLcOse4Cer sialyltransferase activity and the absence of either GalT-3 or FucT-2 suggested a probable pathway for the synthesis of sialylneolactotetraosylceramide [GM1b(GlcNAc)] in addition to a specific blockage of GM1a ganglioside synthesis from GM2 in these TSD transformed cells.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-13979552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-14564716,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-14907713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-272643,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-4237219,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-4288894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-4334559,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-4335001,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-4364825,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-4611525,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-4631392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-4632915,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-5031784,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-5057092,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-5090043,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-5793973,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-5842076,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-5972561,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-618873,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-652414,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-804484,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-937117,
http://linkedlifedata.com/resource/pubmed/commentcorrection/291963-953690
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
76
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4270-4
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:291963-ABO Blood-Group System,
pubmed-meshheading:291963-Brain,
pubmed-meshheading:291963-Fucosyltransferases,
pubmed-meshheading:291963-G(M1) Ganglioside,
pubmed-meshheading:291963-Galactosyltransferases,
pubmed-meshheading:291963-Gangliosides,
pubmed-meshheading:291963-Glycosphingolipids,
pubmed-meshheading:291963-Humans,
pubmed-meshheading:291963-Neuroglia,
pubmed-meshheading:291963-Sialyltransferases,
pubmed-meshheading:291963-Tay-Sachs Disease
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pubmed:year |
1979
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pubmed:articleTitle |
Differential activities of glycolipid glycosyltransferases in Tay-Sachs disease: studies in cultured cells from cerebrum.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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