Linked Life Data

6456144

Source:http://linkedlifedata.com/resource/pubmed/id/6456144

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1981-11-18
pubmed:abstractText
Five cell lines of ricin-resistant BHK cells have been assayed for gross carbohydrate analysis of cellular glycoproteins, for the activities of several glycosidases and of specific glycosyl transferases active in assembly of N-glycans of glycoproteins. The latter enzymes include sialyl transferase using asialofetuin as glycosyl acceptor, fucosyl transferases using asialofetuin and asialoagalactofetuin acceptors, galactosyl transferases using ovalbumin, ovomucoid and N-acetylglucosamine as acceptors and N-acetylglucosaminyl transferases using ovalbumin and glycopeptides as acceptors. Cell line RicR14, binding less ricin than normal BHK cells, contains reduced amounts of sialic acid, galactose and N-acetylglucosamine in cellular glycoproteins and lacks almost completely N-acetylglucosamine transferase I, an essential enzyme in assembly of ricin-binding carbohydrate sequences of N-glycans. These cells also contain reduced levels of N-acetylglucosamine transferase II active on a product of N-acetylglucosamine transferase I action. Sialyl transferase activity is severely depressed while fucose-(alpha 1 leads to 6)-N-acetylglucosamine fucosyl transferase activity is increased. Cell lines RicR15, 17, 19 and 21 showed partial deficiencies in galactosyl and N-acetylglucosaminyl transferases. A hypothesis is put forward to account for the different carbohydrate compositions and ricin binding properties of glycoproteins synthesised by these cells in terms of the determined enzyme defects, the normal level of sialyl transferases detected in RicR15 and RicR21 cells and the elevated levels of sialyl and fucosyl transferases detected in RicR17 and 19 cells. None of the above changes in glycosyl transfer reactions in the RicR cell lines are due to enhanced glycosidase or sugar nucleotidase activities in the mutant cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Carbohydrates, http://linkedlifedata.com/resource/pubmed/chemical/Fucosyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Galactosyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Glucosyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Hexosyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylglucosaminyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/N-acetyllactosaminide..., http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides, http://linkedlifedata.com/resource/pubmed/chemical/Ricin, http://linkedlifedata.com/resource/pubmed/chemical/Sialyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Transferases
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
117
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
275-84
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Glycosyl transferases of baby-hamster-kidney (BHK) cells and ricin-resistant mutants. N-glycan biosynthesis.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't