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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
27
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pubmed:dateCreated |
1985-12-20
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pubmed:abstractText |
The COOH terminus of the externally disposed variant surface glycoprotein (VSG) of the eukaryotic pathogenic protozoan Trypanosoma brucei strain 427 variant MITat 1.4 (117) is covalently linked to a novel phosphatidylinositol-containing glycolipid. This conclusion is supported by analysis of the products of nitrous acid deamination or Staphylococcus aureus phosphatidylinositol-specific phospholipase C treatment of purified membrane-form VSG. Lysis of trypanosomes is accompanied by release of soluble VSG, catalyzed by activation of an endogenous phospholipase C. The only apparent difference between membrane-form VSG and soluble VSG is the removal of sn-1,2-dimyristylglycerol. The COOH-terminal glycopeptide derived by Pronase digestion of soluble VSG was characterized by chemical modification and digestion with alkaline phosphatase. The results are consistent with the single non-N-acetylated glucosamine residue being the reducing terminus of the oligosaccharide and in a glycosidic linkage to a myo-inositol monophosphate that is probably myo-inositol 1,2-cyclic monophosphate. A partial structure for the VSG COOH-terminal moiety is presented. This structure represents a new type of eukaryotic post-translational protein modification and membrane anchor. We discuss the relevance of this structure to observations that have been made with other eukaryotic membrane proteins.
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pubmed:grant |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Carbohydrates,
http://linkedlifedata.com/resource/pubmed/chemical/Glycolipids,
http://linkedlifedata.com/resource/pubmed/chemical/Glycopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Myristic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Myristic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylglycerols,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Pronase,
http://linkedlifedata.com/resource/pubmed/chemical/Tritium,
http://linkedlifedata.com/resource/pubmed/chemical/Variant Surface Glycoproteins...,
http://linkedlifedata.com/resource/pubmed/chemical/dimyristoylphosphatidylglycerol
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
260
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14547-55
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:4055788-Animals,
pubmed-meshheading:4055788-Carbohydrates,
pubmed-meshheading:4055788-Chromatography, Gas,
pubmed-meshheading:4055788-Gas Chromatography-Mass Spectrometry,
pubmed-meshheading:4055788-Glycolipids,
pubmed-meshheading:4055788-Glycopeptides,
pubmed-meshheading:4055788-Glycoproteins,
pubmed-meshheading:4055788-Myristic Acid,
pubmed-meshheading:4055788-Myristic Acids,
pubmed-meshheading:4055788-Peptide Fragments,
pubmed-meshheading:4055788-Phosphatidylglycerols,
pubmed-meshheading:4055788-Phosphatidylinositols,
pubmed-meshheading:4055788-Pronase,
pubmed-meshheading:4055788-Protein Binding,
pubmed-meshheading:4055788-Tritium,
pubmed-meshheading:4055788-Trypanosoma brucei brucei,
pubmed-meshheading:4055788-Variant Surface Glycoproteins, Trypanosoma
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pubmed:year |
1985
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pubmed:articleTitle |
Glycosyl-sn-1,2-dimyristylphosphatidylinositol is covalently linked to Trypanosoma brucei variant surface glycoprotein.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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