Linked Life Data

7706263

Source:http://linkedlifedata.com/resource/pubmed/id/7706263

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1995-5-10
pubmed:abstractText
We have investigated the structure of the glycosylphosphatidylinositol (GPI) anchor and the O-linked glycan chains of the 40/45-kDa glycoprotein from the cell surface of the protozoan parasite Trypanosoma cruzi. This glycoconjugate is the major acceptor for sialic acid transferred by trans-sialidase of T. cruzi Y-strain, epimastigote form. The GPI anchor was liberated by treatment with hot alkali, and the phosphoinositol-oligosaccharide moiety was characterized and shown to have the following structure. [formula: see text] Unusually the glucosamine was 6-O-substituted with 2-aminoethylphosphonate, and 2-aminoethylphosphonate was also present on the third mannose residue distal to glucosamine, partially replacing the ethanolamine phosphate. The beta-eliminated reduced oligosaccharide chains showed that two novel classes of O-linked N-acetylglucosamine oligosaccharide were present. The first series had the structures Galp beta 1-3GlcNAc-ol; Galp beta 1-6(Galp beta 1-3)GlcNAc-ol; and Galp beta 1-2Galp beta 1-6(Galp beta 1-3)GlcNAc-ol, whereas the other series had a 1-4 linkage to N-acetylglucosaminitol and had structures Galp beta 1-4GlcNAc-ol, Galp beta 1-6(Galp beta 1-4)GlcNAc-ol, and Galp beta 1-2Galp beta 1-6(Galp beta 1-4)GlcNAc-ol. We have also investigated the kinetics of in vitro sialylation of these O-linked oligosaccharides by the T. cruzi transsialidase and have shown that incorporation of one molecule of sialic acid hinders entry of a second molecule when two potential acceptor sites are present.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7241-50
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7706263-Animals, pubmed-meshheading:7706263-Carbohydrate Conformation, pubmed-meshheading:7706263-Carbohydrate Sequence, pubmed-meshheading:7706263-Carbohydrates, pubmed-meshheading:7706263-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:7706263-Gas Chromatography-Mass Spectrometry, pubmed-meshheading:7706263-Glycosylphosphatidylinositols, pubmed-meshheading:7706263-Magnetic Resonance Spectroscopy, pubmed-meshheading:7706263-Membrane Glycoproteins, pubmed-meshheading:7706263-Molecular Sequence Data, pubmed-meshheading:7706263-Oligosaccharides, pubmed-meshheading:7706263-Phosphatidylinositol Diacylglycerol-Lyase, pubmed-meshheading:7706263-Phosphatidylinositols, pubmed-meshheading:7706263-Phosphoric Diester Hydrolases, pubmed-meshheading:7706263-Protozoan Proteins, pubmed-meshheading:7706263-Trypanosoma cruzi
pubmed:year
1995
pubmed:articleTitle
Structural characterization of the major glycosylphosphatidylinositol membrane-anchored glycoprotein from epimastigote forms of Trypanosoma cruzi Y-strain.
pubmed:affiliation
Departamento de Microbiologia Geral, Universidade Federal do Rio de Janeiro, Brazil.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't