Linked Life Data

8463235

Source:http://linkedlifedata.com/resource/pubmed/id/8463235

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1993-5-5
pubmed:abstractText
CD22 beta is a glycoprotein found on the surface of B cells during restricted stages of development. It is believed to play a role in cell-cell interactions and B cell activation. The accompanying paper (Sgroi, D., Varki, A., Braesch-Andersen, S., and Stamenkovic, I. (1993) J. Biol. Chem. 268, 7011-7018) shows that CD22 beta recognizes multiple glycoproteins on the surfaces of T and B cells and that sialylation of these ligands is essential for binding. To identify the structure(s) of the sialylated oligosaccharide(s) recognized by CD22 beta, [3H]glucosamine-labeled glycoproteins were purified from Daudi cells by adsorption onto a CD22 beta recombinant immunoglobulin (CD22 beta Rg) chimera attached to protein A-Sepharose (PAS), and the N-linked oligosaccharides were released by peptide N-glycosidase F. These released oligosaccharides failed to bind to CD22 beta Rg-PAS under the conditions used initially to adsorb the glycoproteins, but their elution from a column of CD22 beta Rg-PAS was significantly retarded. Populations of oligosaccharides with different affinities could be identified by their order of elution. Specific sialidases were used to determine the content of alpha-2,3- and alpha-2,6-linked sialic acid in these different populations and their contribution to binding. Multiantennary oligosaccharides with one alpha-2,6-linked residue bound marginally, and those with two or more bound more tightly. alpha-2,3-Linked sialic acid residues were without effect. Binding did not require divalent cations and was abrogated by mild periodate oxidation of the outer side chain of sialic acid. No marked differences in size or fucose content were found between the populations of high and low affinity oligosaccharides. However, the low affinity population could be partially converted into higher affinity by treatment with beta-galactoside alpha-2,6 sialyltransferase and CMP-sialic acid. Thus, CD22 beta is a mammalian lectin that can recognize specific N-linked oligosaccharide structures containing alpha-2,6-linked sialic acids.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7019-27
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8463235-Animals, pubmed-meshheading:8463235-Antigens, CD, pubmed-meshheading:8463235-Antigens, CD22, pubmed-meshheading:8463235-Antigens, Differentiation, B-Lymphocyte, pubmed-meshheading:8463235-B-Lymphocytes, pubmed-meshheading:8463235-Carbohydrate Sequence, pubmed-meshheading:8463235-Cations, Divalent, pubmed-meshheading:8463235-Cell Adhesion Molecules, pubmed-meshheading:8463235-Cell Line, pubmed-meshheading:8463235-Chromatography, High Pressure Liquid, pubmed-meshheading:8463235-Chromatography, Ion Exchange, pubmed-meshheading:8463235-HeLa Cells, pubmed-meshheading:8463235-Humans, pubmed-meshheading:8463235-Lectins, pubmed-meshheading:8463235-Ligands, pubmed-meshheading:8463235-Molecular Sequence Data, pubmed-meshheading:8463235-Oligosaccharides, pubmed-meshheading:8463235-Sialic Acids
pubmed:year
1993
pubmed:articleTitle
Natural ligands of the B cell adhesion molecule CD22 beta carry N-linked oligosaccharides with alpha-2,6-linked sialic acids that are required for recognition.
pubmed:affiliation
Glycobiology Program, University of California, La Jolla 92093-0063.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.