Linked Life Data

8977219

Source:http://linkedlifedata.com/resource/pubmed/id/8977219

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-1-30
pubmed:abstractText
This study was prompted by the paradoxical observation that a pair of dinitrophenyl-specific murine monoclonal IgG2a Abs had similar monosaccharide content and yet differed in their binding to lectins. The differential lectin-binding properties were lost when the Abs were denatured, suggesting that variations in lectin binding reflected the conformational accessibility of the N-glycans rather than intrinsic differences in the lectin binding capacity of the glycans themselves. This hypothesis was supported by experiments indicating that the degree to which the N-glycans on the Abs were reactive with beta-1,4-galactosyltransferase or susceptible to peptide N-glycosidase F corresponded directly to their relative accessibility to lectins. Moreover, the relative susceptibility to these enzymes and accessibility to lectins was inversely related to the capacity of the Abs to activate the classical pathway, suggesting that the orientation of the more accessible N-glycan might inhibit C1q binding. This hypothesis was supported by evidence that enzymatic cleavage of the more accessible N-glycan resulted in enhanced Clq, C4b, and C3b deposition. Conversely, removal of the less accessible N-glycan expressed by the other Ab inhibited C1q, C4b, and C3b deposition. The respective increase or decrease in C3b deposition on the two deglycosylated Abs was magnified when complement activation was performed in factor B-depleted serum, suggesting that N-glycan conformation primarily affects the classical pathway. Collectively, these data suggest that the orientation of the N-glycan expressed on Igs can profoundly influence interaction with the complement system.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
158
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
426-35
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8977219-Amidohydrolases, pubmed-meshheading:8977219-Animals, pubmed-meshheading:8977219-Carbohydrate Conformation, pubmed-meshheading:8977219-Complement Activation, pubmed-meshheading:8977219-Complement C1q, pubmed-meshheading:8977219-Complement C3b, pubmed-meshheading:8977219-Complement C4b, pubmed-meshheading:8977219-Glycosylation, pubmed-meshheading:8977219-Glycosyltransferases, pubmed-meshheading:8977219-Immunoglobulin Constant Regions, pubmed-meshheading:8977219-Immunoglobulin G, pubmed-meshheading:8977219-Immunoglobulin Heavy Chains, pubmed-meshheading:8977219-Isoelectric Focusing, pubmed-meshheading:8977219-Mice, pubmed-meshheading:8977219-Mice, Inbred BALB C, pubmed-meshheading:8977219-Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase, pubmed-meshheading:8977219-Peptides, pubmed-meshheading:8977219-Polysaccharides, pubmed-meshheading:8977219-Protein Binding, pubmed-meshheading:8977219-Protein Conformation
pubmed:year
1997
pubmed:articleTitle
Ig N-glycan orientation can influence interactions with the complement system.
pubmed:affiliation
Department of Microbiology, University of Oklahoma Health Sciences Center, Oklahoma City 73104, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't