Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions |
umls-concept:C0009498,
umls-concept:C0021017,
umls-concept:C0086418,
umls-concept:C0205438,
umls-concept:C0449432,
umls-concept:C0699040,
umls-concept:C0871161,
umls-concept:C1167622,
umls-concept:C1179435,
umls-concept:C1412999,
umls-concept:C1413000,
umls-concept:C1511539,
umls-concept:C1524073,
umls-concept:C1548799,
umls-concept:C1705248
|
pubmed:issue |
7
|
pubmed:dateCreated |
1986-4-15
|
pubmed:abstractText |
In a previous study we demonstrated that the thioester-mediated transacylation of the human C4B isotype onto sheep erythrocytes (ES) was approximately fourfold more efficient than that of C4A. Moreover, although C4B formed predominantly ester linkages, C4A displayed a preference for amide bond formation. We therefore suggested that the relative functional activity observed for the two isotypes would be a combined reflection of their nucleophilic preference and the surface composition of the C1-bearing target. The present study tests this hypothesis. Chemical modification of amino groups on Es with ethylacetimidate produced a twofold decrease in the C1-dependent binding of C4A isotype, while having a negligible effect on C4B binding. Furthermore, with human erythrocytes and two human leukocyte cell lines, K562 and U937, the C4B to C4A deposition ratio decreased from greater than 4 with ES to between 1.5 and 2. Irrespective of the target, C4A and C4B maintained their preference for forming amide and ester bonds, respectively. Interestingly, SDS-PAGE profiles of radiolabeled C4A and C4B, which had been covalently deposited on the various cells, suggested a further degree of transacylation specificity, as the two isotypic alpha-chains sometimes bound to different membrane components. These differences were not easily accounted for by simple differences in the abundance of the preferred nucleophile for each isotype on a given surface constituent, nor were they due to the preferential binding of one isotype to the sensitizing antibody. We speculate that nascent C4B may contain a substrate binding site that facilitates productive attack on the thioester carbonyl by molecules containing the class of nucleophile preferred by each isotype.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
AIM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Complement C1,
http://linkedlifedata.com/resource/pubmed/chemical/Complement C4,
http://linkedlifedata.com/resource/pubmed/chemical/Complement C4a,
http://linkedlifedata.com/resource/pubmed/chemical/Complement C4b,
http://linkedlifedata.com/resource/pubmed/chemical/Imidoesters,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin M,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/ethyl acetimidate
|
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
0022-1767
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
1
|
pubmed:volume |
136
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
2542-50
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:3512717-Acylation,
pubmed-meshheading:3512717-Animals,
pubmed-meshheading:3512717-Antibody Specificity,
pubmed-meshheading:3512717-Carbohydrate Conformation,
pubmed-meshheading:3512717-Complement C1,
pubmed-meshheading:3512717-Complement C4,
pubmed-meshheading:3512717-Complement C4a,
pubmed-meshheading:3512717-Complement C4b,
pubmed-meshheading:3512717-Erythrocyte Membrane,
pubmed-meshheading:3512717-Humans,
pubmed-meshheading:3512717-Imidoesters,
pubmed-meshheading:3512717-Immunoglobulin M,
pubmed-meshheading:3512717-Macromolecular Substances,
pubmed-meshheading:3512717-Molecular Weight,
pubmed-meshheading:3512717-Peptide Hydrolases,
pubmed-meshheading:3512717-Phenotype,
pubmed-meshheading:3512717-Sheep
|
pubmed:year |
1986
|
pubmed:articleTitle |
Covalent binding properties of the C4A and C4B isotypes of the fourth component of human complement on several C1-bearing cell surfaces.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|