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Titolo:
HB4 ANTIBODY RECOGNIZES A CARBOHYDRATE STRUCTURE ON LYMPHOCYTE SURFACE-PROTEINS RELATED TO HB6, CDW75, AND CD76 ANTIGENS
Autore:
DELAU WBM; KUIPERS J; VOSHOL H; CLEVERS H; BAST BJEG;
Indirizzi:
UNIV HOSP UTRECHT,DEPT IMMUNOL F03 821,HEIDELBERGLAAN 100 3584 CX UTRECHT NETHERLANDS UNIV UTRECHT,BIJVOET CTR BIOMOLEC RES UTRECHT NETHERLANDS
Titolo Testata:
The Journal of immunology
fascicolo: 11, volume: 150, anno: 1993,
pagine: 4911 - 4919
SICI:
0022-1767(1993)150:11<4911:HARACS>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
MONOCLONAL-ANTIBODIES; CELL-LINE; RECEPTOR; CHAINS; CDNA; PHENOTYPE; ADHESION; CLONING; CD2;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
W.B.M. Delau et al., "HB4 ANTIBODY RECOGNIZES A CARBOHYDRATE STRUCTURE ON LYMPHOCYTE SURFACE-PROTEINS RELATED TO HB6, CDW75, AND CD76 ANTIGENS", The Journal of immunology, 150(11), 1993, pp. 4911-4919

Abstract

Cells regulate the specificity of the carbohydrate chains on their membrane-bound glycoconjugates by differential expression of glycosyltransferases. In lymphocytes, beta-galactoside alpha2,6-sialyltransferaseis reportedly involved in the generation of epitopes recognized by HB6, CDw75, and CD76 mAb. The HB4 mAb binds to an Ag present on subpopulations of B and NK cells. We now show that this Ag represents another member of a set of neuraminidase-sensitive, alpha2,6-sialyltransferase-generated sugar Ag. Transient expression of a cDNA encoding this enzyme in COS cells generated a minor population of HB4+ cells that was completely contained within the HB6+ COS cell population. Using various proteinases and an inhibitor of N-linked carbohydrate processing, we show both epitopes to represent components of N-glycosylated membrane proteins. Remarkably, porcine thyroglobulin, an alpha2,6-NeuAc+ glycoprotein, is specifically recognized by both mAb. These data underline a close relationship between HB4 and HB6 epitopes and imply further thatboth mAb react with oligosaccharide chains irrespective of the carrier molecule nature. Thus, the terminal sugar residue sialic acid plays a pivotal role in at least four distinct epitopes that are expressed differentially in immune cells. This may point at an important role forthese epitopes in biologic recognition.

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Documento generato il 24/11/20 alle ore 08:35:53