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Titolo:
RECOMBINANT ALPHA-CHAINS OF TYPE-IV COLLAGEN DEMONSTRATE THAT THE AMINO-TERMINAL OF THE GOODPASTURE AUTOANTIGEN IS CRUCIAL FOR ANTIBODY RECOGNITION
Autore:
RYAN JJ; MASON PJ; PUSEY CD; TURNER N;
Indirizzi:
HAMMERSMITH HOSP,RENAL SECT,DIV MED,IMPERIAL COLL,SCH MED,DU CANE RD LONDON W12 0NN ENGLAND HAMMERSMITH HOSP,IMPERIAL COLL,SCH MED,DEPT HAEMATOL LONDON W12 0NN ENGLAND UNIV ABERDEEN,DEPT MED & THERAPEUT ABERDEEN HONG KONG
Titolo Testata:
Clinical and experimental immunology
fascicolo: 1, volume: 113, anno: 1998,
pagine: 17 - 27
SICI:
0009-9104(1998)113:1<17:RAOTCD>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLOMERULAR-BASEMENT-MEMBRANE; ALPHA-3(IV) CHAIN; CDNA ISOLATION; ANTIGEN; IDENTIFICATION; DOMAIN; GENE; LOCALIZATION; EPITOPES; DISEASE;
Keywords:
TYPE IV COLLAGEN; GLOMERULAR BASEMENT MEMBRANE; GOODPASTURE ANTIGEN; AUTOANTIBODY; BINDING; B CELL EPITOPE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
51
Recensione:
Indirizzi per estratti:
Citazione:
J.J. Ryan et al., "RECOMBINANT ALPHA-CHAINS OF TYPE-IV COLLAGEN DEMONSTRATE THAT THE AMINO-TERMINAL OF THE GOODPASTURE AUTOANTIGEN IS CRUCIAL FOR ANTIBODY RECOGNITION", Clinical and experimental immunology, 113(1), 1998, pp. 17-27

Abstract

Goodpasture's disease, an autoimmune disorder causing severe glomerulonephritis and pulmonary haemorrhage, is characterized by antibodies to the glomerular basement membrane (GBM). The principal target antigenhas been identified as the carboxyl terminal non-collagenous (NC1) domain of the alpha 3-chain of type IV collagen. Anti-GEM antibodies appear to recognize one major epitope that is common to all patients, andis largely conformational. We have analysed antibody binding to recombinant alpha(IV)NC1 domains using a construct and expression system shown to produce correctly folded antigen that is strongly recognized byautoantibodies. In this system, as with the native antigen, alpha 3(IV)NC1 was bound strongly by antibodies from all patients, whereas the closely related alpha 1(IV) and alpha 5(IV)NC1 domains, similarly expressed, showed no such binding. A series of chimeric NC1 domains, between human alpha 3(IV) and alpha 1(IV), and between human and rat alpha 3(IV), were expressed as recombinant molecules, and were recognized byautoantibodies to varying degrees. Strong binding required the presence of human alpha 3(IV) sequence in the amino terminal region of both sets of chimeric molecules. This work strongly suggests that the aminoterminal of alpha 3(IV)NC1 is critical for antibody recognition, whereas the carboxyl terminal end of alpha 3(IV)NC1 has a less important role.

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Documento generato il 29/11/20 alle ore 18:12:17