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Titolo:
DIRECT BINDING OF MYELIN BASIC-PROTEIN AND SYNTHETIC COPOLYMER-1 TO CLASS-II MAJOR HISTOCOMPATIBILITY COMPLEX-MOLECULES ON LIVING ANTIGEN-PRESENTING CELLS - SPECIFICITY AND PROMISCUITY
Autore:
FRIDKISHARELI M; TEITELBAUM D; GUREVICH E; PECHT I; BRAUTBAR C; KWON OJ; BRENNER T; ARNON R; SELA M;
Indirizzi:
WEIZMANN INST SCI,DEPT CHEM IMMUNOL IL-76100 REHOVOT ISRAEL HADASSAH MED SCH,LAUTENBERG CTR GEN & TUMOR IMMUNOL,TISSUE TYPING UNIT IL-91120 JERUSALEM ISRAEL HADASSAH MED SCH,DEPT NEUROL,NEUROIMMUNOL LAB IL-91120 JERUSALEM ISRAEL
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 11, volume: 91, anno: 1994,
pagine: 4872 - 4876
SICI:
0027-8424(1994)91:11<4872:DBOMBA>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
EXPERIMENTAL ALLERGIC ENCEPHALOMYELITIS; MULTIPLE-SCLEROSIS PATIENTS; LYMPHOCYTE-T LINES; MHC CLASS-II; IMMUNOGENIC PEPTIDES; MYASTHENIA-GRAVIS; CROSS-REACTIONS; RECOGNITION; HLA; EPITOPES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
47
Recensione:
Indirizzi per estratti:
Citazione:
M. Fridkishareli et al., "DIRECT BINDING OF MYELIN BASIC-PROTEIN AND SYNTHETIC COPOLYMER-1 TO CLASS-II MAJOR HISTOCOMPATIBILITY COMPLEX-MOLECULES ON LIVING ANTIGEN-PRESENTING CELLS - SPECIFICITY AND PROMISCUITY", Proceedings of the National Academy of Sciences of the United Statesof America, 91(11), 1994, pp. 4872-4876

Abstract

Copolymer 1 (Cop 1) is a synthetic basic random copolymer of amino acids that has been shown to be effective in suppression of experimentalallergic encephalomyelitis and is being tested as a candidate drug for multiple sclerosis. It has been previously demonstrated that Cop 1 is immunologically cross-reactive with the autoantigen myelin basic protein (BP) and competitively inhibits the response to BP of T-cell lines and clones of different major histocompatibility complex (MHC) restrictions, of both mouse and human origin. In the present study we demonstrated the direct binding of Cop 1, using its biotinylated derivative, to MHC molecules on living antigen-presenting cells. Binding of biotinylated BP and peptide p84-102 (an immunodominant epitope of BP) was also demonstrated. Cop 1 and BP bound in a promiscuous manner to different types of antigen-presenting cells of various H-2 and HLA haplotypes. The specificity of the binding was confirmed by its inhibition with either the relevant anti-MHC class II antibodies or unlabeled analogs. Cop 1 exhibited the most extensive and fast binding to antigen-presenting cells. In addition, Cop 1 inhibited the binding of biotinylatedderivatives of BP and of p84-102 to the MHC class II molecules and even displaced these antigens when already bound. Thus, these results suggest that Cop 1 indeed competes with BP for MHC binding and, thereby,inhibits T-cell responses to BP. The binding of Cop 1 to different DRalleles, probably because of its multiple MHC binding motifs, may indicate its potential as a broad-spectrum drug for multiple sclerosis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/01/20 alle ore 19:11:41