Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
EXPRESSION AND CHARACTERIZATION OF RECOMBINANT SOLUBLE PEPTIDE - I-A COMPLEXES ASSOCIATED WITH MURINE EXPERIMENTAL AUTOIMMUNE-DISEASES
Autore:
RADU CG; OBER BT; COLANTONIO L; QADRI A; WARD ES;
Indirizzi:
UNIV TEXAS,SW MED CTR,DEPT MICROBIOL,6000 HARRY HINES BLVD DALLAS TX 75235 UNIV TEXAS,SW MED CTR,DEPT MICROBIOL DALLAS TX 75235 UNIV TEXAS,SW MED CTR,CTR CANC IMMUNOBIOL DALLAS TX 75235
Titolo Testata:
The Journal of immunology
fascicolo: 12, volume: 160, anno: 1998,
pagine: 5915 - 5921
SICI:
0022-1767(1998)160:12<5915:EACORS>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
MHC CLASS-II; T-CELL RECEPTOR; MYELIN BASIC-PROTEIN; BOUND SINGLE PEPTIDES; INVARIANT-CHAIN; ANTIGEN RECOGNITION; SURFACE EXPRESSION; ALPHA-CHAIN; BINDING; MOLECULES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
44
Recensione:
Indirizzi per estratti:
Citazione:
C.G. Radu et al., "EXPRESSION AND CHARACTERIZATION OF RECOMBINANT SOLUBLE PEPTIDE - I-A COMPLEXES ASSOCIATED WITH MURINE EXPERIMENTAL AUTOIMMUNE-DISEASES", The Journal of immunology, 160(12), 1998, pp. 5915-5921

Abstract

Structural and functional studies of murine MHC class II I-A molecules have been limited by the low yield and instability of soluble, recombinant heterodimers. In the murine autoimmune diseases experimental autoimmune encephalomyelitis and collagen-induced arthritis, MHC class II molecules I-A(u) and I-A(q) present peptides derived from myelin basic protein and type II collagen, respectively, to autoreactive T cells. To date, systems for the expression of these two I-A molecules in soluble form for use in structure-function relationship studies have notbeen reported. In the present study, we have expressed functional I-A(u) and I-A(q) molecules using a baculovirus insect cell system, The chain pairing and stability of the molecules were increased by covalently linking the antigenic peptides to beta-chains and adding carboxyl-terminal leucine zippers. Peptide:I-Ag complex quantitatively formed anSDS-stable dimer, whereas peptide:I-A(u) formed undetectable amounts. However, the two complexes did not show any significant difference intheir response to thermal denaturation as assessed by circular dichroism analyses, The autoantigen peptide:I-A complexes were highly activein stimulating cognate T cells to secrete IL-2 and inducing Ag-specific apoptosis of the T cells. Interestingly, the T cells were stimulated by these soluble molecules in the apparent absence of experimentallyinduced cross-linking of TCRs, indicating that they may have therapeutic potential in autoimmune disease models.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/11/20 alle ore 13:20:13