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Titolo:
DELINEATION OF THE AMINO-ACID-RESIDUES INVOLVED IN TRANSCYTOSIS AND CATABOLISM OF MOUSE IGG1
Autore:
MEDESAN C; MATESOI D; RADU C; GHETIE V; WARD ES;
Indirizzi:
UNIV TEXAS,SW MED CTR,DEPT MICROBIOL,5323 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: 5, volume: 158, anno: 1997,
pagine: 2211 - 2217
SICI:
0022-1767(1997)158:5<2211:DOTAII>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
SITE-DIRECTED MUTAGENESIS; FC RECEPTOR; IMMUNOGLOBULIN-G; PROTEIN-A; MICE; MOLECULE; FRAGMENT; BINDING; COMPLEX; FETAL;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
C. Medesan et al., "DELINEATION OF THE AMINO-ACID-RESIDUES INVOLVED IN TRANSCYTOSIS AND CATABOLISM OF MOUSE IGG1", The Journal of immunology, 158(5), 1997, pp. 2211-2217

Abstract

The MHC class I-related receptor, FcRn, is involved in both the transcytosis of serum gamma-globulins (IgGs) and in regulating their serum persistence. The interaction site of FcRn on the Fc region of rodent IgG has been mapped to residues at the CH2-CH3 domain interface using site-directed mutagenesis and x-ray crystallographic analyses. In the current study, the role of individual residues (H310, H433, and N434) at this interface in mediating the Fc-FcRn interaction has been investigated using recombinant, mutated Fc hinge fragments derived from mouseIgG1. In addition, two highly conserved Fc histidines (H435 and H436)have been mutated to alanine, and the resulting mutated Fc hinge fragments were analyzed in both transcytosis and pharmacokinetic studies in mice and in competition binding assays using recombinant, soluble FcRn. The analyses indicate that mutation of H310, H435, and, to a lesser extent, H436 to alanine results in reduced activity of the re hinge fragments in both in vivo and in vitro assays. Thus, in addition to the previously defined role of 1253 in the FcRn-IgG interaction, these histidines play a key role in mediating the functions conducted by thisFc receptor. The effects of these mutations on binding of Fc hinge fragments to staphylococcal protein A have also been analyzed and demonstrate a partial, but not complete, overlap of the FcRn and staphylococcal protein A interaction sites on mouse IgG1.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 06:34:35