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Titolo:
Multiple roles for the major histocompatibility complex class I-related receptor FcRn
Autore:
Ghetie, V; Ward, ES;
Indirizzi:
Univ Texas, SW Med Ctr, Ctr Immunol, Dallas, TX 75235 USA Univ Texas Dallas TX USA 75235 Med Ctr, Ctr Immunol, Dallas, TX 75235 USA Univ Texas, SW Med Ctr, Ctr Canc Immunobiol, Dallas, TX 75235 USA Univ Texas Dallas TX USA 75235 Ctr Canc Immunobiol, Dallas, TX 75235 USA
Titolo Testata:
ANNUAL REVIEW OF IMMUNOLOGY
, volume: 18, anno: 2000,
pagine: 739 - 766
SICI:
0732-0582(2000)18:<739:MRFTMH>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
MURINE IGG1 MOLECULE; IMMUNOGLOBULIN-G IGG; CANINE KIDNEY-CELLS; AMINO-ACID-RESIDUES; SERUM HALF-LIVES; DI-LEUCINE MOTIF; HUMAN-PLACENTA; CRYSTAL-STRUCTURE; MONOCLONAL-ANTIBODIES; GAMMA-RECEPTOR;
Keywords:
neonatal Fc receptor; gammaglobulin; transcytosis; serum half-life; maternofetal/intestinal transfer of IgGs;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
144
Recensione:
Indirizzi per estratti:
Indirizzo: Ghetie, V Univ Texas, SW Med Ctr, Ctr Immunol, 5323 Harry Hines Blvd, Dallas, TX 75235 USA Univ Texas 5323 Harry Hines Blvd Dallas TX USA 75235 X 75235 USA
Citazione:
V. Ghetie e E.S. Ward, "Multiple roles for the major histocompatibility complex class I-related receptor FcRn", ANN R IMMUN, 18, 2000, pp. 739-766

Abstract

Multiple functions have recently been identified for the neonatal Fc receptor FcRn. In addition, a human homolog of the rodent forms of FcRn has beenidentified and characterized. This major histocompatibility complex class I-related receptor plays a role in the passive delivery of immunoglobulin (Ig)Gs from mother to young and the regulation of serum IgG levels. In addition, FcRn expression in tissues such as liver, mammary gland, and adult intestine suggests that it may modulate IgG transport at these sites. These diverse functions are apparently brought about by the ability of FcRn to bindIgGs and transport them within and across cells. However, the molecular details as to how FcRn traffics within cells have yet to be fully understood,although in vitro systems have been developed for this purpose. The molecular nature of the FcRn-IgG interaction has been studied extensively and encompasses residues located at the CH2-CH3 domain interface of the Fc region of IgG. These Fc amino acids are highly conserved in rodents and man and interact with residues primarily located on the alpha 2 domain of FcRn. Thus,it is now possible to engineer IgGs with altered affinities for FcRn, and this has relevance to the modulation of Ige serum half-lift and maternofetal IgG transport for therapeutic applications.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 22:17:50