Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Molecular cloning and characterization of mouse CD97
Autore:
Hamann, J; van Zeventer, C; Bijl, A; Molenaar, C; Tesselaar, K; van Lier, RAW;
Indirizzi:
Univ Amsterdam, Acad Med Ctr, CLB, Dept Immunobiol, NL-1066 CX Amsterdam, Netherlands Univ Amsterdam Amsterdam Netherlands NL-1066 CX X Amsterdam, Netherlands Univ Amsterdam, Acad Med Ctr, Expt & Clin Immunol Lab, NL-1066 CX Amsterdam, Netherlands Univ Amsterdam Amsterdam Netherlands NL-1066 CX X Amsterdam, Netherlands
Titolo Testata:
INTERNATIONAL IMMUNOLOGY
fascicolo: 4, volume: 12, anno: 2000,
pagine: 439 - 448
SICI:
0953-8178(200004)12:4<439:MCACOM>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
DECAY-ACCELERATING FACTOR; 7-SPAN TRANSMEMBRANE MOLECULE; SECRETIN RECEPTOR SUPERFAMILY; PROTEIN-COUPLED RECEPTORS; GUINEA-PIG; EXTRACELLULAR DOMAIN; DIFFERENTIAL DISPLAY; MESSENGER-RNA; FACTOR DAF; FAMILY;
Keywords:
adhesion; CD55; cDNA cloning; EGF-TM7 family; G protein-coupled receptors; phylogenetic restriction;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Hamann, J Univ Amsterdam, Acad Med Ctr, CLB, Dept Immunobiol, Plesmanlaan 125, NL-1066 CX Amsterdam, Netherlands Univ Amsterdam Plesmanlaan 125 Amsterdam Netherlands NL-1066 CX
Citazione:
J. Hamann et al., "Molecular cloning and characterization of mouse CD97", INT IMMUNOL, 12(4), 2000, pp. 439-448

Abstract

The EGF-TM7 family (CD97 and EMR1) is a group of class II seven-span transmembrane receptors predominantly expressed by cells of the immune system. Recently, we have identified CD55, a regulatory molecule of the complement cascade, as a cellular ligand of human CD97 (hCD97), In this study, the molecular properties of mouse CD97 (mCD97) are described. Like hCD97, mCD97 hasan extended extracellular region with several epidermal growth factor-like(EGF) domains. Due to alternative RNA splicing, isoforms with three and four EGF domains exist, designated mCD97(EGF1,2,4) and mCD97(EGF1,2,3,4) respectively. All EGF domains, except for the N-terminal one, possess a calcium-binding site. In a third isoform mCD97(EGF1,2,X,3,4), a sequence of 45 amino acids was found between the second and third EGF domain that does not correspond to any known protein module. Using newly generated mCD97 mAb, we show that analogous to the blood expression pattern of hCD97, mCD97 can be found on lymphoid and myeloid cells. Adhesion of mouse erythrocytes and splenocytes to COS cells expressing mCD97(EGF1,2,4) or mCD97(EGF1,2,3,4) could be blocked by mouse CD55 (mCD55) antibody, identifying mCD55 as a cellular ligand for mCD97, Consistent with the necessity of directly linked EGF domains for the integrity of the CD55-binding site on hCD97, no adhesion was detected to the largest mouse isoform mCD97(EGF1,2,X,3,4), Remarkably, we found that the interaction between CD97 and CD55 is phylogenetically restricted, as indicated by the selective adhesion of primate erythrocytes to hCD97 transfectants, and of mouse and rat erythrocytes to mCD97 transfectants respectively.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 09:16:57