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Titolo:
CD38 BINDING TO HUMAN MYELOID CELLS IS MEDIATED BY MOUSE AND HUMAN CD31
Autore:
HORENSTEIN AL; STOCKINGER H; IMHOF BA; MALAVASI F;
Indirizzi:
UNIV TURIN,DEPT GENET BIOL & BIOCHEM,CELL BIOL LAB,VIA SANTENA 19 I-10126 TURIN ITALY UNIV VIENNA,VIRCC,INST IMMUNOL VIENNA AUSTRIA BASEL INST IMMUNOL CH-4005 BASEL SWITZERLAND UNIV ANCONA,SCH MED,INST BIOL & GENET I-60131 ANCONA ITALY
Titolo Testata:
Biochemical journal
, volume: 330, anno: 1998,
parte:, 3
pagine: 1129 - 1135
SICI:
0264-6021(1998)330:<1129:CBTHMC>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
SURFACE ANTIGEN CD38; ADP-RIBOSYL CYCLASE; ADHESION MOLECULE-1; PECAM-1 CD31; TYROSINE PHOSPHORYLATION; RETINOIC ACID; HL-60 CELLS; PROTEIN; IDENTIFICATION; ANTIBODY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
41
Recensione:
Indirizzi per estratti:
Citazione:
A.L. Horenstein et al., "CD38 BINDING TO HUMAN MYELOID CELLS IS MEDIATED BY MOUSE AND HUMAN CD31", Biochemical journal, 330, 1998, pp. 1129-1135

Abstract

Soluble forms of membrane receptors are emerging candidates as physiological regulators of leukocyte trafficking. In the present study, we found that the soluble form of the CD38 antigen (sCD38) bears a binding domain of low affinity for a cellular receptor on U937 cells, Cross-linking and peptide-mapping studies confirmed the physical associationand the identification of the U937 receptor as a 130 kDa protein. Thebinding of sCD38 to the receptor was differentially inhibited by several monoclonal antibodies against the CD31 cell-adhesion molecule. Thus the interaction was analysed through direct association of soluble and membrane CD38 with soluble recombinant murine CD31 with three N-terminal and with all six extracellular Ig domains. Cross-linking experiments on U937 intact cells, and ligand blot assays of the immunoprecipitated CD38 molecule, indicated that (i) the recognized epitope is determined by the tertiary structure of the molecule, and that (ii) the binding domain involved resides in the ectocellular portion of the CD31 molecule, more precisely in the first three N-terminal domains. A comparative functional activity between murine and human CD31 was also explored. The data presented suggest that (i) human CD31 bears a highly functional similarity with its murine counterpart, as it is a receptor in myeloid cells with more than one ligand (the alpha(v) beta(3) integrin and the CD38 molecule), and that (ii) the activity of sCD38 as decoy molecule for CD31 may play an important role in cell-cell interactions in physiological and pathological conditions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 19:57:43