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Titolo:
MAPPING OF THE CATALYTIC AND EPITOPIC SITES OF HUMAN CD38 NAD(+) GLYCOHYDROLASE TO A FUNCTIONAL DOMAIN IN THE CARBOXYL-TERMINUS/
Autore:
HOSHINO S; KUKIMOTO I; KONTANI K; INOUE S; KANDA Y; MALAVASI F; KATADA T;
Indirizzi:
UNIV TOKYO,FAC PHARMACEUT SCI,DEPT PHYSIOL CHEM TOKYO 113 JAPAN UNIV ANCONA,SCH MED,INST BIOL & GENET ANCONA ITALY
Titolo Testata:
The Journal of immunology
fascicolo: 2, volume: 158, anno: 1997,
pagine: 741 - 747
SICI:
0022-1767(1997)158:2<741:MOTCAE>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
CYCLIC ADP-RIBOSE; LYMPHOCYTE ANTIGEN CD38; LEUKEMIC HL-60 CELLS; MONOCLONAL-ANTIBODY; NAD GLYCOHYDROLASE; RETINOIC ACID; B-CELLS; SURFACE; MOLECULE; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
36
Recensione:
Indirizzi per estratti:
Citazione:
S. Hoshino et al., "MAPPING OF THE CATALYTIC AND EPITOPIC SITES OF HUMAN CD38 NAD(+) GLYCOHYDROLASE TO A FUNCTIONAL DOMAIN IN THE CARBOXYL-TERMINUS/", The Journal of immunology, 158(2), 1997, pp. 741-747

Abstract

We reported that 1) ecto-NAD(+) glycohydrolase (NADase) activity induced upon differentiation of HL-60 cells is localized on the extracellular carboxyl-terminal side of CD38 and that 2) CD38 ligation by specific mAbs is followed by protein tyrosine phosphorylation in the cells. The strategy selected for identifying the relevant catalytic domains of the molecule relies upon the production in COS-7 cells of carboxyl-terminal deletion mutants of CD38. The mutants with fewer than 15 aminoacids deleted at the carboxyl terminus of the 300-amino acid wild-type molecule maintained NADase activity, whereas those with more than 27amino acids deleted did not. The general inference is that the carboxyl-terminal 273-285 sequence bears the site of enzyme activity. introduction of site-directed mutation of a conserved cysteine residue (Cys(275)), located in the 273-285 sequence, completely abolished NADase activity. The second issue resolved in this work is the definition of anepitope of the agonistic anti-CD38 mAbs. To this aim, a panel of selected anti-CD38 mAbs was tested using these mutants and various CD38 fragments as the target in immunoblot analyses. All of the epitopes recognized by mAbs inducing protein tyrosine phosphorylation were mapped on an identical site containing the carboxyl-terminal sequence of 273-285. The conclusion is that the discrete carboxyl-terminal sequence identified in the present study not only plays a key role in its ecto-NADase activity, but actually constitutes the epitopes exploited by the agonistic anti-CD38 mAbs for transmembrane signaling.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/11/20 alle ore 07:39:32