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Titolo:
POSTTRANSLATIONAL MODIFICATION OF CD38 PROTEIN INTO A HIGH-MOLECULAR-WEIGHT FORM ALTERS ITS CATALYTIC PROPERTIES
Autore:
UMAR S; MALAVASI F; MEHTA K;
Indirizzi:
UNIV TEXAS,MD ANDERSON CANCER CTR,DEPT BIOIMMUNOTHERAPY,BOX 60,1515 HOLCOMBE BLVD HOUSTON TX 77030 UNIV TEXAS,MD ANDERSON CANCER CTR,DEPT BIOIMMUNOTHERAPY HOUSTON TX 77030 UNIV ANCONA,SCH MED,INST BIOL & GENET I-60100 ANCONA ITALY
Titolo Testata:
The Journal of biological chemistry
fascicolo: 27, volume: 271, anno: 1996,
pagine: 15922 - 15927
SICI:
0021-9258(1996)271:27<15922:PMOCPI>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
CYCLIC ADP-RIBOSE; LYMPHOCYTE ANTIGEN CD38; LEUKEMIA HL-60 CELLS; EGG-SPECIFIC NADASE; RETINOIC ACID; RECEPTOR DIMERIZATION; 2ND-MESSENGER ENZYME; HUMAN ERYTHROCYTES; OUTER SURFACE; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
S. Umar et al., "POSTTRANSLATIONAL MODIFICATION OF CD38 PROTEIN INTO A HIGH-MOLECULAR-WEIGHT FORM ALTERS ITS CATALYTIC PROPERTIES", The Journal of biological chemistry, 271(27), 1996, pp. 15922-15927

Abstract

Human CD38 is a 45-kDa transmembrane protein that acts as a bifunctional ectoenzyme, catalyzing the synthesis of cyclic ADP-ribose (cADPR) from NAD(+) and the hydrolysis of cADPR to ADP-ribose, All-trans-retinoic acid (RA) is a potent and specific inducer of CD38 in myeloid cells, In this report, we demonstrate that RA-induced CD38 protein hom human myeloid (HL-60) leukemia cells coimmunoprecipitates with another protein of molecular mass approximate to 190 kDa (p190), The p190 protein is localized exclusively in the membranes and is a consequence of post-translational cross-linking of CD38 protein, This conclusion was based on the observations that purified CD38 effectively competes with p190, its accumulation is preceded by the accumulation of CD38, it immunoreacted with three different monospecific anti-CD38 antibodies on immunoblots, and its peptide map revealed several peptides in common with CD38. Furthermore, CD38 could serve as a suitable substrate for transglutaminase (TGase)-catalyzed cross-linking reactions in vitro, and the accumulation of p190 in RA-treated HL-60 cells is effectively blocked by the presence of TGase-specific inhibitor, The purified p190 showed at least three times more cyclase activity than CD38, Conversely, p190 was at least 2.5-fold less active than CD38 in hydrolyzing cADPR to ADPR. These results suggest that post-translational modification of CD38 may represent an important mechanism for regulating the two catalytic activities of this bifunctional enzyme.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/09/20 alle ore 06:34:32