CD157, the Janus of CD38 but with a unique personality

被引:45
作者
Ortolan, E
Vacca, P
Capobianco, A
Armando, E
Crivellin, F
Horenstein, A
Malavasi, F
机构
[1] Univ Turin, Sch Med, Dept Genet Biol & Biochem, Immunogenet Lab, I-10126 Turin, Italy
[2] San Giovanni Battista Hosp, Expt Med Res Ctr, Turin, Italy
关键词
CD157; CD38; ectoenzyme; ADP-ribosyl cyclase; NAD(+) glycohydrolase;
D O I
10.1002/cbf.978
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
CD157 is a pleiotropic ectoenzyme which belongs to the CD38 family and to the growing number of leukocyte surface molecules known to act independently as both receptors and enzymes. A 45-kDa surface structure with a GPI anchor, the CD157 molecule displays two distinct domains in its extracellular component. The first is implicated in the enzymic activities of the molecule and the second features adhesion/signalling properties. CD157 shares several characteristics with CD38, including a similar amino acid sequence and enzymic functions. Both molecules are involved in the metabolism of NAD+, and the CD157 gene is synthenic on 4p15 with CD38, with which it also shares a unique genomic organization. Their conservation in phylogeny is striking evidence for their relevance in the life and death cycle of the cell. Copyright (C) 2002 John Wiley Sons, Ltd.
引用
收藏
页码:309 / 322
页数:14
相关论文
共 95 条
[1]   ADP-ribosyl cyclase and CD38 catalyze the synthesis of a calcium-mobilizing metabolite from NADP(+) [J].
Aarhus, R ;
Graeff, RM ;
Dickey, DM ;
Walseth, TF ;
Lee, HC .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (51) :30327-30333
[2]   Expression of CD157 and CD38 antigens on human myeloid leukaemia cells:: A similar pattern of modulation with differentiating inducers [J].
Anani, L ;
Coffre, C ;
Binet, C ;
Degenne, M ;
Domenech, J ;
Hérault, O .
ACTA HAEMATOLOGICA, 2001, 105 (04) :249-251
[3]   CD38 EXPRESSION ON MOUSE T-CELLS - CD38 DEFINES FUNCTIONALLY DISTINCT SUBSETS OF ALPHA-BETA-TCR(+)CD4(-)CD8(-) THYMOCYTES [J].
BEAN, AGD ;
GODFREY, DI ;
FERLIN, WG ;
SANTOSARGUMEDO, L ;
PARKHOUSE, RME ;
HOWARD, MC ;
ZLOTNIK, A .
INTERNATIONAL IMMUNOLOGY, 1995, 7 (02) :213-221
[4]   Probing ligand-induced conformational changes of human CD38 [J].
Berthelier, V ;
Laboureau, J ;
Boulla, G ;
Schuber, F ;
Deterre, P .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2000, 267 (10) :3056-3064
[5]   Nicotinamide adenine dinucleotide (NAD) and its metabolites inhibit T lymphocyte proliferation: Role of cell surface NAD glycohydrolase and pyrophosphatase activities [J].
Bortell, R ;
Moss, J ;
McKenna, RC ;
Rigby, MR ;
Niedzwiecki, D ;
Stevens, LA ;
Patton, WA ;
Mordes, JP ;
Greiner, DL ;
Rossini, AA .
JOURNAL OF IMMUNOLOGY, 2001, 167 (04) :2049-2059
[6]   Functional role of glycosylation on the recombinant CD38/ADP-ribosyl cyclase in CHO cells [J].
Chidambaram, N ;
Chang, CF .
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, 1998, 30 (09) :1011-1018
[7]   NADP+-dependent internalization of recombinant CD38 in CHO cells [J].
Chidambaram, N ;
Chang, CF .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1999, 363 (02) :267-272
[8]   Mice deficient for the ecto-nicotinamide adenine dinucleotide glycohydrolase CD38 exhibit altered humoral immune responses [J].
Cockayne, DA ;
Muchamuel, T ;
Grimaldi, JC ;
Muller-Steffner, H ;
Randall, TD ;
Lund, FE ;
Murray, R ;
Schuber, F ;
Howard, MC .
BLOOD, 1998, 92 (04) :1324-1333
[9]  
Deaglio S, 2001, FASEB J, V15, P580
[10]  
Deaglio S, 2000, CHEM IMMUNOL, V75, P99