期刊论文详细信息
FEBS Letters
Dimeric and tetrameric forms of catalytically active transmembrane CD38 in transfected HeLa cells
Zocchi, Elena2  Guida, Lucrezia2  Franco, Luisa2  Bruzzone, Santina2  Corte, Giorgio1  De Flora, Antonio2 
[1] National Institute for Cancer Research-CBA, University of Genoa, Genoa, Italy;Institute of Biochemistry, University of Genoa, Viale Benedetto XV, 1, 16132 Genoa, Italy
关键词: CD38;    Cyclic ADP-ribose;    CD38 oligomer;    Ectoenzyme;    NAD+;    cADPR;    cyclic ADP-ribose;    NAD+;    nicotinamide adenine dinucleotide;    ADPR;    ADP-ribose;    BS3;    bis(sulfosuccinimidyl)suberate;    rCD38;    recombinant soluble CD38;    β-OG;    β-octylglucopyranoside;    PMSF;    phenylmethylsulfonyl fluoride;    PBS;    phosphate-buffered saline;    NHD+;    nicotinamide hypoxanthine dinucleotide;    ϵ-NAD+;    1-N 6-etheno NAD+;    ϵ-ADPR;    1-N 6-etheno ADP-ribose;    cIDPR;    cyclic inosine diphosphoribose;    IDPR;    inosine diphosphoribose;    M r;    molecular weight;    mAb;    monoclonal antibody;    GSH;    glutathione (reduced form);   
DOI  :  10.1016/S0014-5793(98)00929-6
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

CD38, a type II transmembrane glycoprotein, behaves as a catalytically active transporter responsible for ectocellular generation of cyclic ADP-ribose (cADPR) from NAD+ and for subsequent influx of cADPR across membranes [Franco, L., Guida, L., Bruzzone, S., Zocchi, E., Usai, C. and De Flora, A. (1998) FASEB J. in press]. cADPR regulates intracellular calcium homeostasis by releasing calcium from responsive stores. The cADPR-transporting function of CD38 requires channel-generating oligomeric forms of the protein rather than the 46 kDa monomers that have been described so far in CD38+ cells. Here we demonstrate that CD38, both in reconstituted proteoliposomes and in CD38-transfected HeLa cells, is a mixture of catalytically active monomers, homodimers and homotetramers. A soluble recombinant form of CD38 corresponding to its ectocellular region proved to be monomeric. Thus, association of native CD38 with wither artificial or natural membranes seems to result in a reversible juxtaposition of monomers suitable to cADPR-transporting activity.

【 授权许可】

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