Molecular Cloning, Expression, and Functional Characterization of a Novel Member of the CD38 Family of ADP-ribosyl Cyclases

We report the molecular cloning and functional characterization of a novel member of the CD38 family of cyclic ADP-ribose (cADPr)-generating cyclases. We cloned a cDNA insert that encoded a 298-amino-acid-long protein (Mw ∼39 kDa). The predicted protein displayed 69, 61, and 58% similarity, respecti...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2000-07, Vol.273 (3), p.884-889
Main Authors: Adebanjo, Olugbenga A., Koval, Anatoliy, Moonga, Baljit S., Wu, Xue B., Yao, Shen, Bevis, Peter J.R., Kumegawa, Mayaoshi, Zaidi, Mone, Sun, Li
Format: Article
Language:English
Subjects:
3T3 Cells
ADP-ribosyl Cyclase
ADP-ribosyl Cyclase 1
Amino Acid Sequence
Animals
Antigens, CD
Antigens, Differentiation - chemistry
Antigens, Differentiation - genetics
Antigens, Differentiation - metabolism
Base Sequence
Ca2+ signaling
CD157 antigen
CD38 antigen
Cloning, Molecular
DNA, Complementary
Green Fluorescent Proteins
Humans
Luminescent Proteins - genetics
Membrane Glycoproteins
Mice
Microscopy, Fluorescence
Molecular Sequence Data
NAD+ Nucleosidase - chemistry
NAD+ Nucleosidase - genetics
NAD+ Nucleosidase - metabolism
osteoblast
osteoclast
Rabbits
Rats
ryanodine receptor
Sequence Homology, Amino Acid
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Summary:We report the molecular cloning and functional characterization of a novel member of the CD38 family of cyclic ADP-ribose (cADPr)-generating cyclases. We cloned a cDNA insert that encoded a 298-amino-acid-long protein (Mw ∼39 kDa). The predicted protein displayed 69, 61, and 58% similarity, respectively, to mouse, rat, and human CD38. Rabbit CD38 was also 28% homologous to Aplysia ADP-ribosyl cyclase and leukocyte CD157 (another ADP-ribosyl cyclase); the three cyclases shared 10 cysteine and 2 adjacent proline residues. We then transfected CD38-negative NIH3T3 cells with cDNA encoding a CD38-EGFP fusion protein. Epifluorescence microscopy showed intense EGFP fluorescence confirming CD38 expression. We finally confirmed the ADP-ribosyl cyclase activity of the expressed CD38 by measuring its ability to catalyze the cyclization of the nicotinamide adenine dinucleotide (NAD+) surrogate, NGD+, to its fluorescent nonhydrolyzable derivative, cGDPr.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.2000.3041