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Catalytic properties of the retinal rod outer segment disk ADP-ribosyl cyclase

Published online by Cambridge University Press:  27 January 2011

ANDREA FABIANO ,
ISABELLA PANFOLI ,
DANIELA CALZIA ,
MAURIZIO BRUSCHI ,
SILVIA RAVERA ,
ANGELA BACHI ,
ANGELA CATTANEO ,
ALESSANDRO MORELLI  and
GIOVANNI CANDIANO
ANDREA FABIANO
Affiliation:
Department of Biology, University of Genoa, Genova, Italy
ISABELLA PANFOLI*
Affiliation:
Department of Biology, University of Genoa, Genova, Italy
DANIELA CALZIA
Affiliation:
Department of Biology, University of Genoa, Genova, Italy
MAURIZIO BRUSCHI
Affiliation:
Laboratory on Pathophysiology of Uraemia G. Gaslini Children Hospital, Genoa, Genova, Italy
SILVIA RAVERA
Affiliation:
Department of Biology, University of Genoa, Genova, Italy
ANGELA BACHI
Affiliation:
DIBIT-San Raffaele Scientific Institute, Milano, Italy
ANGELA CATTANEO
Affiliation:
DIBIT-San Raffaele Scientific Institute, Milano, Italy
ALESSANDRO MORELLI
Affiliation:
Department of Biology, University of Genoa, Genova, Italy
GIOVANNI CANDIANO
Affiliation:
Laboratory on Pathophysiology of Uraemia G. Gaslini Children Hospital, Genoa, Genova, Italy
*
†Address correspondence and reprint requests to: Dr. Isabella Panfoli, Dipartimento di Biologia, Università di Genova, V.le Benedetto XV, 3 16132 Genova, Italy. E-mail: Isabella.Panfoli@unige.it
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Abstract

Cyclic ADP-ribose (cADPR) is a second messenger modulating intracellular calcium levels. We have previously described a cADPR-dependent calcium signaling pathway in bovine rod outer segments (ROS), where calcium ions play a pivotal role. ROS ADP-ribosyl cyclase (ADPR-cyclase) was localized in the membrane fraction. In the present work, we examined the properties of the disk ADPR-cyclase through the production of cyclic GDP-ribose from the NAD+ analogue NGD+. The enzyme displayed an estimated Km for NGD+ of 12.5 ± 0.3 μM, a Vmax of 26.50 ± 0.70 pmol cyclic GDP-ribose synthesized/min/mg, and optimal pH of 6.5. The effect of divalent cations (Zn2+, Cu2+, and Ca2+) was also tested. Micromolar Zn2+ and Cu2+ inhibited the disk ADPR-cyclase activity (half maximal inhibitory concentration, IC50 = 1.1 and 3.6 μM, respectively). By contrast, Ca2+ ions had no effect. Interestingly, the properties of the intracellular membrane–associated ROS disk ADPR-cyclase are more similar to those of the ADPR-cyclase found in CD38-deficient mouse brain, than to those of CD38 or CD157. The novel intracellular mammalian ADPR-cyclase would elicit Ca2+ release from the disks at various rates in response to change in free Ca2+ concentrations, caused by light versus dark adaptation, in fact there was no difference in disk ADPR-cyclase activity in light or dark conditions. Data suggest that disk ADPR-cyclase may be a potential target of retinal toxicity of Zn2+ and may shed light to the role of Cu2+ and Zn2+ deficiency in retina.

Keywords

ADPR-cyclaseCalcium ionCyclic ADP-ribose disksNGD+Phototrasduction
Type
Research Articles
Information
Visual Neuroscience , Volume 28 , Issue 2 , March 2011 , pp. 121 - 128
Copyright
Copyright © Cambridge University Press 2011

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