Sperm express a Ca2+-regulated NAADP synthase.

The Biochemical Journal
Sridhar R VasudevanG C Churchill

Abstract

NAADP (nicotinic acid-adenine dinucleotide phosphate), the most potent Ca2+-mobilizing second messenger, is active in a wide range of organisms and cell types. Until now, all NAADP-producing enzymes have been thought to be members of the ADP-ribosyl cyclase family. ADP-ribosyl cyclases exhibit promiscuous substrate selectivity, synthesize a variety of products and are regulated in a limited manner, which may be non-physiological. In the present paper, we report the presence of an enzyme on the surface of sea urchin sperm that exhibits bell-shaped regulation by Ca2+ over a range (EC(50) of 10 nM and IC(50) of 50 microM) that is physiologically relevant. Uniquely, this surface enzyme possesses complete selectivity for nucleotides with a 2'-phosphate group and exhibits only base-exchange activity without any detectable cyclase activity. Taken together, these findings indicate that this novel enzyme should be considered as the first true NAADP synthase.

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Citations

Jan 24, 2014·Molecular Biology of the Cell·Lilli ArndtIngrid Boekhoff
Dec 12, 2012·Cell Calcium·Isabela Ramos, Gary M Wessel
May 13, 2015·Reproduction : the Official Journal of the Society for the Study of Fertility·Joao CorreiaStephen Publicover
Jun 12, 2010·Communicative & Integrative Biology·Michael X ZhuAntony Galione
Oct 21, 2011·Physiological Reviews·Alberto DarszonClaudia L Treviño
Mar 13, 2008·The Biochemical Journal·Guy A Rutter, Elisa A Bellomo
Jul 28, 2020·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Tae-Sik NamUh-Hyun Kim
Apr 14, 2016·Biochemical Society Transactions·Anthony J Morgan
Apr 13, 2021·Neuroscience Research·Keiji Ibata, Michisuke Yuzaki
Nov 6, 2008·Science Signaling·Andreas H Guse, Hon Cheung Lee

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