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J. Biol. Chem., Vol. 280, Issue 44, 37289-37296, November 4, 2005

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Phosphodiesterase Activity of Alkaline Phosphatase in ATP-initiated Ca²⁺ and Phosphate Deposition in Isolated Chicken Matrix Vesicles^*

Le Zhang1, Marcin Balcerzak, Jacqueline Radisson, Cyril Thouverey, Slawomir Pikula, Gérard Azzar, and René Buchet

From the Laboratoire de Physico-Chimie Biologique, UMR CNRS 5013, Université Claude Bernard Lyon 1, UFR de Chimie-Biochimie F-69622 Villeurbanne, France and the Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warsaw, Poland

Inorganic pyrophosphate is a potent inhibitor of bone mineralization by preventing the seeding of calcium-phosphate complexes. Plasma cell membrane glycoprotein-1 and tissue nonspecific alkaline phosphatase were reported to be antagonistic regulators of mineralization toward inorganic pyrophosphate formation (by plasma cell membrane glycoprotein-1) and degradation (by tissue nonspecific alkaline phosphatase) under physiological conditions. In addition, they possess broad overlapping enzymatic functions. Therefore, we examined the roles of tissue nonspecific alkaline phosphatase within matrix vesicles isolated from femurs of 17-day-old chick embryos, under conditions where these both antagonistic and overlapping functions could be evidenced. Addition of 25 µM ATP significantly increased duration of mineralization process mediated by matrix vesicles, while supplementation of mineralization medium with levamisole, an alkaline phosphatase inhibitor, reduces the ATP-induced retardation of mineral formation. Phosphodiesterase activity of tissue nonspecific alkaline phosphatase for bis-p-nitrophenyl phosphate was confirmed, the rate of this phosphodiesterase activity is in the same range as that of phosphomonoesterase activity for p-nitrophenyl phosphate under physiological pH. In addition, tissue nonspecific alkaline phosphatase at pH 7.4 can hydrolyze ADPR. On the basis of these observations, it can be concluded that tissue nonspecific alkaline phosphatase, acting as a phosphomonoesterase, could hydrolyze free phosphate esters such as pyrophosphate and ATP, while as phosphodiesterase could contribute, together with plasma cell membrane glycoprotein-1, in the production of pyrophosphate from ATP.

Received for publication, April 19, 2005 , and in revised form, September 6, 2005.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Deceased.

¹ To whom correspondence should be addressed: Université Claude Bernard Lyon 1, UFR Chimie-Biochimie UMR CNRS 5013, 43 Boulevard du 11 Novembre 1918, 69622 Villeurbanne Cedex, France. Tel.: 33-4-7243-1320; Fax: 33-4-7243-1543; E-mail: le_zhang{at}hotmail.com.

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