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J. Biol. Chem., Vol. 281, Issue 40, 29441-29447, October 6, 2006

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ATP-consuming and ATP-generating Enzymes Secreted by Pancreas^*

Gennady G. Yegutkin, Sergei S. Samburski, Sirpa Jalkanen, and Ivana Novak¹

From the MediCity Research Laboratory and Department of Medical Microbiology, Turku University and National Public Health Institute, FIN-2050 Turku, Finland and the Institute of Molecular Biology and Physiology, August Krogh Building, University of Copenhagen, Universitetsparken 13, DK-2100 Copenhagen Ø, Denmark

Pancreatic acini release ATP in response to various stimuli, including cholecystokinin octapeptide (CCK-8), as we show in the present study. There were indications that pancreatic juice also contains enzymes that could hydrolyze ATP during its passage through the ductal system. The aim of this study was to determine which ATP-degrading and possibly ATP-generating enzymes were present in pancreatic secretion. For this purpose, pancreatic juice was collected from anesthetized rats stimulated with infusion of CCK-8. Purine-converting activities in juice samples were assayed by TLC using either [-³²P]ATP or ¹⁴C/³H-labeled and unlabeled nucleotides as appropriate substrates. Data show that the juice contains the enzyme ecto-nucleoside triphosphate diphosphohydrolase that can hydrolyze both [¹⁴C]ATP and [³H]ADP about equally well, i.e. CD39. Reverse-phase high-performance liquid chromatography analysis additionally shows that this enzyme has broad substrate specificity toward other nucleotides, UTP, UDP, ITP, and IDP. In addition, secretion contains ecto-5'-nucleotidase, CD73, further converting [³H]AMP to adenosine. Along with highly active hydrolytic enzymes, there were also ATP-generating enzymes in pancreatic juice, adenylate kinase, and NDP kinase, capable of sequentially phosphorylating AMP via ADP to ATP. Activities of nonspecific phosphatases, nucleotide pyrophosphatase/phosphodiesterases, and adenosine deaminase were negligible. Taken together, CCK-8 stimulation of pancreas causes release of both ATP-consuming and ATP-generating enzymes into pancreatic juice. This newly discovered richness of secreted enzymes underscores the importance of purine signaling between acini and pancreatic ducts lumen and implies regulation of the purine-converting enzymes release.

Received for publication, March 16, 2006 , and in revised form, May 19, 2006.

^* This work was supported by the Finnish Academy, the Sigrid Juselius Foundation (to G. G. Y); and the Danish Medical and Science Research Councils and Novo Nordisk Foundation (to I. N.). 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.

¹ To whom correspondence should be addressed. Tel.: 45-3532-1645; Fax: 45-3532-1567; E-mail: inovak{at}aki.ku.dk.

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