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Journal of Histochemistry and Cytochemistry, Vol. 50, 549-556, April 2002, Copyright © 2002, The Histochemical Society, Inc.

ARTICLE

Localization of NTPDase1/CD39 in Normal and Transformed Human Pancreas

Agnes Kittela, Marta Garridob, and Gábor Vargaa
a Department of Pathophysiology, Laboratory of Gastrointestinal Research, Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary,
b Institut Municipal d'Investigació Medica, Universitat Pompeu Fabra, Barcelona, Spain

Correspondence to: Agnes Kittel, Inst. of Experimental Medicine, Hungarian Academy of Sciences, PO Box 67, 1450 Budapest, Hungary. E-mail: kittel@koki.hu

Elevated levels of extracellular ATP have been observed in many tumors. We have localized NTPDase1/CD39, one of the principal extracellular nucleotide-hydrolyzing enzymes, in normal and cancerous human pancreas. NTPDase/E-ATPDase activity was demonstrated with an enzyme histochemical technique on cryosections of human pancreas. Acinar and duct epithelial cells were devoid of E-ATPDase activity in both normal and transformed tissue. Endothelial cells and smooth muscle around blood vessels and larger ducts showed strong activity. Nerves, connective tissue, and the ß-cells of the islets were also stained. In cancerous tissue this activity was diminished in the smooth muscle around the ducts and was absent from newly formed connective tissue. Immunostaining for CD39 supported these results but revealed the presence of inactive CD39 in the duct epithelial cells. We hypothesize that the significantly diminished activity of NTPDase1 in the tissues surrounding the ducts may be associated with the processes that lead to tumor formation in human pancreas. (J Histochem Cytochem 50:549–555, 2002)

Key Words: NTPDase1/CD39, extracellular nucleotides, ATP, purinoceptors, pancreas, tumor, islets


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