title: Localization of nucleoside triphosphate diphosphohydrolase-1 (NTPDase1) and NTPDase2 in pancreas and salivary gland.
abstract: Ectonucleoside triphosphate diphosphohydrolases (NTPDases) are membrane-bound ectoenzymes that hydrolyze extracellular nucleotides. We investigated the distribution of NTPDase1 and NTPDase2 in murine salivary gland and pancreas. Histochemistry and immunostaining (by both light and electron microscopy), combined with functional assays, were used to describe the localization patterns and enzyme activities in the organs of wild-type and NTPDase1/cd39-null mice. Pancreatic acinar cells and salivary gland acinar/myoepithelial cells were positive for NTPDase1 and NTPDase2. Ecto-ATPase activity was slightly higher in salivary glands. Ductal epithelial cells expressed ecto-ATPase activity but NTPDase1 and NTPDase2 expression were weak at best. ATPase activity was found in blood vessels of both tissues and its localization pattern overlapped with NTPDase1 staining. In these structures, NTPDase2 antibodies stained the basolateral aspect of endothelial cells and the supporting cells. Biochemical assays and histochemical staining showed relatively high levels of ATPase activity in both glands of cd39(-/-) mice. Our data therefore support a physiological role for NTPDase2 and other ectonucleotidases in the pancreas and salivary glands. Because NTPDase1 is expressed in non-vascular cell types, this finding suggests that NTPDase1 may have functions in the gastrointestinal tract that differ from those demonstrated in the vascular system.
authors.affiliation: Department of Pharmacology, Institute of Experimental Medicine, Hungarian Academy of Sciences, PO Box 67, 1450 Budapest, Hungary. kittel@koki.hu
authors.forename: Agnes
authors.initials: A
authors.lastname: Kittel
authors.forename: Julie
authors.initials: J
authors.lastname: Pelletier
authors.forename: François
authors.initials: F
authors.lastname: Bigonnesse
authors.forename: Olaf
authors.initials: O
authors.lastname: Guckelberger
authors.forename: Krisztina
authors.initials: K
authors.lastname: Kordás
authors.forename: Norbert
authors.initials: N
authors.lastname: Braun
authors.forename: Simon C
authors.initials: SC
authors.lastname: Robson
authors.forename: Jean
authors.initials: J
authors.lastname: Sévigny
mesh_terms: D000251:Adenosine Triphosphatases / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D015703:Antigens, CD / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D001081:Apyrase; D007150:Immunohistochemistry; D008297:Male; D051379:Mice; D008810:Mice, Inbred C57BL; D008817:Mice, Mutant Strains; D010179:Pancreas / Q000201:enzymology* / Q000648:ultrastructure; D012469:Salivary Glands / Q000201:enzymology* / Q000648:ultrastructure; D013363:Submandibular Gland / Q000201:enzymology* / Q000648:ultrastructure
chemical_list: D015703:Antigens, CD; D000251:Adenosine Triphosphatases; C027201:ectoATPase; D001081:Apyrase; C067869:CD39 antigen