Characterization and purification of a calcium-sensitive ATP diphosphohydrolase from pig pancreas.

Lebel, Denis; Poirier, Guy G.; Phaneuf, S; St-Jean, P; Laliberte, Jean Francois; Beaudoin, Adrien R.

doi:10.1016/s0021-9258(19)86167-7

Cited by 127 publications

(22 citation statements)

References 28 publications

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“…The presence of E-ATPDase activity has previously been demonstrated on several cell types in the exocrine pancreas of rat and pig (LeBel et al 1980;Sévigny et al 1998;Beaudoin et al 1999). Both basolateral and apical membranes of the acinar cells were positive, as were the membranes of zymogen granules in the acinar cells.…”

Section: Discussionmentioning

confidence: 78%

Localization of NTPDase1/CD39 in Normal and Transformed Human Pancreas

Kittel

Garrido

Varga

2002

J Histochem Cytochem.

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S U M M A R Y 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 ␤ -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.

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Section: Discussionmentioning

confidence: 78%

Localization of NTPDase1/CD39 in Normal and Transformed Human Pancreas

Kittel

Garrido

Varga

2002

J Histochem Cytochem.

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“…Biochemical ATPase Assays After Method of Le Bel. Intact pEC or hEC preparations were incubated with 5-200 M ADP or ATP, and free phosphate release was determined over time (30).…”

Section: Endothelial Cell Atpdase Assaysmentioning

confidence: 99%

Loss of ATP Diphosphohydrolase Activity with Endothelial Cell Activation

Robson

Kaczmarek

Siegel

et al. 1997

The Journal of Experimental Medicine

271

232

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Quiescent endothelial cells (EC) regulate blood flow and prevent intravascular thrombosis. This latter effect is mediated in a number of ways, including expression by EC of thrombomodulin and heparan sulfate, both of which are lost from the EC surface as part of the activation response to proinflammatory cytokines. Loss of these anticoagulant molecules potentiates the procoagulant properties of the injured vasculature. An additional thromboregulatory factor, ATP diphosphohydrolase (ATPDase; designated as EC 3.6.1.5) is also expressed by quiescent EC, and has the capacity to degrade the extracellular inflammatory mediators ATP and ADP to AMP, thereby inhibiting platelet activation and modulating vascular thrombosis. We describe here that the antithrombotic effects of the ATPDase, like heparan sulfate and thrombomodulin, are lost after EC activation, both in vitro and in vivo. Because platelet activation and aggregation are important components of the hemostatic changes that accompany inflammatory diseases, we suggest that the loss of vascular ATPDase may be crucial for the progression of vascular injury.

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“…An ATPDase has been purified and characterized from the zymogen granule membrane of pig pancreas (LeBel et al 1980;Laliberte et al 1982;Sevigny et al 1995). Immunolocalization was later performed in the porcine digestive system (Sevigny et al 1998) with an antiserum directed against the apyrase conserved region 4 (ACR-4) of NTPDases (Kaczmarek et al 1996;Sevigny et al 1997a).…”

mentioning

confidence: 99%

Localization of Nucleoside Triphosphate Diphosphohydrolase-1 (NTPDase1) and NTPDase2 in Pancreas and Salivary Gland

Kittel

Pelletier²,

Bigonnesse

et al. 2004

J Histochem Cytochem.

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S U M M A R YEctonucleoside 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 Ϫ / Ϫ 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.

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Characterization and purification of a calcium-sensitive ATP diphosphohydrolase from pig pancreas.

Cited by 127 publications

References 28 publications

Localization of NTPDase1/CD39 in Normal and Transformed Human Pancreas

Localization of NTPDase1/CD39 in Normal and Transformed Human Pancreas

Loss of ATP Diphosphohydrolase Activity with Endothelial Cell Activation

Localization of Nucleoside Triphosphate Diphosphohydrolase-1 (NTPDase1) and NTPDase2 in Pancreas and Salivary Gland

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