ATPase-ADPase activities of rat placental tissue

Pieber, M.; Valenzuela, Manuel; Kettlun, Ana M.; Mancilla, Marta; Aranda, Evelyn; Collados, L.; Traverso-Cori, A.

doi:10.1016/0305-0491(91)90375-n

Cited by 15 publications

(8 citation statements)

References 29 publications

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“…Since then, however, the catalytic unit of the enzyme has not be established with certainty. Other ATPDases have been found in vertebrate cells, including those of blood vessels [7][8][9][10][11][12][13][14][15][16]. Some evidence agrees with the view that the catalytic site of the ATPDase on endothelial and smooth muscle cells of blood vessels and trachea is a component of plasma membranes and would be responsible for the major part of the ectoADPase and ectoATPase activities at the cell surface [8,17].…”

Section: Introductionsupporting

confidence: 59%

Purification of pancreas type-I ATP diphosphohydrolase and identification by affinity labelling with the 5′-p-fluorosulphonylbenzoyladenosine ATP analogue

Sévigny

Côté

Beaudoin

1995

Biochemical Journal

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The enzyme recently identified as type-I ATP diphosphohydrolase (ATPDase; EC 3.6.1.5) has been purified from the zymogen granule membrane of pig pancreas. After solubilization with Triton X-100 and chromatographies on ion-exchange and Affi-Gel Blue columns an approximate 3500-fold purification was obtained. The enzyme preparation with a specific activity of 45 units/mg of protein was much further purified by PAGE under non-denaturing conditions. The active band localized on the gel contained two proteins after SDS/PAGE and silver staining, corresponding to apparent molecular masses of 56 and 54 kDa. The identity of the ATPDase was confirmed by an affinity labelling technique with 5'-p-fluorosulphonylbenzoyladenosine (FSBA) as an ATP analogue. The latter was detected by a Western blot technique. A strong reaction was observed with the band corresponding to 54 kDa. N-terminal sequence analysis revealed that the 56 kDa protein has significant similarities (50-72%) with lipases, whereas the 54 kDa enzyme has no significant similarity with any known proteins. N-glycosidase F treatment confirmed the glycoprotein nature of the enzyme and suggested that the enzyme bears several N-glycosylation sites. Comparisons of molecular masses and biochemical properties show that this ATPDase is different from other reported mammalian ATPDases.

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Section: Introductionsupporting

confidence: 59%

Purification of pancreas type-I ATP diphosphohydrolase and identification by affinity labelling with the 5′-p-fluorosulphonylbenzoyladenosine ATP analogue

Sévigny

Côté

Beaudoin

1995

Biochemical Journal

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“…The enzyme, responsible for the ecto-ATPase activity in myocytes, is likely NTPDase2. This assumption is supported by several previous works (Knowles and Kaplan 1981;Pieber et al 1991;Plesner 1995;Braun et al 2004;Kittel et al 2004). The NTPDase2, this ecto-ATPase, undistinguishable from NTPDase1 by enzyme histochemical method or HPLC, was found together with NTPDase1 in almost every tissue investigated but predominantly in the heart (Yeung et al 2000).…”

Section: Discussionsupporting

confidence: 50%

Expression of NTPDase1 and caveolins in human cardiovascular disease

Kittel

Kiss

Müllner

et al. 2005

Histochem Cell Biol

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Pathological circumstances like inflammation or ischemic insult facilitate the release of adenine nucleotides from several types of cells. These extracellular nucleotides are rapidly converted to adenosine by ectonucleotidases, mainly ectonucleoside triphosphate diphosphohydrolase1 (NTPDase1/CD39) and CD73. NTPDase1/CD39 can interact with caveolins, structural proteins of signal-transducing microdomains termed caveolae. Caveolins are thought to have physiological roles in heart ageing and cardiac diseases. The aim of this study was to investigate the expression of NTPDase1 together with caveolins in chronic human cardiovascular diseases and elucidate their role in human heart. The HPLC analysis showed significant increase in ATPase activity in pathological samples from patients with ischemic heart disease. Immunostaining also showed alterations in the expression and distribution of NTPDase1. Caveolin-1 and caveolin-2 expression was much alike in control and pathological cases, while expression of caveolin-3 was lower in pathological samples. Changes in the expression of NTPDase1 and caveolins seem to be independent of human cardiovascular disease.

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“…Wang et al have noted that recombinant rat ectoapyrase could form a tetramer that did not appear to require intermolecular disulfide bonds (33). These and other observations examining CD39 multimer formation dependent upon disulfide bonds (19,40) should be considered in the light of prior data derived from gel filtration and 60 Co irradiation inactivation techniques which suggest that mammalian ATPDases, including those of the rat placenta and kidney, exist as active monomeric forms under nondenaturing conditions (41)(42)(43). Thus, multiple factors may influence enzymatic activity associated with the formation of multimers including the effects of limited proteolysis, as alluded to above.…”

Section: Discussionmentioning

confidence: 96%

Structural Elements and Limited Proteolysis of CD39 Influence ATP Diphosphohydrolase Activity

et al. 1999

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CD39, the mammalian ATP diphosphohydrolase (ATPDase), is thought to contain two transmembrane domains and five "apyrase conserved regions" (ACR) within a large extracellular region. To study the structure of this ectoenzyme, human CD39 was modified by directed mutations within these ACRs or by sequential deletions at both termini. ATPDase activity was well preserved with FLAG tagging, followed by the removal of either of the demonstrated C- or N-transmembrane regions. However, deletions within ACR-1 (aa 54-61) or -4 (aa 212-220), as well as truncation mutants that included ACR-1, -4, or -5 (aa 447-454), resulted in substantive loss of biochemical activity. Intact ACR-1, -4, and -5 within CD39 are therefore required for maintenance of biochemical activity. Native and mutant forms of CD39 lacking TMR were observed to undergo multimerization, associated with the formation of intermolecular disulfide bonds. Limited tryptic cleavage of intact CD39 resulted in two noncovalently membrane-associated fragments (56 and 27 kDa) that substantially augmented ATPDase activity. Glycosylation variation accounted for minor heterogeneity in native and mutant forms of CD39 but did not influence ATPDase function. Enzymatic activity of ATPDase may be influenced by certain posttranslational modifications that are relevant to vascular inflammation.

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ATPase-ADPase activities of rat placental tissue

Cited by 15 publications

References 29 publications

Purification of pancreas type-I ATP diphosphohydrolase and identification by affinity labelling with the 5′-p-fluorosulphonylbenzoyladenosine ATP analogue

Purification of pancreas type-I ATP diphosphohydrolase and identification by affinity labelling with the 5′-p-fluorosulphonylbenzoyladenosine ATP analogue

Expression of NTPDase1 and caveolins in human cardiovascular disease

Structural Elements and Limited Proteolysis of CD39 Influence ATP Diphosphohydrolase Activity

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