Characterization and cytochemical localization of an ATP diphosphohydrolase from Leishmania amazonensis promastigotes
An ATP diphosphohydrolase was identified in the plasma membranes isolated from promastigote forms of Leishmania amazonensis. Both ATP and ADP were hydrolysed at similar rates by the enzyme. Other nucleotides such as UTP, GTP and CTP were also degraded, revealing a broad substrate specificity. Adding...
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| Veröffentlicht in: | Parasitology 2002-02, Vol.124 (2), p.137-143 |
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| creator | COIMBRA, E. S. GONÇALVES-DA-COSTA, S. C. CORTE-REAL, S. DE FREITAS, F. G. R. DURÃO, A. C. SOUZA, C. S. F. SILVA-SANTOS, M. I. VASCONCELOS, E. G. |
| description | An ATP diphosphohydrolase was identified in the plasma membranes isolated from promastigote forms of Leishmania amazonensis. Both ATP and ADP were hydrolysed at similar rates by the enzyme. Other nucleotides such as UTP, GTP and CTP were also degraded, revealing a broad substrate specificity. Adding ATP and ADP simultaneously, the amount of hydrolysis achieved was compatible with the presence of a single enzyme. ATPase activity was not affected by addition of vanadate, ouabain, thapsigargin, dicyclohexylcarbodiimide, oligomycin and bafilomycin A, thus excluding involvement of P-, F- and V-type ATPases. The effects of pH in the range 6·5–8·5 were examined using ATP or p-NPP as substrate. At pH 7·4, the phosphatase activity decreased, and did not show a significant contribution to ATP hydrolysis. In addition, the enzyme was not inhibited by levamisole and ammonium molybdate, excluding alkaline phosphatase and nucleotidase activities, respectively. Sodium azide (5–10 mM) caused inhibition of the ATP and ADP hydrolysis in a dose-dependent manner. Calcium was the best activating metal ion for both ATPase and ADPase activities. Ultrastructural cytochemical microscopy showed ATP diphosphohydrolase on the surface and flagellar pocket of the parasite. We have proposed that L. amazonensis ATP diphosphohydrolase may participate in the salvage pathway of nucleosides. |
| doi_str_mv | 10.1017/S0031182001001056 |
| format | Article |
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S. ; GONÇALVES-DA-COSTA, S. C. ; CORTE-REAL, S. ; DE FREITAS, F. G. R. ; DURÃO, A. C. ; SOUZA, C. S. F. ; SILVA-SANTOS, M. I. ; VASCONCELOS, E. G.</creator><creatorcontrib>COIMBRA, E. S. ; GONÇALVES-DA-COSTA, S. C. ; CORTE-REAL, S. ; DE FREITAS, F. G. R. ; DURÃO, A. C. ; SOUZA, C. S. F. ; SILVA-SANTOS, M. I. ; VASCONCELOS, E. G.</creatorcontrib><description>An ATP diphosphohydrolase was identified in the plasma membranes isolated from promastigote forms of Leishmania amazonensis. Both ATP and ADP were hydrolysed at similar rates by the enzyme. Other nucleotides such as UTP, GTP and CTP were also degraded, revealing a broad substrate specificity. Adding ATP and ADP simultaneously, the amount of hydrolysis achieved was compatible with the presence of a single enzyme. ATPase activity was not affected by addition of vanadate, ouabain, thapsigargin, dicyclohexylcarbodiimide, oligomycin and bafilomycin A, thus excluding involvement of P-, F- and V-type ATPases. The effects of pH in the range 6·5–8·5 were examined using ATP or p-NPP as substrate. At pH 7·4, the phosphatase activity decreased, and did not show a significant contribution to ATP hydrolysis. In addition, the enzyme was not inhibited by levamisole and ammonium molybdate, excluding alkaline phosphatase and nucleotidase activities, respectively. Sodium azide (5–10 mM) caused inhibition of the ATP and ADP hydrolysis in a dose-dependent manner. Calcium was the best activating metal ion for both ATPase and ADPase activities. Ultrastructural cytochemical microscopy showed ATP diphosphohydrolase on the surface and flagellar pocket of the parasite. We have proposed that L. amazonensis ATP diphosphohydrolase may participate in the salvage pathway of nucleosides.</description><identifier>ISSN: 0031-1820</identifier><identifier>EISSN: 1469-8161</identifier><identifier>DOI: 10.1017/S0031182001001056</identifier><identifier>PMID: 11862992</identifier><identifier>CODEN: PARAAE</identifier><language>eng</language><publisher>Cambridge, UK: Cambridge University Press</publisher><subject>Adenosine diphosphate ; Adenosine Diphosphate - metabolism ; Adenosine Triphosphate - metabolism ; Ammonium ; Animals ; apyrase ; Apyrase - antagonists & inhibitors ; Apyrase - isolation & purification ; Apyrase - metabolism ; ATP ; ATP diphosphohydrolase ; Biological and medical sciences ; Calcium - chemistry ; Cell Membrane - enzymology ; Cell Membrane - ultrastructure ; Enzyme Inhibitors - pharmacology ; Female ; Fundamental and applied biological sciences. Psychology ; Hydrogen-Ion Concentration ; Hydrolysis ; Leishmania - enzymology ; Leishmania - ultrastructure ; Leishmania amazonensis ; Levamisole - pharmacology ; Life cycle. Host-agent relationship. Pathogenesis ; Mice ; Mice, Inbred BALB C ; Microscopy, Electron ; Molybdenum - chemistry ; Parasites ; promastigote ; Protozoa ; Sodium Azide - chemistry ; Substrate Specificity</subject><ispartof>Parasitology, 2002-02, Vol.124 (2), p.137-143</ispartof><rights>2002 Cambridge University Press</rights><rights>2002 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c467t-be2798cc9aec439841aa921255148b095a67a5a8d7582dee5697136781f6f5f83</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.cambridge.org/core/product/identifier/S0031182001001056/type/journal_article$$EHTML$$P50$$Gcambridge$$H</linktohtml><link.rule.ids>164,315,782,786,27933,27934,55637</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=13934171$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11862992$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>COIMBRA, E. S.</creatorcontrib><creatorcontrib>GONÇALVES-DA-COSTA, S. C.</creatorcontrib><creatorcontrib>CORTE-REAL, S.</creatorcontrib><creatorcontrib>DE FREITAS, F. G. R.</creatorcontrib><creatorcontrib>DURÃO, A. C.</creatorcontrib><creatorcontrib>SOUZA, C. S. F.</creatorcontrib><creatorcontrib>SILVA-SANTOS, M. I.</creatorcontrib><creatorcontrib>VASCONCELOS, E. G.</creatorcontrib><title>Characterization and cytochemical localization of an ATP diphosphohydrolase from Leishmania amazonensis promastigotes</title><title>Parasitology</title><addtitle>Parasitology</addtitle><description>An ATP diphosphohydrolase was identified in the plasma membranes isolated from promastigote forms of Leishmania amazonensis. Both ATP and ADP were hydrolysed at similar rates by the enzyme. Other nucleotides such as UTP, GTP and CTP were also degraded, revealing a broad substrate specificity. Adding ATP and ADP simultaneously, the amount of hydrolysis achieved was compatible with the presence of a single enzyme. ATPase activity was not affected by addition of vanadate, ouabain, thapsigargin, dicyclohexylcarbodiimide, oligomycin and bafilomycin A, thus excluding involvement of P-, F- and V-type ATPases. The effects of pH in the range 6·5–8·5 were examined using ATP or p-NPP as substrate. At pH 7·4, the phosphatase activity decreased, and did not show a significant contribution to ATP hydrolysis. In addition, the enzyme was not inhibited by levamisole and ammonium molybdate, excluding alkaline phosphatase and nucleotidase activities, respectively. Sodium azide (5–10 mM) caused inhibition of the ATP and ADP hydrolysis in a dose-dependent manner. Calcium was the best activating metal ion for both ATPase and ADPase activities. Ultrastructural cytochemical microscopy showed ATP diphosphohydrolase on the surface and flagellar pocket of the parasite. We have proposed that L. amazonensis ATP diphosphohydrolase may participate in the salvage pathway of nucleosides.</description><subject>Adenosine diphosphate</subject><subject>Adenosine Diphosphate - metabolism</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Ammonium</subject><subject>Animals</subject><subject>apyrase</subject><subject>Apyrase - antagonists & inhibitors</subject><subject>Apyrase - isolation & purification</subject><subject>Apyrase - metabolism</subject><subject>ATP</subject><subject>ATP diphosphohydrolase</subject><subject>Biological and medical sciences</subject><subject>Calcium - chemistry</subject><subject>Cell Membrane - enzymology</subject><subject>Cell Membrane - ultrastructure</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrolysis</subject><subject>Leishmania - enzymology</subject><subject>Leishmania - ultrastructure</subject><subject>Leishmania amazonensis</subject><subject>Levamisole - pharmacology</subject><subject>Life cycle. Host-agent relationship. Pathogenesis</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Microscopy, Electron</subject><subject>Molybdenum - chemistry</subject><subject>Parasites</subject><subject>promastigote</subject><subject>Protozoa</subject><subject>Sodium Azide - chemistry</subject><subject>Substrate Specificity</subject><issn>0031-1820</issn><issn>1469-8161</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><recordid>eNp1kd9rFDEQx4NY7Hn6B_giQdC3rfmxSTaP5dBWOGzFCsWXMJfNdlN3N9dkF7z-9ea41QNFyCQP389MvjOD0CtKziih6v1XQjilFSOE7o-QT9CCllIXFZX0KVrs5WKvn6LnKd0TQiSX7Bk6zUmSac0WaFq1EMGOLvpHGH0YMAw1trsx2Nb13kKHu5Dv32poMoDPb65x7bdtSDnaXR1DB8nhJoYer51PbQ-DBww9PIbBDcknvM0apNHfhdGlF-ikgS65l_O7RN8-frhZXRbrq4tPq_N1YUupxmLjmNKVtRqcLbmuSgqgGWVC0LLaEC1AKhBQ1UpUrHZOSK0ol6qijWxEU_Eleneom39_mFwaTe-TdV0HgwtTMnkMRBLGM_jmL_A-THHI3gzLE83BZYboAbIxpBRdY7bR9xB3hhKzX4j5ZyE55_VceNr0rj5mzBvIwNsZgJTn3EQYrE9Hjmte0tzVEhUHzqfR_fyjQ_xhpOJKGHnxxXxfcXp5e_vZiMzz2Sz0m-jrO3ds6f92fwFcqbHl</recordid><startdate>20020201</startdate><enddate>20020201</enddate><creator>COIMBRA, E. 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S. ; GONÇALVES-DA-COSTA, S. C. ; CORTE-REAL, S. ; DE FREITAS, F. G. R. ; DURÃO, A. C. ; SOUZA, C. S. F. ; SILVA-SANTOS, M. I. ; VASCONCELOS, E. 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Psychology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydrolysis</topic><topic>Leishmania - enzymology</topic><topic>Leishmania - ultrastructure</topic><topic>Leishmania amazonensis</topic><topic>Levamisole - pharmacology</topic><topic>Life cycle. Host-agent relationship. Pathogenesis</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Microscopy, Electron</topic><topic>Molybdenum - chemistry</topic><topic>Parasites</topic><topic>promastigote</topic><topic>Protozoa</topic><topic>Sodium Azide - chemistry</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>COIMBRA, E. S.</creatorcontrib><creatorcontrib>GONÇALVES-DA-COSTA, S. C.</creatorcontrib><creatorcontrib>CORTE-REAL, S.</creatorcontrib><creatorcontrib>DE FREITAS, F. G. R.</creatorcontrib><creatorcontrib>DURÃO, A. C.</creatorcontrib><creatorcontrib>SOUZA, C. S. F.</creatorcontrib><creatorcontrib>SILVA-SANTOS, M. 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S.</au><au>GONÇALVES-DA-COSTA, S. C.</au><au>CORTE-REAL, S.</au><au>DE FREITAS, F. G. R.</au><au>DURÃO, A. C.</au><au>SOUZA, C. S. F.</au><au>SILVA-SANTOS, M. I.</au><au>VASCONCELOS, E. G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization and cytochemical localization of an ATP diphosphohydrolase from Leishmania amazonensis promastigotes</atitle><jtitle>Parasitology</jtitle><addtitle>Parasitology</addtitle><date>2002-02-01</date><risdate>2002</risdate><volume>124</volume><issue>2</issue><spage>137</spage><epage>143</epage><pages>137-143</pages><issn>0031-1820</issn><eissn>1469-8161</eissn><coden>PARAAE</coden><abstract>An ATP diphosphohydrolase was identified in the plasma membranes isolated from promastigote forms of Leishmania amazonensis. Both ATP and ADP were hydrolysed at similar rates by the enzyme. Other nucleotides such as UTP, GTP and CTP were also degraded, revealing a broad substrate specificity. Adding ATP and ADP simultaneously, the amount of hydrolysis achieved was compatible with the presence of a single enzyme. ATPase activity was not affected by addition of vanadate, ouabain, thapsigargin, dicyclohexylcarbodiimide, oligomycin and bafilomycin A, thus excluding involvement of P-, F- and V-type ATPases. The effects of pH in the range 6·5–8·5 were examined using ATP or p-NPP as substrate. At pH 7·4, the phosphatase activity decreased, and did not show a significant contribution to ATP hydrolysis. In addition, the enzyme was not inhibited by levamisole and ammonium molybdate, excluding alkaline phosphatase and nucleotidase activities, respectively. Sodium azide (5–10 mM) caused inhibition of the ATP and ADP hydrolysis in a dose-dependent manner. Calcium was the best activating metal ion for both ATPase and ADPase activities. Ultrastructural cytochemical microscopy showed ATP diphosphohydrolase on the surface and flagellar pocket of the parasite. We have proposed that L. amazonensis ATP diphosphohydrolase may participate in the salvage pathway of nucleosides.</abstract><cop>Cambridge, UK</cop><pub>Cambridge University Press</pub><pmid>11862992</pmid><doi>10.1017/S0031182001001056</doi><tpages>7</tpages></addata></record> |
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| subjects | Adenosine diphosphate Adenosine Diphosphate - metabolism Adenosine Triphosphate - metabolism Ammonium Animals apyrase Apyrase - antagonists & inhibitors Apyrase - isolation & purification Apyrase - metabolism ATP ATP diphosphohydrolase Biological and medical sciences Calcium - chemistry Cell Membrane - enzymology Cell Membrane - ultrastructure Enzyme Inhibitors - pharmacology Female Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Hydrolysis Leishmania - enzymology Leishmania - ultrastructure Leishmania amazonensis Levamisole - pharmacology Life cycle. Host-agent relationship. Pathogenesis Mice Mice, Inbred BALB C Microscopy, Electron Molybdenum - chemistry Parasites promastigote Protozoa Sodium Azide - chemistry Substrate Specificity |
| title | Characterization and cytochemical localization of an ATP diphosphohydrolase from Leishmania amazonensis promastigotes |
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