Involvement of calyculin A-sensitive phosphatase(s) in the differentiation of Trypanosoma cruzi trypomastigotes to amastigotes
Differentiation of the non-dividing trypomastigote form of Trypanosoma cruzi, the causative agent of Chagas disease, to the dividing amastigote form normally occurs in cytoplasm of infected cells. Here we show that calyculin A, a potent inhibitor of protein phosphatases 1 and 2A, induces at pH 7.5 e...
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| Veröffentlicht in: | Molecular and biochemical parasitology 1999-01, Vol.98 (2), p.239-252 |
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| container_title | Molecular and biochemical parasitology |
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| creator | Grellier, Philippe Blum, Joseph Santana, Jaime Bylèn, Eva Mouray, Elisabeth Sinou, Véronique Teixeira, Antonio R.L. Schrével, Joseph |
| description | Differentiation of the non-dividing trypomastigote form of
Trypanosoma cruzi, the causative agent of Chagas disease, to the dividing amastigote form normally occurs in cytoplasm of infected cells. Here we show that calyculin A, a potent inhibitor of protein phosphatases 1 and 2A, induces at pH 7.5 extracellular transformation of long slender trypomastigotes to round amastigote-like forms which acquire characteristic features observed after the normal differentiation process: repositioning and structural changes of the kinetoplast, release of surface neuraminidase, and expression of amastigote-specific epitopes. Calyculin A inhibits parasite phosphatases and changes in the phosphorylation of specific proteins occur during the transformation process. As an exposure of trypomastigotes to calyculin A concentrations as low as 1 nM and for only 1–2 h is sufficient to induce transformation, the inhibition of calyculin A-sensitive phosphatase(s) appears to play a major role in initiating the trypomastigote differentiation. |
| doi_str_mv | 10.1016/S0166-6851(98)00172-8 |
| format | Article |
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Trypanosoma cruzi, the causative agent of Chagas disease, to the dividing amastigote form normally occurs in cytoplasm of infected cells. Here we show that calyculin A, a potent inhibitor of protein phosphatases 1 and 2A, induces at pH 7.5 extracellular transformation of long slender trypomastigotes to round amastigote-like forms which acquire characteristic features observed after the normal differentiation process: repositioning and structural changes of the kinetoplast, release of surface neuraminidase, and expression of amastigote-specific epitopes. Calyculin A inhibits parasite phosphatases and changes in the phosphorylation of specific proteins occur during the transformation process. As an exposure of trypomastigotes to calyculin A concentrations as low as 1 nM and for only 1–2 h is sufficient to induce transformation, the inhibition of calyculin A-sensitive phosphatase(s) appears to play a major role in initiating the trypomastigote differentiation.</description><identifier>ISSN: 0166-6851</identifier><identifier>EISSN: 1872-9428</identifier><identifier>DOI: 10.1016/S0166-6851(98)00172-8</identifier><identifier>PMID: 10080392</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Animals ; Antigens, Protozoan - metabolism ; Calyculin A ; Cell Differentiation ; Chagas disease ; Differentiation ; Membrane Proteins - metabolism ; Neuraminidase - metabolism ; Oxazoles - pharmacology ; Phosphatase ; Phosphoprotein Phosphatases - antagonists & inhibitors ; Phosphorylation ; Protein Processing, Post-Translational ; Trypanosoma cruzi ; Trypanosoma cruzi - drug effects ; Trypanosoma cruzi - enzymology ; Trypanosoma cruzi - ultrastructure ; Trypanosome</subject><ispartof>Molecular and biochemical parasitology, 1999-01, Vol.98 (2), p.239-252</ispartof><rights>1999 Elsevier Science B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-24638572755786e90f813e719cacd4f11c58f0716bddb1b9c5bf9c1313e452203</citedby><cites>FETCH-LOGICAL-c392t-24638572755786e90f813e719cacd4f11c58f0716bddb1b9c5bf9c1313e452203</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0166685198001728$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10080392$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Grellier, Philippe</creatorcontrib><creatorcontrib>Blum, Joseph</creatorcontrib><creatorcontrib>Santana, Jaime</creatorcontrib><creatorcontrib>Bylèn, Eva</creatorcontrib><creatorcontrib>Mouray, Elisabeth</creatorcontrib><creatorcontrib>Sinou, Véronique</creatorcontrib><creatorcontrib>Teixeira, Antonio R.L.</creatorcontrib><creatorcontrib>Schrével, Joseph</creatorcontrib><title>Involvement of calyculin A-sensitive phosphatase(s) in the differentiation of Trypanosoma cruzi trypomastigotes to amastigotes</title><title>Molecular and biochemical parasitology</title><addtitle>Mol Biochem Parasitol</addtitle><description>Differentiation of the non-dividing trypomastigote form of
Trypanosoma cruzi, the causative agent of Chagas disease, to the dividing amastigote form normally occurs in cytoplasm of infected cells. Here we show that calyculin A, a potent inhibitor of protein phosphatases 1 and 2A, induces at pH 7.5 extracellular transformation of long slender trypomastigotes to round amastigote-like forms which acquire characteristic features observed after the normal differentiation process: repositioning and structural changes of the kinetoplast, release of surface neuraminidase, and expression of amastigote-specific epitopes. Calyculin A inhibits parasite phosphatases and changes in the phosphorylation of specific proteins occur during the transformation process. As an exposure of trypomastigotes to calyculin A concentrations as low as 1 nM and for only 1–2 h is sufficient to induce transformation, the inhibition of calyculin A-sensitive phosphatase(s) appears to play a major role in initiating the trypomastigote differentiation.</description><subject>Animals</subject><subject>Antigens, Protozoan - metabolism</subject><subject>Calyculin A</subject><subject>Cell Differentiation</subject><subject>Chagas disease</subject><subject>Differentiation</subject><subject>Membrane Proteins - metabolism</subject><subject>Neuraminidase - metabolism</subject><subject>Oxazoles - pharmacology</subject><subject>Phosphatase</subject><subject>Phosphoprotein Phosphatases - antagonists & inhibitors</subject><subject>Phosphorylation</subject><subject>Protein Processing, Post-Translational</subject><subject>Trypanosoma cruzi</subject><subject>Trypanosoma cruzi - drug effects</subject><subject>Trypanosoma cruzi - enzymology</subject><subject>Trypanosoma cruzi - ultrastructure</subject><subject>Trypanosome</subject><issn>0166-6851</issn><issn>1872-9428</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1v3CAQhlHVqtmm_QmJOFXJwS1jLzY-RauoH5Ei9dD0jDAeukS2cRi80vbQ3142GzW99QIMPC8DD2NnID6AgPrj9zzURa0kXLTqUghoykK9YCtQedGuS_WSrf4iJ-wN0b0QQjZ1_ZqdgBBKVG25Yr9vpl0YdjjilHhw3Jphb5fBT3xTEE7kk98hn7eB5q1JhvCCLnk-TVvkvXcOYw56k3yYDvG7uJ_NFCiMhtu4_PI85Z1cUfI_Q0LiKXDzXL5lr5wZCN89zafsx-dPd9dfi9tvX26uN7eFza9MRbmuKyWbspGyUTW2wimosIHWGtuvHYCVyokG6q7vO-haKzvXWqgytJZlKapT9v547xzDw4KU9OjJ4jCYCcNCOtuTogLIoDyCNgaiiE7P0Y8m7jUIfRCvH8Xrg1XdKv0oXqucO39qsHQj9v-kjqYzcHUEMH9z5zFqsh4ni72PaJPug_9Piz-ZhJVV</recordid><startdate>19990125</startdate><enddate>19990125</enddate><creator>Grellier, Philippe</creator><creator>Blum, Joseph</creator><creator>Santana, Jaime</creator><creator>Bylèn, Eva</creator><creator>Mouray, Elisabeth</creator><creator>Sinou, Véronique</creator><creator>Teixeira, Antonio R.L.</creator><creator>Schrével, Joseph</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>M7N</scope></search><sort><creationdate>19990125</creationdate><title>Involvement of calyculin A-sensitive phosphatase(s) in the differentiation of Trypanosoma cruzi trypomastigotes to amastigotes</title><author>Grellier, Philippe ; 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Trypanosoma cruzi, the causative agent of Chagas disease, to the dividing amastigote form normally occurs in cytoplasm of infected cells. Here we show that calyculin A, a potent inhibitor of protein phosphatases 1 and 2A, induces at pH 7.5 extracellular transformation of long slender trypomastigotes to round amastigote-like forms which acquire characteristic features observed after the normal differentiation process: repositioning and structural changes of the kinetoplast, release of surface neuraminidase, and expression of amastigote-specific epitopes. Calyculin A inhibits parasite phosphatases and changes in the phosphorylation of specific proteins occur during the transformation process. As an exposure of trypomastigotes to calyculin A concentrations as low as 1 nM and for only 1–2 h is sufficient to induce transformation, the inhibition of calyculin A-sensitive phosphatase(s) appears to play a major role in initiating the trypomastigote differentiation.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>10080392</pmid><doi>10.1016/S0166-6851(98)00172-8</doi><tpages>14</tpages></addata></record> |
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| ispartof | Molecular and biochemical parasitology, 1999-01, Vol.98 (2), p.239-252 |
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| language | eng |
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| subjects | Animals Antigens, Protozoan - metabolism Calyculin A Cell Differentiation Chagas disease Differentiation Membrane Proteins - metabolism Neuraminidase - metabolism Oxazoles - pharmacology Phosphatase Phosphoprotein Phosphatases - antagonists & inhibitors Phosphorylation Protein Processing, Post-Translational Trypanosoma cruzi Trypanosoma cruzi - drug effects Trypanosoma cruzi - enzymology Trypanosoma cruzi - ultrastructure Trypanosome |
| title | Involvement of calyculin A-sensitive phosphatase(s) in the differentiation of Trypanosoma cruzi trypomastigotes to amastigotes |
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