{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T04:11:18Z","timestamp":1790223078598,"version":"4.1.0"},"reference-count":39,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[2013,7,1]],"date-time":"2013-07-01T00:00:00Z","timestamp":1372636800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2013,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Cardiomyopathy is a serious complication of Chagas' disease, caused by the protozoan parasite\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Trypanosoma cruzi<\/jats:named-content>\n            . The parasite often infects cardiac myocytes, causing the release of inflammatory mediators, including eicosanoids. A recent study from our laboratory demonstrated that calcium-independent phospholipase A\n            <jats:sub>2<\/jats:sub>\n            \u03b3 (iPLA\n            <jats:sub>2<\/jats:sub>\n            \u03b3) accounts for the majority of PLA\n            <jats:sub>2<\/jats:sub>\n            activity in rabbit ventricular myocytes and is responsible for arachidonic acid (AA) and prostaglandin E\n            <jats:sub>2<\/jats:sub>\n            (PGE\n            <jats:sub>2<\/jats:sub>\n            ) release. Thus, we hypothesized that cardiac iPLA\n            <jats:sub>2<\/jats:sub>\n            \u03b3 contributes to eicosanoid production in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">T. cruzi<\/jats:named-content>\n            infection. Inhibition of the isoform iPLA\n            <jats:sub>2<\/jats:sub>\n            \u03b3 or iPLA\n            <jats:sub>2<\/jats:sub>\n            \u03b2, with the\n            <jats:italic>R<\/jats:italic>\n            or\n            <jats:italic>S<\/jats:italic>\n            enantiomer of bromoenol lactone (BEL), respectively, demonstrated that iPLA\n            <jats:sub>2<\/jats:sub>\n            \u03b3 is the predominant isoform in immortalized mouse cardiac myocytes (HL-1 cells). Stimulation of HL-1 cells with thrombin, a serine protease associated with microthrombus formation in Chagas' disease and a known activator of iPLA\n            <jats:sub>2<\/jats:sub>\n            , increased AA and PGE\n            <jats:sub>2<\/jats:sub>\n            release, accompanied by platelet-activating factor (PAF) production. Similarly,\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">T. cruzi<\/jats:named-content>\n            infection resulted in increased AA and PGE\n            <jats:sub>2<\/jats:sub>\n            release over time that was inhibited by pretreatment with (\n            <jats:italic>R<\/jats:italic>\n            )-BEL. Further,\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">T. cruzi<\/jats:named-content>\n            -infected iPLA\n            <jats:sub>2<\/jats:sub>\n            \u03b3-knockout (KO) mice had lower survival rates and increased tissue parasitism compared to wild-type (WT) mice, suggesting that iPLA\n            <jats:sub>2<\/jats:sub>\n            \u03b3-KO mice were more susceptible to infection than WT mice. A significant increase in iPLA\n            <jats:sub>2<\/jats:sub>\n            activity was observed in WT mice following infection, whereas iPLA\n            <jats:sub>2<\/jats:sub>\n            \u03b3-KO mice showed no alteration in cardiac iPLA\n            <jats:sub>2<\/jats:sub>\n            activity and produced less PGE\n            <jats:sub>2<\/jats:sub>\n            . In summary, these studies demonstrate that\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">T. cruzi<\/jats:named-content>\n            infection activates cardiac myocyte iPLA\n            <jats:sub>2<\/jats:sub>\n            \u03b3, resulting in increased AA and PGE\n            <jats:sub>2<\/jats:sub>\n            release, mediators that may be essential for host survival during acute infection. Thus, these studies suggest that iPLA\n            <jats:sub>2<\/jats:sub>\n            \u03b3 plays a cardioprotective role during the acute stage of Chagas' disease.\n          <\/jats:p>","DOI":"10.1128\/iai.00497-12","type":"journal-article","created":{"date-parts":[[2013,2,20]],"date-time":"2013-02-20T07:15:35Z","timestamp":1361344535000},"page":"2278-2287","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":16,"title":["The Absence of Myocardial Calcium-Independent Phospholipase A\n            <sub>2<\/sub>\n            \u03b3 Results in Impaired Prostaglandin E\n            <sub>2<\/sub>\n            Production and Decreased Survival in Mice with Acute Trypanosoma cruzi Infection"],"prefix":"10.1128","volume":"81","author":[{"given":"Janhavi","family":"Sharma","sequence":"first","affiliation":[{"name":"Department of Pathology, Saint Louis University School of Medicine, St. Louis, Missouri, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher S.","family":"Eickhoff","sequence":"additional","affiliation":[{"name":"Division of Infectious Diseases, Department of Internal Medicine, Saint Louis University School of Medicine, St. Louis, Missouri, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel F.","family":"Hoft","sequence":"additional","affiliation":[{"name":"Division of Infectious Diseases, Department of Internal Medicine, Saint Louis University School of Medicine, St. Louis, Missouri, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David A.","family":"Ford","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology and Center for Cardiovascular Research, Saint Louis University School of Medicine, St. Louis, Missouri, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard W.","family":"Gross","sequence":"additional","affiliation":[{"name":"Division of Bioorganic Chemistry and Molecular Pharmacology, Department of Medicine, and Department of Chemistry, Washington University School of Medicine in St. Louis, St. Louis, Missouri, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jane","family":"McHowat","sequence":"additional","affiliation":[{"name":"Department of Pathology, Saint Louis University School of Medicine, St. Louis, Missouri, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_1_2_2","volume-title":"WHO factsheet for Chagas' disease","author":"WHO","year":"2012","unstructured":"WHO. 2012. 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