Modified lipids from Trypanosoma cruzi amastigotes down-regulate the pro-inflammatory response and increase the expression of alternative activation markers in macrophages.

Herein, we analyzed the in vitro effect induced by total lipid extracts from Trypanosoma cruzi amastigotes of RA and K98 strains, which were obtained after overnight incubation (RAinc and K98inc) to mimic phospholipid hydrolytic processes that occurred adjacent to degenerating amastigote nests in tissues of Chagas disease patients. We demonstrated that RAinc and K98inc might possess bioactive lipid molecules with anti-inflammatory bias since they inactivated the NF-κB pathway, in contrast to intact lipids. Moreover, different M1/M2 macrophage phenotype markers of polarization were analyzed by RT-qPCR which evidenced that RAinc and K98inc promoted an increased expression of the M2 markers Arginase-1, IL-10, FIZZ and YM-1, and a decreased expression of iNOS and proinflammatory cytokines IL-6 and TNF-α.

Involvement of lipids from Leishmania braziliensis promastigotes and amastigotes in macrophage activation.

Leishmania are obligate protozoan parasites responsible for substantial public health problems in tropical and subtropical regions around the world, with L. braziliensis being one of the causative agents of American Tegumentary Leishmaniasis. Macrophages, fundamental cells in the innate inflammatory response against Leishmania, constitute a heterogeneous group with multiple activation phenotypes and functions.

Cellular localization, cloning and expression of Leishmania braziliensis Phospholipase A.

Leishmaniasis is caused by several species of protozoan parasites of the genus Leishmania and represents an important global health problem. Leishmania braziliensis in particular is responsible of cutaneous and mucocutaneous forms of this parasitosis, with prevalence in Latin America. In the present work, we describe in L.

Phospholipase A1: a novel virulence factor in Trypanosoma cruzi.

Phospholipase A1 (PLA1) has been described in the infective stages of Trypanosoma cruzi as a membrane-bound/secreted enzyme that significantly modified host cell lipid profile with generation of second lipid messengers and concomitant activation of protein kinase C. In the present work we determined higher levels of PLA1 expression in the infective amastigotes and trypomastigotes than in the non-infective epimastigotes of lethal RA strain. In addition, we found similar expression patterns but distinct PLA1 activity levels in bloodstream trypomastigotes from Cvd and RA (lethal) and K98 (non-lethal) T.

Phospholipases a in trypanosomatids.

Phospholipases are a complex and important group of enzymes widespread in nature, that play crucial roles in diverse biochemical processes and are classified as A(1), A(2), C, and D. Phospholipases A(1) and A(2) activities have been linked to pathogenesis in various microorganisms, and particularly in pathogenic protozoa they have been implicated in cell invasion. Kinetoplastids are a group of flagellated protozoa, including extra- and intracellular parasites that cause severe disease in humans and animals.

Involvement of protein kinase C isoenzymes in Trypanosoma cruzi metacyclogenesis induced by oleic acid.

Previously, we showed that oleic acid (OA) induces Trypanosoma cruzi metacyclogenesis through a signaling pathway involving de novo diacylglycerol biosynthesis and simultaneous protein kinase C (PKC) activation. Herein, we demonstrated that OA also triggers a transient Ca(2+) signal in epimastigotes, necessary for parasite differentiation, that could account for PKC activation. In addition, we found that this free fatty acid (FFA) directly stimulated in vitro the activity of T.