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1.
Parasite Immunol ; 33(12): 661-8, 2011 Dec.
Article in English | MEDLINE | ID: mdl-21919917

ABSTRACT

To define the role of CD38 in the migration of neutrophils to the liver and consequently in the induction of an innate immune response during murine hepatic amoebiasis by Entamoeba histolytica, we examined amoebic liver abscess development (ALA), presence of amoebae and neutrophils, and expression levels of cytokines and other inflammation mediators mRNA, in infected wild-type and CD38 Knockout (CD38KO) C57BL/6J mice. Results showed that CD38KO mice undergo a delay in ALA development in comparison with the wild-type strain. The presence of amoebae lasted longer in CD38(-/-), and although neutrophils arrived to the liver in both strains, there was a clear difference in the time between the two strains; whereas in the wild-type strain, neutrophils arrived at early times (6-12 h), in the CD38KO strain, neutrophils arrived later (48-72 h). Cytokines profile during the innate immune response development (TNF-α, IL-1ß, IL-6) was, for WT mice concomitant with, and preceded, for CD38KO mice, the time in which neutrophils were present in the liver lesion. In conclusion, CD38 is important for neutrophils migration during hepatic amoebiasis, and in turn, these cells play an important role in the innate immune response.


Subject(s)
ADP-ribosyl Cyclase 1/deficiency , Entamoeba histolytica/immunology , Immunity, Innate , Liver Abscess, Amebic/immunology , Liver/immunology , Membrane Glycoproteins/deficiency , Neutrophils/immunology , ADP-ribosyl Cyclase 1/immunology , Animals , Cytokines/biosynthesis , Disease Models, Animal , Gene Expression Profiling , Inflammation Mediators/immunology , Male , Membrane Glycoproteins/immunology , Mice , Mice, Inbred C57BL , Mice, Knockout , Time Factors
2.
Acta Histochem ; 103(2): 209-24, 2001 Apr.
Article in English | MEDLINE | ID: mdl-11368101

ABSTRACT

Dp71 is a member of the dystrophin family and the most abundant dmd gene product in the brain. In the present study, we focused on a short dystrophin transcript named Dp71f, which is alternatively spliced when exon 78 is absent The topographic localization of this protein in the encephalon has not been properly described yet, nor its cellular or subcellular localization, and even less its functions. Dp71f was found to be a cytoplasmic 70 kDa protein and localized in all encephalon regions studied. Double labeling using specific markers for various cell types confirmed Dp71f distribution in the cytoplasm of all cell types studied. Labeling was more conspicuous near the nucleus and diminished towards the periphery of cells. In some cases, we observed cells that were positive for actin and Dp71f in regions corresponding to lamellipodia-like structures. Dp71f and Dp71d isoforms were differently distributed. Our study is the first specific and unambiguous description of the topography and cellular localization patterns of Dp71f in brain, suggesting that Dp71f is a ubiquitous protein.


Subject(s)
Brain Chemistry , Brain/metabolism , Dystrophin/analysis , Animals , Blotting, Western , Cells, Cultured , Dystrophin/analogs & derivatives , Microscopy, Immunoelectron , Protein Isoforms/analysis , Rats , Subcellular Fractions/metabolism , Tissue Extracts/chemistry
3.
Biochem Biophys Res Commun ; 271(1): 54-8, 2000 Apr 29.
Article in English | MEDLINE | ID: mdl-10777680

ABSTRACT

Bacillus thuringiensis (Bt), considered a safe insecticide, produces insecticidal proteins named Cry during sporulation, which possess exceptional immunological properties. In this work using an immunohistochemical test we demonstrated that Cry1Ac protoxin (pCry1Ac) binds to the mucosal surface of the mouse small intestine. Ligand blot assay allowed us to detect, under denaturing conditions, six pCry1Ac-binding polypeptides present in brush border membrane vesicles isolated from the small intestine. Moreover, this protein induced in situ temporal changes in the electrophysiological properties of the mouse jejunum. The data obtained indicate a possible interaction in vivo of Cry proteins with the animal bowel which could induce changes in the physiological status of the intestine.


Subject(s)
Bacillus thuringiensis/chemistry , Bacterial Proteins/metabolism , Bacterial Toxins , Endotoxins/metabolism , Intestine, Small/metabolism , Intestine, Small/microbiology , Membrane Proteins/metabolism , Animals , Bacillus thuringiensis Toxins , Electrophysiology , Escherichia coli/metabolism , Fluorescent Antibody Technique , Hemolysin Proteins , Jejunum/metabolism , Ligands , Male , Mice , Mice, Inbred BALB C , Microvilli/metabolism , Plants, Genetically Modified/metabolism , Protein Binding , Recombinant Proteins/metabolism , Time Factors
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