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giardiasis/phosphatase
Linkki tallennetaan leikepöydälle
Sivu 1 alkaen 51 tuloksia
The acid phosphatase positive organelles of the Giardia lamblia trophozoite contain a membrane bound cathepsin C activity.
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We found a dipeptidyl aminopeptidase activity in the parasitic protozoan Giardia lamblia with properties similar to the lysosomal cathepsin C of rat-liver lysosomes. Subcellular fractionation of this parasite indicated that the cathepsin C activity is located in organelles not distinguishable from
Excystation of Giardia muris induced by a phosphate-bicarbonate medium: localization of acid phosphatase.
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Giardia muris cysts were incubated briefly in an aqueous induction medium of 0.1 M potassium phosphate with 0.1, 0.2, or 0.3 M sodium bicarbonate. High rates of excystation (91.1-96.7%) were recorded within 5 min after the cysts were placed in trypticase-yeast extract-iron-serum (TYI-S) medium.
Localization of acid phosphatase activity in Giardia lamblia and Giardia muris trophozoites.
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Numerous membrane-bounded vacuoles are found adjacent to the plasma membrane of the pathogenic protozoan Giardia lamblia. The function of these vacuoles has been discussed by several authors. Approximately 100-400 nm in diameter with a core of low electron density, they have been suggested to be
Intestinal disaccharidase and alkaline phosphatase activity in giardiasis.
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We report results on determinations of small intestinal brush-border enzyme activities in 22 children (aged 11 months to 14 years) with giardiasis. In particular, activities of disaccharidases (lactase, sucrase, maltase) and of alkaline phosphatase were investigated. Forty-one percent of the
Giardia lamblia: expression of alkaline phosphatase activity in infected rat intestine.
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Alkaline phosphatase (IAP) is a marker of intestinal microvillus membrane. Changes in IAP activity have been studied as a function of Giardia lamblia (G. lamblia) infection using rat as the experimental model. At day 11 and 15 post-infection, enzyme activity was reduced (p<0.01) compared to
Giardia lamblia: Characterization of ecto-phosphatase activities.
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Ecto-phosphatase activities of Giardia lamblia were characterized in intact cells, which are able to hydrolyze the artificial substrate p-nitrophenylphosphate (p-NPP) to p-nitrophenol (p-NP) at a rate of 8.4+/-0.8 nmol p-NP/h/10(7) cells. The ecto-phosphatase activities were inhibited at high pH as
Calcium-binding proteins that are type B″ regulatory subunits of phosphatase 2A in Giardia intestinalis.
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Giardia intestinalis is a protozoan parasite that colonizes the upper part of the small intestine of its mammalian hosts. The trophozoite, which is the replicative stage, has a complex cytoskeleton that allows it to move and adhere to intestinal cells. It has been proposed that protein phosphatase
Protein phosphatase 2A plays a crucial role in Giardia lamblia differentiation.
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The ability of Giardia lamblia to undergo two distinct differentiations in response to physiologic stimuli is central to its pathogenesis. The giardial cytoskeleton changes drastically during encystation and excystation. However, the signal transduction pathways mediating these transformations are
[Enterokinase and alkaline phosphatase activity in children with hymenolepiasis and lambliasis].
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Dephosphorylation of cyst wall proteins by a secreted lysosomal acid phosphatase is essential for excystation of Giardia lamblia.
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Transport studies and enzyme assays in mice infected with human Giardia lamblia.
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It is well established that Giardia infection causes malabsorption. However, the precise mechanism of such a malabsorption is not known. To investigate this, transport studies, using the tissue accumulation technique, were carried out in mice infected with G. lamblia obtained from human stools.
Transcriptome analyses of the Giardia lamblia life cycle.
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We quantified mRNA abundance from 10 stages in the Giardia lamblia life cycle in vitro using Serial Analysis of Gene Expression (SAGE). 163 abundant transcripts were expressed constitutively. 71 transcripts were upregulated specifically during excystation and 42 during encystation. Nonetheless, the
Giardia lamblia infection in immunosuppressed animals causes severe alterations to brush border membrane enzymes.
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NMRI mice immunosuppressed with dexamethasone followed by challenge intraesophageally with axenic Giardia lamblia (Portland I) trophozoites had severe infection in terms of the trophozoite counts in the jejunum. Although the immunosuppressive treatment with cortisone itself resulted in a deleterious
Detection of Giardia duodenalis antigen in human fecal eluates by enzyme-linked immunosorbent assay using polyclonal antibodies.
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The present study developed and standardized an enzime-linked immunosorbent assay (ELISA) to detect Giardia antigen in feces using rabbit polyclonal antibodies. Giardia cysts were purified from human fecal samples by sucrose and percoll gradients. Gerbils (Meriones unguiculatus) were infected to
Sorting of cyst wall proteins to a regulated secretory pathway during differentiation of the primitive eukaryote, Giardia lamblia.
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Giardia lamblia, which belongs to the earliest identified lineage to diverge from the eukaryotic line of descent, is one of many protists reported to lack a Golgi apparatus. Our recent finding of a developmentally regulated secretory pathway in G. lamblia makes it an ideal organism with which to
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