Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In the syncytiotrophoblastic surface of the toxemic full-term placentae, the sialates and their consequent negative charging were studied by both electron microscopic histochemistry (Ferritin method) and Western blot analysis. Evidence is presented showing (1) that the reactions with both the ferritin labelled Limulus Polyphemus Agglutinin (LPA-ferritin), specific to sialates, and the cationized ferritin, specific to a negative charge, decrease in the specimens of toxemic placentae, (2) that the density of sialates in placentae of severe gestational proteinuria or/and hypertension is statistically lower than that of severe gestational edema, and (3) that there is no difference between the blotted bands in normal placentae and toxemic ones regardless of the severity of the toxemia. These results indicate that the reduction of the surface negative charging is demonstrated in toxemic syncytiotrophoblasts and appears to be secondary to the decrease in the amount of sialate.
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PMID:Sialates and negative charge on the surface of syncytiotrophoblastic cells of full-term placentae in toxemic patients. 233 76

The localization of complex carbohydrates in the Golgi apparatus, secretory granules and plasmalemma of mouse parotid acinar cells was studied using the fracture-labelling method. The hexose residues of glycoconjugates were identified using ferritin conjugated with Wheat Germ Agglutinin (WGA-), Ricinnus Communis Agglutinin II (RCA-II-), Phaseolus Vulgaris Agglutinin (PHA-) and Limulus Polyphemus Agglutinin (LPA-). We found that the fracture-labelling method allows not only the labelling of membrane faces but also analysis of the compartment's content that is exposed during the fracturing of the tissue. Our results revealed differences in the hexose residues located in the Golgi apparatus, secretory granules and the apical and lateral plasmalemma. Numerous binding sites for WGA-, PHA- and RCA-II-ferritin were demonstrable in the Golgi apparatus. In secretory granules, the WGA- and RCA-II-ferritin binding sites were most numerous, while LPA-ferritin binding sites were very rare. The density of the binding sites for PHA-ferritin showed considerable variation in secretory granules. The apical plasmalemma exhibited a high density of binding sites for all of the lectins used. In the lateral plasmalemma, LPA-ferritin was not bound, and there were fewer binding sites for WGA-, RCA-II- and PHA-ferritin.
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PMID:Lectin-binding pattern in parotid acinar cells. The fracture-labelling method and post-embedding staining. 243 Sep 21

The surface charge of epimastigote and trypomastigote forms of Trypanosoma cruzi was analysed by three approaches: a) visualization by electron microscopy of the binding of cationic particles (cationized ferritin at pH 7.2 and colloidal iron hydroxyde at pH 1.8) to the parasite's surface, b) visualization of the binding of fluorescein-labeled lectins (PNA and LPA) to the parasite's surface, and c) by cell electrophoresis. In all cases control, trypsin and neuraminidase-treated cells were analysed. The results obtained indicate that sialic acid residues located on the parasite's surface are responsible for the binding of cationic particles to it and the major component responsible for the net negative surface charge presented by T. cruzi. Phosphate groups, associated to phospholipids, also contribute to the negative surface charge. The effect of previous incubation of the parasites in the presence of lectins (ConA, WGA, PNA, RCA and LPA) on their surface charge was also analysed by cell electrophoresis.
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PMID:The surface charge of Trypanosoma cruzi: analysis using cell electrophoresis, lectins and ultrastructural cytochemistry. 309 34

The endocytic pathway of Tritrichomonas foetus, a parasitic protozoan of cattle, was studied using (a) vital dyes, such as Lucifer yellow, neutral red and acridine orange, (b) cationized ferritin, (c) gold-labeled lactoferrin and lectins: HPA, UEA, PNA and LPA, and (d) DAMP (3-(2,4-dinitroanilino) 3' amino-N-methyldipropylamine). Light and confocal laser microscopy as well as transmission electron microscopy were used in this study. Assays were monitored by fluorescence and electron microscopy after exposing the parasites to different conditions. Cells that were incubated at 15 degrees C or 20 degrees C with gold-labeled lactoferrin and processed for electron microscopy show that of 15 degrees C this ligand is found only in an early endosomal compartment and at 20 degrees C it is found in late endosomes but not in lysosomes. Immunocytochemical data from cryosections using DAMP as a pH probe show that T. foetus has acidic compartments, with a pH range of 5.2 to 6.6, with variable morphology, localization and size. Lectin-binding sites and anionic sites were also internalized and appear to be associated with membranes lining the vacuoles. Images of patching and shedding of these sites were also observed when HPA and UEA were used.
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PMID:Partial characterization of cytoplasmic compartments involved in the endocytic process of Tritrichomonas foetus. 908 87

A new sandwich-like electrochemical immunosensor has been developed for quantification of organophosphorylated acetylcholinesterase (OP-AChE), an exposure biomarker of organophosphate pesticides and nerve agents. Zirconia nanoparticles (ZrO2 NPs) were anchored on a screen printed electrode (SPE) to preferably capture OP-AChE adducts by metal chelation with phospho-moieties, which was selectively recognized by lead phosphate-apoferritin labeled anti-AChE antibody (LPA-anti-AChE). The sandwich-like immunoreactions were performed among ZrO2 NPs, OP-AChE and LPA-anti-AChE to form ZrO2/OP-AChE/LPA-anti-AChE complex and the released lead ions were detected on a disposable SPE. The binding affinity was investigated by both square wave voltammetry (SWV) and quartz crystal microbalance (QCM) measurements. The proposed immunosensor yielded a linear response current over a broad OP-AChE concentrations range from 0.05 nM to 10 nM, with detection limit of 0.02 nM, which has enough sensitivity for monitoring of low-dose exposure to OPs. This method avoids the drawback of unavailability of commercial OP-specific antibody as well as amplifies detection signal by using apoferritin encoded metallic phosphate nanoparticle tags. This nanoparticle-based immunosensor offers a new method for rapid, sensitive, selective and inexpensive quantification of phosphorylated adducts for monitoring of OP pesticides and nerve agents exposures.
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PMID:Nanoparticle-based immunosensor with apoferritin templated metallic phosphate label for quantification of phosphorylated acetylcholinesterase. 2148 80