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)

The morphologic display of testicular cancer is a heterogenous cellular pattern. A biological heterogeneity is also true for the expression of tumor markers. The biosynthesis of tumor marker proteins alpha-fetoprotein (AFP), ferritin, Schwangerschaftsprotein (SP 1) glycoprotein, tissue polypeptide antigen and of hormones (beta-human chorionic gonadotropin (HCG) = significantly present in nonseminoma germ cell tumors--does, however, define only a small number of cancer cells. To better visualize the majority of cancer cells, lectin binding was studied. During the oncogenic transformation a distinct change of cell membrane glycoproteins has been observed. Reactions of WGA/PNA lectins which get attached to glycoproteins with cancer tissue sample from seminomas (n = 20) and nonseminomas (n = 20) were analyzed. The results were correlated to AFP/beta-HCG positive (negative) immunohistology to establish further subgroups of biological homogeneity. The binding of WGA lectin appears relatively more frequent in both seminoma and nonseminoma than that of PNA. Lectin binding of WGA and/or PNA can be stained in 3/11 AFP- and beta-HCG-negative nonseminoma tissues while lectin staining is positive in 7/18 beta-HCG-negative seminomas. The fact that lectin binding is dependent on the spermatozoogenesis and on androgens in normal testis tissues asks for more detailed studies in this field.
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PMID:[Lectin binding in immunohistologically AFP/HCG positive and negative testicular carcinoma]. 243 37

The glycoconjugate composition of mouse intercalated duct and acinar cells of parotid gland has been compared. Mucins containing 1,2-glycols were demonstrated by the tannic acid-uranyl acetate technique. Hexose residues of glycoconjugates were identified using ferritin conjugated with Canavalia ensiformis agglutinin (Con A), Triticum vulgare or wheat germ agglutinin (WGA), Ricinus communis I agglutinin (RCA-I), Phaseolus vulgaris agglutinin (PHA-E) and Arachis hypogaea agglutinin (PNA). Whereas qualitative and quantitative differences were observed in sugar residues of secretory granules in intercalated duct and acinar cells, apical plasmalemmae were labelled sparsely and similarly. This indicates that the glycocalyx composition of apical plasmalemmae in the parotid acinar and intercalated duct cells is little influenced by secretory granule composition.
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PMID:Cytochemical localization of carbohydrates in intercalated duct and acinar cells of mouse parotid gland. 247 Jul

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

Bloodstream trypomastigote and culture procyclic (insect midgut) forms of a cloned T. rhodesiense variant (WRAT at 1) were tested for agglutination with the lectins concanavalin A (Con A), phytohemagglutinin P (PP), soybean agglutinin (SBA), fucose binding protein (FBP), wheat germ agglutinin (WGA), and castor bean lectin (RCA). Fluorescence-microscopic localization of lectin binding to both formalin-fixed trypomastigotes and red cells was determined with fluorescein isothiocyanate (FITC)-conjugated Con A, SBA, FBP, WGA, RCA, PNA (peanut agglutinin), DBA (Dolichos bifloris), and UEA (Ulex europaeus) lectins. Electron microscopic localization of lectin binding sites on bloodstream trypomastigotes was accomplished by the Con A-horseradish peroxidase-diamino-benzidine (HRP-DAB) technique, and by a Con A-biotin/avidin-ferritin method. Trypomastigotes, isolated by centrifugation or filtration through DEAE-cellulose or thawed after cryopreservation, were agglutinated by the lectins Con A and PP with agglutination strength scored as Con A greater than PP. No agglutination was observed in control preparations or with the lectins WGA, FBA or SBA. Red cells were agglutinated by all the lectins tested. Formalin-fixed bloodstream trypomastigotes bound FITC-Con A and FITC-RCA but not FITC-WAG, -SBA, -PNA, -UEA or -DBA lectins. All FITC-labeled lectins bound to red cells. Con A receptors, visualized by Con A-HRP-DAB and Con A-biotin/avidin-ferritin techniques, were distributed uniformly on T. rhodesiense bloodstream forms. No lectin receptors were visualized on control preparations. Culture procyclics lacked a cell surface coat and were agglutinated by Con A and WGA but not RCA, SBA, PP and FBP. Procyclics were not agglutinated by lectins in the presence of competing sugar at 0.25 M.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Trypanosoma rhodesiense bloodstream trypomastigote and culture procyclic cell surface carbohydrates. 668 36

The arrangement of carbohydrate molecules on surfaces of fungal cells may play an important role in nonself recognition of these microorganisms by potential invertebrate hosts. Changes in the ability of various galactose and mannose-specific lectins to bind to surface components on cell walls of the insect pathogen Paecilomyces farinosus were therefore examined during growth and differentiation of the fungus. Fluorescein isothiocyanate conjugates of concanavalin A (Con A, specific for alpha-D-mannose) and peanut agglutinin (PNA, beta-D-galactose) bound inconsistently to blastospores and weakly to mycelia except at apical regions where strong fluorescence was observed. Labeling patterns were similar on cells tested with a galactose-specific lectin purified from Spodoptera exigua (beet armyworm) hemolymph, but Bandeiraea simplicifolia lectin (BS-I alpha-D-galactose) bound only to mycelia. Electron microscopy using ferritin and gold probes showed that the galactomannans are located in a loosely bound coating on the cell wall surface. Variations in lectin binding patterns are apparently due to absence (e.g., by shedding) of the coat or to rearrangement of carbohydrate components in the coat. Staining of Western blots of dithiothreitol (DTT) cell wall extracts further indicated that the BS-I-binding entity is a unique component of the mycelial surface since, as in the fluorescence studies, blastospore preparations were not labeled. Staining of blastospore blots with other galactose-specific probes (e.g., PNA) was comparable to staining of mycelial blots.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Variations in the ability of galactose and mannose-specific lectins to bind to cell wall surfaces during growth of the insect pathogenic fungus Paecilomyces farinosus. 833 Jun 30

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

It was suggested in a previous study that cells of Acinetobacter venetianus VE-C3 adhere to diesel fuel by synthesizing a capsular polysaccharide containing glucose and/or mannose. To study the fine structure of cells and localization of bacterial polysaccharide in the presence of diesel fuel, two lectins were used: ConA, an agglutinin from Canavalia ensiformis specific for mannose and/or glucose residues, and PNA, an agglutinin from Arachis hypogaea, for terminal galactose residues. The lectins were conjugated with electron dense ferritin for transmission electron microscopy (TEM) and with fluorescein isothiocyanate (FITC) for scanning confocal laser microscopy (SCLM). Samples were prepared by freeze substitution, which allows glycosylation to be determined in situ in thin sections of specimens. The distribution of glycosylation was imaged with and without treatment of specimens with their specific hapten (glucose and galactose). The glycosylation activity produced a polysaccharide capsule. Emulsified diesel fuel nanodroplets were observed at the cell envelope perimeter. Fine structure of vesicles consisted of polysaccharide and diesel fuel nanodroplets. Lectin blotting analysis showed ConA-positive glycoprotein with an apparent molecular mass of 22 kDa in the outer membrane. Its production was induced by diesel fuel. This glycoprotein was probably responsible for bioemulsifying activity at the cell envelope. Several other glycoproteins were positive for PNA lectin, the main constituent migrating with an apparent molecular weight of 17.8 kDa. However, they were all constitutive and probably involved in cell biofilm formation at the oil surface.
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PMID:Envelope glycosylation determined by lectins in microscopy sections of Acinetobacter venetianus induced by diesel fuel. 1289 48

Circulating tumor DNA (ctDNA), which includes DNA mutations, epigenetic alterations and other forms of tumor-specific abnormalities, is a promising "real-time" biomarker for noninvasive cancer assessment. Tumor DNA is of great value in the process of cancer treatment, including diagnostic and prognostic information before, during treatment and at progression. Here we introduce a peptide nucleic acids probe-gold nanoparticles (PNA-AuNPs) and lead phosphate apoferritin (LPA)-based dual biomarker detection platform, which could be used in a DNA biosensor to quantify ctDNA by detection of tumor-specific mutations and methylation of PIK3CA gene. On the one hand, PNA probe and anti-5-Methylcytosine monoclonal antibody (anti-5-mC) were used to recognize the different parts of ctDNA, forming a sandwich-structure on a screen-printed electrode (SPE) surface. On the other hand, AuNPs and LPA were introduced to construct the biosensor for double signal amplification. Square-wave voltammetry (SWV) was used to monitor the electrochemical signal of lead ions released from apoferritin. The proposed DNA biosensor yielded a linear current response to ctDNA concentrations over a broad range of 50-10000 fM with a detection limit of 10 fM. It also successfully detected ctDNA collected from cancer patient serum. Therefore, we anticipate this new platform opens up an approach to detect and monitor diverse malignancies, facilitating personalized cancer therapy.
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PMID:A dual biomarker detection platform for quantitating circulating tumor DNA (ctDNA). 2929 Nov 60