scholarly journals Nickel uptake and intracellular localization in Cupriavidus pauculus KPS 201, native to ultramafic ecosystem

2010 ◽  
Vol 01 (04) ◽  
pp. 276-280 ◽  
Author(s):  
Arundhati Pal ◽  
A. K. Paul
Keyword(s):  
Intracellular Localization ◽  
Nickel Uptake ◽  
Cupriavidus Pauculus

The Morphology of the Rat Kidney Following Folic Acid Administration

1970 ◽  
Vol 28 ◽  
pp. 200-201
Author(s):  
Aline Byrnes ◽  
Elsa E. Ramos ◽  
Minoru Suzuki ◽  
E.D. Mayfield
Keyword(s):  
Folic Acid ◽  
De Novo ◽  
Specific Activity ◽  
Rat Kidney ◽  
Present Report ◽  
Intracellular Localization ◽  
Male Rats ◽  
Renal Hypertrophy ◽  
Electron Microscopic ◽  
Biochemical Alterations

Renal hypertrophy was induced in 100 g male rats by the injection of 250 mg folic acid (FA) dissolved in 0.3 M NaHCO3/kg body weight (i.v.). Preliminary studies of the biochemical alterations in ribonucleic acid (RNA) metabolism of the renal tissue have been reported recently (1). They are: RNA content and concentration, orotic acid-c14 incorporation into RNA and acid soluble nucleotide pool, intracellular localization of the newly synthesized RNA, and the specific activity of enzymes of the de novo pyrimidine biosynthesis pathway. The present report describes the light and electron microscopic observations in these animals. For light microscopy, kidney slices were fixed in formalin, embedded, sectioned, and stained with H & E and PAS.

The Immuno-Electron Microscopic Localization of the Mo-Fe Protein Component of Nitrogenase in Cells of Azotobacter Vinelandii

1973 ◽  
Vol 31 ◽  
pp. 574-575
Author(s):  
J. T. Stasny ◽  
R. C. Burns ◽  
R. W. F. Hardy
Keyword(s):  
Cellular Localization ◽  
Direct Evidence ◽  
Azotobacter Vinelandii ◽  
Intracellular Localization ◽  
Protein Component ◽  
Electron Microscopic ◽  
Thin Sections ◽  
Fe Protein ◽  
Intracytoplasmic Membranes

Structure-functlon studies of biological N2-fixation have correlated the presence of the enzyme nitrogenase with increased numbers of intracytoplasmic membranes in Azotobacter. However no direct evidence has been provided for the internal cellular localization of any nitrogenase. Recent advances concerned with the crystallizatiorTand the electron microscopic characterization of the Mo-Fe protein component of Azotobacter nitrogenase, prompted the use of this purified protein to obtain antibodies (Ab) to be conjugated to electron dense markers for the intracellular localization of the protein by electron microscopy. The present study describes the use of ferritin conjugated to goat antitMo-Fe protein immunoglobulin (IgG) and the observations following its topical application to thin sections of N2-grown Azotobacter.

An immunocytochemical study of maternal immunoglobulin localization in the suckling pig intestine

1990 ◽  
Vol 48 (3) ◽  
pp. 922-923
Author(s):  
László G. Kömüves ◽  
Donna S. Turner ◽  
Kathy S. McKee ◽  
Buford L. Nichols ◽  
Julian P. Heath
Keyword(s):  
Sodium Ethoxide ◽  
Intracellular Localization ◽  
Protein A ◽  
Tween 20 ◽  
Intestinal Epithelial ◽  
Immunocytochemical Study ◽  
Fish Skin ◽  
Newborn Piglets ◽  
Rabbit Igg ◽  
Fish Skin Gelatin

In this study we used colloidal gold probes to detect the intracellular localization of colostral immunoglobulins in intestinal epithelial cells of newborn piglets.Tissues were obtained from non-suckled newborn and suckled piglets aged between 1 hour to 1 month. Samples were fixed in 2.5 % glutaraldehyde, osmicated and embedded into Spurr’s resin. Thin (80 nm) sections were etched with 5% sodium ethoxide for 5 min, washed and treated with 4 % sodium-m-periodate in distilled water for 30 min. The sections were then first incubated with blocking buffer (2 % BSA, 0.25 % fish skin gelatin, 0.5 % Tween 20 in 10 mM Trizma buffer, pH=7.4 containing 500 mM NaCl) for 30 min followed by the immunoreagents diluted in the same buffer, 1 hr each. For the detection of pig immunoglobulins a rabbit anti-pig IgG antiserum was used followed by goat anti-rabbit IgG-Au10 or protein A-Au15 probes.

Immunoferritin Labelling of Murine Leukemia Virus Antigens in thin Sections

1980 ◽  
Vol 38 ◽  
pp. 508-509
Author(s):  
Ray A. Weigand ◽  
Gregory C. Varjabedian
Keyword(s):  
Murine Leukemia Virus ◽  
Leukemia Virus ◽  
Intracellular Localization ◽  
Uranyl Acetate ◽  
Antibody Technique ◽  
Thin Sections ◽  
Tumor Virus ◽  
Labelling Procedure ◽  
Unlabelled Antibody ◽  
Murine Leukemia

We previously described the intracellular localization of murine mammary tumor virus (MuMTV) p28 protein in thin sections (1). In that study, MuMTV containing cells fixed in 3% paraformaldehyde plus 0.05% glutaraldehyde were labelled after thin sectioning using ferritin-antiferritin in an unlabelled antibody technique. We now describe the labelling of murine leukemia virus (MuLV) particles using the unlabelled antibody technique coupled to ferritin-Fab antiferritin. Cultures of R-MuLV in NIH/3T3 cells were grown to 90% confluence (2), fixed with 2% paraformaldehyde plus 0.5% glutaraldehyde in 0.1 M cacodylate at pH 7.2, postfixed with buffered 17 OsO4, dehydrated with a series of etha-nols, and embedded in Epon. Thin sections were collected on nickel grids, incubated in 107 H2O2, rinsed in HEPES buffered saline, and subjected to the immunoferritin labelling procedure. The procedure included preincubation in 27 egg albumin, a four hour incubation in goat antisera against purified gp69/71 of MuLV (3) (primary antibody), incubation in F(ab’)2 fragments of rabbit antisera to goat IgG (secondary antibody), incubation in apoferritin, incubation in ferritin-Fab ferritin, and a brief fixation with 2% glutaraldehyde. The sections were stained with uranyl acetate and examined in a Siemens IA electron microscope at an accelerating voltage of 60 KV.

NeuN As a Neuronal Nuclear Antigen and Neuron Differentiation Marker

Acta Naturae ◽  
2015 ◽  
Vol 7 (2) ◽  
pp. 42-47 ◽  
Author(s):  
V. V. Gusel’nikova ◽  
D. E. Korzhevskiy
Keyword(s):  
Experimental Data ◽  
Intracellular Localization ◽  
Nuclear Antigen ◽  
Structure And Properties ◽  
Immunocytochemical Detection ◽  
Perinuclear Cytoplasm ◽  
Diagnosis Of Cancer ◽  
Morphological Diagnosis ◽  
The Central Nervous System ◽  
Differentiation Marker

The NeuN protein is localized in nuclei and perinuclear cytoplasm of most of the neurons in the central nervous system of mammals. Monoclonal antibodies to the NeuN protein have been actively used in the immunohistochemical research of neuronal differentiation to assess the functional state of neurons in norm and pathology for more than 20 years. Recently, NeuN antibodies have begun to be applied in the differential morphological diagnosis of cancer. However, the structure of the protein, which can be revealed by antibodies to NeuN, remained unknown until recently, and the functions of the protein are still not fully clear. In the present mini-review, data on NeuN accumulated so far are summarized and analyzed. Data on the structure and properties of the protein, its isoforms, intracellular localization, and hypothesized functions are reported. The application field of immunocytochemical detection of NeuN in scientific and clinical studies, as well as the difficulties in the interpretation of the obtained experimental data and their possible causes, is described in details.

Prediction of Soluble Nickel Removal by Activated Sludge Using Free Metal Ion Concentrations

1987 ◽  
Vol 19 (3-4) ◽  
pp. 439-448 ◽  
Author(s):  
Jeppe S. Nielsen ◽  
Steve E. Hrudey ◽  
Frederick F. Cantwell
Keyword(s):  
Activated Sludge ◽  
Metal Ion ◽  
Municipal Sewage ◽  
Nickel Ion ◽  
Ion Concentrations ◽  
Untreated Sewage ◽  
Nickel Uptake ◽  
Nickel Removal ◽  
Free Metal ◽  
Free Metal Ion

Batch isotherm studies using spiked sewage samples containing a range of total soluble nickel concentrations typical of municipal sewage strongly suggested that it is the free (i.e. uncomplexed) nickel ion that is sorbed by activated sludge. Equations relating nickel uptake by activated sludge to free nickel ion concentrations and the extent of complexation in untreated sewage were developed and applied. Predicted and measured nickel removals generally agreed to within ± 30%.

scholarly journals A Holistic Evolutionary and 3D Pharmacophore Modelling Study Provides Insights into the Metabolism, Function, and Substrate Selectivity of the Human Monocarboxylate Transporter 4 (hMCT4)

2021 ◽  
Vol 22 (6) ◽  
pp. 2918
Author(s):  
Eleni Papakonstantinou ◽  
Dimitrios Vlachakis ◽  
Trias Thireou ◽  
Panayiotis G. Vlachoyiannopoulos ◽  
Elias Eliopoulos
Keyword(s):  
Cancer Cell ◽  
Structural Characteristics ◽  
Cell Metabolism ◽  
Intracellular Localization ◽  
Selective Inhibition ◽  
Monocarboxylate Transporter ◽  
Cancer Drug ◽  
Pharmacophore Modelling ◽  
Anti Cancer ◽  
Cancer Cell Metabolism

Monocarboxylate transporters (MCTs) are of great research interest for their role in cancer cell metabolism and their potential ability to transport pharmacologically relevant compounds across the membrane. Each member of the MCT family could potentially provide novel therapeutic approaches to various diseases. The major differences among MCTs are related to each of their specific metabolic roles, their relative substrate and inhibitor affinities, the regulation of their expression, their intracellular localization, and their tissue distribution. MCT4 is the main mediator for the efflux of L-lactate produced in the cell. Thus, MCT4 maintains the glycolytic phenotype of the cancer cell by supplying the molecular resources for tumor cell proliferation and promotes the acidification of the extracellular microenvironment from the co-transport of protons. A promising therapeutic strategy in anti-cancer drug design is the selective inhibition of MCT4 for the glycolytic suppression of solid tumors. A small number of studies indicate molecules for dual inhibition of MCT1 and MCT4; however, no selective inhibitor with high-affinity for MCT4 has been identified. In this study, we attempt to approach the structural characteristics of MCT4 through an in silico pipeline for molecular modelling and pharmacophore elucidation towards the identification of specific inhibitors as a novel anti-cancer strategy.

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