nystatin-a1 and Carcinoma--Hepatocellular

nystatin-a1 has been researched along with Carcinoma--Hepatocellular* in 2 studies

Other Studies

2 other study(ies) available for nystatin-a1 and Carcinoma--Hepatocellular

Article	Year
High cell sensitivity to Helicobacter pylori VacA toxin depends on a GPI-anchored protein and is not blocked by inhibition of the clathrin-mediated pathway of endocytosis. Molecular biology of the cell, 2000, Volume: 11, Issue:11 Helicobacter pylori vacuolating toxin (VacA) causes vacuolation in a variety of cultured cell lines, sensitivity to VacA differing greatly, however, among the different cell types. We found that the high sensitivity of HEp-2 cells to VacA was impaired by treating the cells with phosphatidylinositol-specific phospholipase C (PI-PLC) which removes glycosylphosphatidylinositol (GPI)-anchored proteins from the cell surface. Incubation of cells with a cholesterol-sequestering agent, that impairs both structure and function of sphingolipid-cholesterol-rich membrane microdomains ("lipid rafts"), also impaired VacA-induced cell vacuolation. Overexpression into HEp-2 cells of proteins inhibiting clathrin-dependent endocytosis (i.e., a dominant-negative mutant of Eps15, the five tandem Src-homology-3 domains of intersectin, and the K44A dominant-negative mutant of dynamin II) did not affect vacuolation induced by VacA. Nevertheless, F-actin depolymerization, known to block the different types of endocytic mechanisms, strongly impaired VacA vacuolating activity. Taken together, our data suggest that the high cell sensitivity to VacA depends on the presence of one or several GPI-anchored protein(s), intact membrane lipid rafts, and an uptake mechanism via a clathrin-independent endocytic pathway. Topics: Actin Cytoskeleton; Actins; Animals; Bacterial Proteins; Bacterial Toxins; Carcinoma, Hepatocellular; Cell Line; CHO Cells; Clathrin; Cricetinae; Cytochalasin D; Dogs; Dose-Response Relationship, Drug; Endocytosis; Humans; Iodine Radioisotopes; Nystatin; Phosphatidylinositols; Proteins; Type C Phospholipases; Vacuoles	2000
[The damaging effect of the sodium salt of nystatin on ascitic tumor cells]. Voprosy onkologii, 1975, Volume: 21, Issue:6 The experiments in vitro have demonstrated that an application of 0.1 mg/ml of nistatine into ascitic cells suspension would result in swelling of cells and 80% loss of intracellular potassium, associated with a considerable reduction of Na+K+-ATP-ase activity, the intensity of respiration and glycosis being changed but insignificantly. Thus, the influence of a polyene antibiotic - nistatine on the water-salt balance of ascitic cells under study is likely to be somewhat related with inhibition of NA+K+-dependent ATP-ase. Topics: Adenosine Triphosphatases; Animals; Antibiotics, Antineoplastic; Ascitic Fluid; Carcinoma, Ehrlich Tumor; Carcinoma, Hepatocellular; Female; Glycolysis; In Vitro Techniques; Liver Neoplasms; Mice; Neoplasms, Experimental; Nystatin; Ovarian Neoplasms; Oxygen Consumption; Potassium; Sodium	1975

Article

Year

High cell sensitivity to Helicobacter pylori VacA toxin depends on a GPI-anchored protein and is not blocked by inhibition of the clathrin-mediated pathway of endocytosis.

Molecular biology of the cell, 2000, Volume: 11, Issue:11

Helicobacter pylori vacuolating toxin (VacA) causes vacuolation in a variety of cultured cell lines, sensitivity to VacA differing greatly, however, among the different cell types. We found that the high sensitivity of HEp-2 cells to VacA was impaired by treating the cells with phosphatidylinositol-specific phospholipase C (PI-PLC) which removes glycosylphosphatidylinositol (GPI)-anchored proteins from the cell surface. Incubation of cells with a cholesterol-sequestering agent, that impairs both structure and function of sphingolipid-cholesterol-rich membrane microdomains ("lipid rafts"), also impaired VacA-induced cell vacuolation. Overexpression into HEp-2 cells of proteins inhibiting clathrin-dependent endocytosis (i.e., a dominant-negative mutant of Eps15, the five tandem Src-homology-3 domains of intersectin, and the K44A dominant-negative mutant of dynamin II) did not affect vacuolation induced by VacA. Nevertheless, F-actin depolymerization, known to block the different types of endocytic mechanisms, strongly impaired VacA vacuolating activity. Taken together, our data suggest that the high cell sensitivity to VacA depends on the presence of one or several GPI-anchored protein(s), intact membrane lipid rafts, and an uptake mechanism via a clathrin-independent endocytic pathway.

Topics: Actin Cytoskeleton; Actins; Animals; Bacterial Proteins; Bacterial Toxins; Carcinoma, Hepatocellular; Cell Line; CHO Cells; Clathrin; Cricetinae; Cytochalasin D; Dogs; Dose-Response Relationship, Drug; Endocytosis; Humans; Iodine Radioisotopes; Nystatin; Phosphatidylinositols; Proteins; Type C Phospholipases; Vacuoles

2000

[The damaging effect of the sodium salt of nystatin on ascitic tumor cells].

Voprosy onkologii, 1975, Volume: 21, Issue:6

The experiments in vitro have demonstrated that an application of 0.1 mg/ml of nistatine into ascitic cells suspension would result in swelling of cells and 80% loss of intracellular potassium, associated with a considerable reduction of Na+K+-ATP-ase activity, the intensity of respiration and glycosis being changed but insignificantly. Thus, the influence of a polyene antibiotic - nistatine on the water-salt balance of ascitic cells under study is likely to be somewhat related with inhibition of NA+K+-dependent ATP-ase.

Topics: Adenosine Triphosphatases; Animals; Antibiotics, Antineoplastic; Ascitic Fluid; Carcinoma, Ehrlich Tumor; Carcinoma, Hepatocellular; Female; Glycolysis; In Vitro Techniques; Liver Neoplasms; Mice; Neoplasms, Experimental; Nystatin; Ovarian Neoplasms; Oxygen Consumption; Potassium; Sodium

1975