cytochalasin-b and Glioma

cytochalasin-b has been researched along with Glioma* in 24 studies

Other Studies

24 other study(ies) available for cytochalasin-b and Glioma

ArticleYear
Cytochalasin B inhibits the proliferation of human glioma U251 cells through cell cycle arrest and apoptosis.
    Genetics and molecular research : GMR, 2014, Dec-19, Volume: 13, Issue:4

    Cytochalasin B (CB) is known to inhibit a number of cancer types, but its effects on gliomas are unknown. We examined the in vitro effects of CB on the proliferation of human glioma U251 cells, as well as determined its mechanism of action. Cell proliferation was determined using CCK-8. The effect of CB on U251 cell morphology was observed under a transmission electron microscope. Cell cycle distribution was assessed using propidium iodine and Giemsa staining, and cell apoptosis was determined by annexin V-fluorescein isothiocyanate/propidium iodide. Cell cycle-related proteins were determined by Western blot. CB effectively inhibited U251 cell proliferation in a dose- and time-dependent manner. The 24, 48, 72, and 96 h IC50 values were 6.41 x 10(-2), 9.76 x 10(-4), 2.57 x 10(-5), and 2.08 x 10(-5) M, respectively. CB increased the proportion of cells in the G2/M phase in a dose-dependent manner, thus increasing the mitotic index and decreasing cdc2 and cyclin B1 protein levels. CB induced morphological changes in the cytoskeleton. Additionally, 10(-5) M CB induced apoptosis in 23.4 ± 0.5% of U251 cells (P < 0.05 vs control group). Caspase-3, -8, and -9 activities were increased after CB treatment. CB inhibited U251 glioma cell proliferation by damaging the microfilament structure. CB also induced glioma cell apoptosis, suggesting that it may be an effective therapeutic agent against gliomas.

    Topics: Antineoplastic Agents; Apoptosis; Brain Neoplasms; Cell Cycle Checkpoints; Cell Cycle Proteins; Cell Line, Tumor; Cell Proliferation; Cytochalasin B; Gene Expression Regulation, Neoplastic; Glioma; Humans

2014
A fast and robust quantitative time-lapse assay for cell migration.
    Experimental cell research, 2005, Dec-10, Volume: 311, Issue:2

    We describe a simple and widely applicable method to measure cell migration in time-lapse sequences of fluorescently labeled cells in culture. Briefly, binarized cell images obtained after thresholding were cumulatively projected, and the covered areas were measured. This procedure determines the time course of the track area successively covered by the cell population. Under conditions where cell growth is negligible, a robust index of cell motility is derived from normalized plots for the displacement of cells over time. We applied this method to quantitatively examine the migration of B35 neuroblastoma cells transiently expressing GFP and to C6 glioma cells after staining with Hoechst 33258. This sensitive assay detected the influence of agents which inhibit actin polymerization (cytochalasin B) or interfere with the maintenance of cell polarity (methyl-beta-cyclodextrin) on cell migration. Thus, this assay is a versatile tool to measure quickly the migration of different cell types using different labeling strategies.

    Topics: Animals; beta-Cyclodextrins; Cell Line, Tumor; Cell Movement; Cytochalasin B; Glioma; Green Fluorescent Proteins; Microscopy, Fluorescence; Neuroblastoma; Neuroglia; Neurons; Rats

2005
Cytoplasmic retention of mutant tsp53 is dependent on an intermediate filament protein (vimentin) scaffold.
    Oncogene, 1998, Jul-02, Volume: 16, Issue:26

    The temperature-sensitive mutant tsp53val135 accumulates in the cytoplasm of cells kept at the non-permissive temperature (39 degrees C), but is rapidly transported into the cell nucleus at the permissive temperature (30 degrees C). tsp53 thus may serve as a model for analysing cellular parameters influencing the subcellular location of p53. Here we provide evidence that retention of tsp53 in the cytoplasm at the non-permissive temperature is due to cytoskeletal anchorage of the p53 protein. Two sublines of C6 rat glioma cells differing in their expression of the intermediate filament protein vimentin (vimentin expressing or vimentin negative cells) were stably transfected with a vector encoding tsp53. Whereas cells of vimentin expressing C6 subclones retained tsp53 in the cytoplasm at the non-permissive temperature, cells of vimentin negative subclones exclusively harbored the tsp53 within their nuclei. Intermediate filament deficient cells that had been reconstituted with a full length vimentin protein again showed a cytoplasmic localization of tsp53, whereas in cells expressing a C-terminally truncated (tail-less) vimentin tsp53 localized to the nucleus. We conclude that cytoplasmic sequestration of tsp53 requires an intact intermediate filament system.

    Topics: Actins; Animals; Biological Transport; Cell Compartmentation; Cell Nucleus; Cytochalasin B; Cytoplasm; Cytoskeleton; Fluorescent Antibody Technique; Glioma; Mice; Mutation; Rats; Tubulin; Tumor Cells, Cultured; Tumor Suppressor Protein p53; Vimentin; Vinblastine

1998
Cell density regulates crypticity of GM3 ganglioside on human glioma cells.
    Experimental cell research, 1997, May-25, Volume: 233, Issue:1

    Human glioma cell line KG-1C contains GM3 ganglioside as its sole glycolipid. The degree of M2590 antibody binding to GM3 was found to be regulated by the cell density; the percentage of positive cells in FACS analysis decreased from approximately 20% to close to none as the cells increased their density from sparse to confluent. The contents of GM3 with different cell densities were consistent, being more than 0.4 micromol/g of the cellular weight, which was high enough to be recognized by the antibody. Trypsin treatment of the cells did not increase antibody reactivity. The extracted GM3 retained its antigenicity, being intensely stained with M2590 on a TLC plate; there was no change in chromatographic mobility either, indicating no modification of its chemical structure. The fluorescent microscope disclosed scattered dot-like staining of GM3, particularly at the periphery of the cells. We were able to expose cryptic GM3 fully within 12 h by dispersion of the cells to a sparse density. Surface labeling of GM3 with the use of limited sodium periodate oxidation of sialylated residue equally labeled GM3 either from the confluent cells or the sparse cells. Disassembly of actin filaments with cytochalasin B (10 microM) partially exposed cryptic GM3 of confluent cells, indicating reversibility of the crypticity. All together, the results indicate that cryptic GM3 actually exists on the cell surface, hidden from the surface not by other molecules but by other mechanisms associated with the cellular architecture. We are beginning to explore the possibility of selective localization of GM3 in small caves or folds of the cell membrane produced upon cell-to-cell contact.

    Topics: Antigens, Neoplasm; Biomarkers, Tumor; Cell Count; Cell Membrane; Cytochalasin B; Flow Cytometry; Fluorescent Antibody Technique; G(M3) Ganglioside; Glioma; Glycolipids; Humans; Neuraminidase; Tumor Cells, Cultured

1997
Neurofibromatosis 2 tumor suppressor protein colocalizes with ezrin and CD44 and associates with actin-containing cytoskeleton.
    Journal of cell science, 1997, Volume: 110 ( Pt 18)

    Neurofibromatosis 2 (NF2) protein (merlin; schwannomin) is a tumor suppressor involved in tumorigenesis of NF2-associated and sporadic schwannomas and meningiomas. The protein shares the domain structure of three homologous proteins: ezrin, radixin and moesin (ERM). ERM proteins function as membrane organizers and may act as linkers between plasma membrane molecules, such as CD44 and ICAM-2, and the cytoskeleton. We analyzed the distribution and effects of transfected NF2 protein in COS-1, CHO and 293 cells, and endogenous NF2 protein in U251 glioma cells. The distribution was compared to ezrin, CD44 and F-actin. Both transfected and endogenous NF2 protein localized underneath the plasma membrane in a pattern typical of an ERM protein. In COS-1 transfectants, NF2 protein typically codistributed with ezrin but, in cells with poorly developed actin cytoskeleton, it replaced ezrin in filopodia and ruffling edges. NF2 protein colocalized with CD44, which in transfected cells accumulated into restructured cell membrane protrusions. The association of CD44 and NF2 protein was further suggested by binding of CD44 from cellular lysates to recombinant NF2 protein. Interaction between NF2 protein and the actin-containing cytoskeleton was indicated by partial colocalization, by cytochalasin B-induced coclustering, and by retention of NF2 protein in the detergent-insoluble fraction. Transfected NF2 protein induced morphogenic changes. The cells contained restructured membrane extensions and blebs, and CHO cells expressing NF2 protein were more elongated than control transfectants. In conclusion, NF2 protein possesses functional properties of an ERM family member.

    Topics: Actins; Animals; Cell Membrane; CHO Cells; COS Cells; Cricetinae; Cytochalasin B; Cytoskeletal Proteins; Cytoskeleton; Detergents; Fluorescent Antibody Technique; Gene Expression; Glioma; Humans; Hyaluronan Receptors; Immunoblotting; Kidney; Membrane Proteins; Neoplasm Proteins; Neurofibromin 2; Phosphoproteins; Rabbits; Transfection; Tumor Cells, Cultured

1997
Cell-based screen for identification of inhibitors of tubulin polymerization.
    Journal of natural products, 1996, Volume: 59, Issue:12

    This assay is based on morphological changes of rat glioma cells treated with db-cAMP. The db-cAMP treatment induces a tubulin-dependent change causing the cells to acquire a spherical shape. Pretreatment with tubulin inhibitors brings about the disintegration of tubulin polymer and/or prevents its polymerization. Cells with inhibited tubulin fail to respond to db-cAMP treatment. Cells treated with inhibitors of tubulin polymerization are then separated from the spherical cells by aspiration. A semiautomated scanning procedure evaluates the final culture density and yields graphical data.

    Topics: Animals; Brain Neoplasms; Bucladesine; Cell Differentiation; Drug Screening Assays, Antitumor; Formazans; Glioma; Rats; Tubulin; Tumor Cells, Cultured

1996
Assessment of brain tumor cell motility in vivo and in vitro.
    Journal of neurosurgery, 1995, Volume: 82, Issue:4

    Brain tumor dispersal far from bulk tumor contributes to and, in some instances, dominates disease progression. Three methods were used to characterize brain tumor cell motility in vivo and in vitro: 1) 2 weeks after implantation in rat cerebral cortex, single C6 cells labeled with a fluorescent tag had migrated to brain sites greater than 16 mm distant from bulk tumor; 2) time-lapse videomicroscopy of human brain tumor cells revealed motility of 12.5 microns/hr. Ruffling leading edges and pseudopod formation were most elaborate in more malignant cells; 3) an in vitro assay was devised to quantitatively evaluate motility from a region of high cell density to one of lower cell density. Human brain tumor cells were plated in the center of a petri dish, washed, and refed, establishing a 2-cm circular zone of cells in the dish center. Motility was determined by counting cells daily at predetermined distances from the central zone perimeter. Cells were found 1 cm from the perimeter by 24 hours and 3 cm from the perimeter by 4 days. Increasing serum concentration increased motility; however, neither fibronectin nor arrest of cells in the G0 phase by hydroxyurea altered motility. The addition of cytochalasin B to block cytoskeletal assembly prevented cell motility. Motility increased with increased malignancy. Subpopulations of cells were created by clonal amplification of cells that had migrated most rapidly to the dish periphery. Although morphologically indistinguishable when compared to the original cell line from which they were derived, these subpopulations demonstrated significantly increased motility.

    Topics: Amidines; Animals; Astrocytoma; Brain Neoplasms; Cell Movement; Clone Cells; Cytochalasin B; Fibronectins; Fluorescent Dyes; Glioma; Humans; Hydroxyurea; Image Processing, Computer-Assisted; Interphase; Microscopy, Video; Neoplasm Transplantation; Pseudopodia; Rats; Rats, Sprague-Dawley; Tumor Cells, Cultured

1995
Inhibition of phosphatidylcholine and phosphatidylethanolamine biosynthesis by cytochalasin B in cultured glioma cells: potential regulation of biosynthesis by Ca(2+)-dependent mechanisms.
    Biochimica et biophysica acta, 1991, Jul-09, Volume: 1084, Issue:2

    The major route of phosphatidylcholine (PtdCho) biosynthesis in mammalian cells is the sequence: choline (Cho)----phosphocholine (PCho)----cytidinediphosphate choline (CDP-Cho)----PtdCho. Recently, we have found that intermediates of this pathway are not freely diffusible in cultured rat glioma (C6) cells but are channeled towards PtdCho biosynthesis (George et al. (1989). Biochim. Biophys. Acta. 1004, 283-291). Channeling of intermediates in other mammalian systems is thought to be mediated through adsorption of enzymes to membranes and cytoskeletal elements to form multienzyme complexes. In this study, agents which perturb the structure and function of cytoskeletal elements were tested for effects on phospholipid metabolism in glioma cells. The filament-disrupting agent cytochalasin B (CB), but not other cytochalasins or the microtubule depolymerizer colchicine inhibited PtdCho and phosphatidylethanolamine (PtdEtn) biosynthesis as judged by dose-dependent reduction of labeling from [3H]Cho and [14C]ethanolamine (Etn). 32Pi pulse-labeling indicated that CB selectively decreased PtdCho and PtdEtn biosynthesis without affecting synthesis of other phospholipids. Synthesis of water-soluble intermediates of PtdCho metabolism was unaffected but the conversion of phosphoethanolamine to CDP-ethanolamine was reduced by CB. Effects of CB on phospholipid biosynthesis were not due to inhibition of glucose uptake as shown by experiments with 2-deoxyglucose, glucose-starved cells and other cytochalasins. Experiments with Ca(2+)-EGTA buffers and digitonin-permeabilized cells, and the Ca(2+)-channel blocker verapamil suggest that effects of CB on PtdCho and PtdEtn biosynthesis are due to alteration of intracellular Ca2+. Taken together, these results suggest that CB acts at sites distinct from glucose transport and cellular microfilaments to specifically inhibit PtdCho and PtdEtn biosynthesis by mechanisms dependent on intracellular Ca2+.

    Topics: Animals; Biological Transport, Active; Calcium; Carbon Radioisotopes; Cell Line; Choline; Cytochalasin B; Deoxyglucose; Ethanolamine; Ethanolamines; Glioma; Glucose; Kinetics; Phosphates; Phosphatidylcholines; Phosphatidylethanolamines; Phosphorus Radioisotopes; Rats; Tritium; Verapamil

1991
Motility factor produced by malignant glioma cells: role in tumor invasion.
    Journal of neurosurgery, 1990, Volume: 73, Issue:6

    To better understand the cellular mechanism of tumor invasion, the production of a cell motility-stimulating factor by malignant glioma cells was studied in vitro. Serum-free conditioned media from cultures of rat C6 and human T98G cell lines contained a factor that stimulated the locomotion of the producer cells. This factor was termed the "glioma-derived motility factor." The glioma-derived motility factor is a heat-labile protein with a molecular weight greater than 10 kD and has relative stability to acid. The factor showed not only chemotactic activity but also chemokinetic (stimulated random locomotion) activity in the two types of glioma cells studied. Although glioma-derived motility factors in conditioned media obtained from two different cell origins are likely to be the same, chemokinetic migration of T98G cells to their conditioned medium was much stronger than that of C6 cells to theirs. Coincubation of cells with cytochalasin B, which disrupts the assembly of cellular actin microfilaments, almost completely inhibited the cell migration stimulated by glioma-derived motility factor. Cytochalasin B also induced marked alterations in cell morphology, including cell retraction and arborization, while the drug did not affect cell attachment to culture dishes. These results indicate that glioma cells produce a motility factor which may play a role particularly when tumor cells are detached and migrate away from the original tumor mass, thus promoting tumor invasion. Also, glioma cell migration stimulated by the motility factor requires the normal organization of cytoskeletons such as actin microfilaments.

    Topics: Animals; Chemotaxis; Culture Media; Cytochalasin B; Glioma; Humans; Neoplasm Invasiveness; Neoplasm Proteins; Rats; Tumor Cells, Cultured

1990
Cell adhesion to fibronectin and tenascin: quantitative measurements of initial binding and subsequent strengthening response.
    The Journal of cell biology, 1989, Volume: 109, Issue:4 Pt 1

    Cell-substratum adhesion strengths have been quantified using fibroblasts and glioma cells binding to two extracellular matrix proteins, fibronectin and tenascin. A centrifugal force-based adhesion assay was used for the adhesive strength measurements, and the corresponding morphology of the adhesions was visualized by interference reflection microscopy. The initial adhesions as measured at 4 degrees C were on the order of 10(-5)dynes/cell and did not involve the cytoskeleton. Adhesion to fibronectin after 15 min at 37 degrees C were more than an order of magnitude stronger; the strengthening response required cytoskeletal involvement. By contrast to the marked strengthening of adhesion to FN, adhesion to TN was unchanged or weakened after 15 min at 37 degrees C. The absolute strength of adhesion achieved varied according to protein and cell type. When a mixed substratum of fibronectin and tenascin was tested, the presence of tenascin was found to reduce the level of the strengthening of cell adhesion normally observed at 37 degrees C on a substratum of fibronectin alone. Parallel analysis of corresponding interference reflection micrographs showed that differences in the area of cell surface within 10-15 nm of the substratum correlated closely with each of the changes in adhesion observed: after incubation for 15 min on fibronectin at 37 degrees C, glioma cells increased their surface area within close contact to the substrate by integral to 125-fold. Cells on tenascin did not increase their surface area of contact. The increased surface area of contact and the inhibitory activity of cytochalasin b suggest that the adhesive "strengthening" in the 15 min after initial binding brings additional adhesion molecules into the adhesive site and couples the actin cytoskeleton to the adhesion complex.

    Topics: Animals; Astrocytoma; Cell Adhesion; Cell Adhesion Molecules, Neuronal; Cell Line; Cytochalasin B; Fibroblasts; Fibronectins; Glioma; Humans; Kinetics; Neoplasm Proteins; Tenascin

1989
Morphologic plasticity of rapid-onset neurites in NG108-15 cells stimulated by substratum-bound laminin.
    Brain research. Developmental brain research, 1989, Jan-01, Volume: 45, Issue:1

    Undifferentiated NG108-15 cells, when replated onto laminin-coated substrata, extend multipolar, highly branched neurite-like extensions up to 200 microns in length within 4 h; morphologic and pharmacologic properties of these 'rapid-onset neurites' have been described recently. The present study has extended these observations, using time lapse video recordings of their dynamic behavior and additional pharmacologic studies. Rapid-onset neurites and neuronal growth cones were shown to be regulated in an identical manner in all respects examined, including inhibition of outgrowth by cytochalasin B. Of particular interest was the observation that rapid-onset neurites in contact with laminin exhibited an extremely high rate of turnover, which was inhibited by 5'-deoxy-5'-methylthioadenosine (MTA). This system provides a uniquely favorable in vitro preparation in which neuritic plasticity can be elicited, directly observed and experimentally modulated under controlled conditions.

    Topics: Adenosine; Animals; Cell Differentiation; Cells, Cultured; Cytochalasin B; Dendrites; Deoxyadenosines; Glioma; Laminin; Neuroblastoma; Thionucleosides; Time Factors; Tumor Cells, Cultured

1989
Glucose transporter in plasma membranes of cultured neural cells, as characterized by cytochalasin B binding.
    Journal of neurochemistry, 1986, Volume: 47, Issue:5

    Identification of hexose transporter sites by cytochalasin B binding was conducted with a centrifugation assay. The determination of KD and Bmax values by LIGAND computer analysis provided binding data that are similar in primary astrocytes (238 nM and 14 pmol/mg protein) and neuroblastoma cells (179 nM and 13.6 pmol/mg protein). In contrast, only an insignificant number of transporter sites was detectable in C6 glioma cells, irrespective of whether membrane fractions were obtained by a two-phase polymer system or by a latex phagocytosis technique yielding inside-out plasma membranes. The latter membrane preparation was utilized to identify and quantitate the transporter molecules at the inner membrane surface of primary astrocytes, i.e., 160 nM (KD) and 5.8 pmol/mg protein (Bmax), respectively.

    Topics: Animals; Astrocytes; Binding, Competitive; Cell Line; Cell Membrane; Cytochalasin B; Glioma; Kinetics; Monosaccharide Transport Proteins; Neuroblastoma; Neurons

1986
Promotion of cell-substratum adhesion of clonal rat pheochromocytoma cells (PC12) by factors contained in glioma-conditioned medium (GCM): separation of two active factors contained in GCM.
    Brain research, 1986, Volume: 389, Issue:1-2

    Culture medium conditioned over C6 glioma cells (GCM) contains factors which induce neurite outgrowth from clonal rat pheochromocytoma (PC12) cells. The effects of GCM on the cell-substratum adhesion of PC12 cells, which is an early event required for the neurite outgrowth, were investigated. The results obtained are as follows. Addition of GCM promoted the adhesion of PC12 cells specifically to collagen-coated tissue culture dish. The GCM-promoted adhesion of PC12 cells was prevented by the treatment of the cells with cytochalasin B, concanavalin A and glycosidase mixture suggesting the contribution of microfilaments and cell surface carbohydrates in the cell adhesion. GCM did not increase significantly the intracellular content of cAMP and the extent of cell adhesion promoted by cAMP or dibutyryl-cAMP was much less than that by GCM. Two active factors contained in GCM were separated by either gel filtration or chromatofocusing using the cell adhesion assay as an index. The first factor with an apparent mol. wt. around 40,000 had the abilities to induce the neurite outgrowth and to enhance the choline acetyltransferase activity in addition to the ability to promote the adhesion of PC12 cells. The second factor with an apparent mol. wt. around 10,000 was devoid of the ability to induce the neurite outgrowth, but had the abilities to enhance the choline acetyltransferase activity and to promote the adhesion of PC12 cells. Both factors were sensitive to trypsin digestion and relatively heat stable. The significance of these factors in the neuronal differentiation was discussed.

    Topics: Adrenal Gland Neoplasms; Animals; Carbohydrates; Cell Adhesion; Cell Line; Choline O-Acetyltransferase; Clone Cells; Colchicine; Culture Media; Cytochalasin B; Glioma; Hot Temperature; Nerve Growth Factors; Nerve Tissue Proteins; Pheochromocytoma; Rats; Species Specificity

1986
Effect of drugs and temperature on biosynthesis and transport of glycosphingolipids in cultured neurotumor cells.
    Biochimica et biophysica acta, 1984, May-22, Volume: 804, Issue:1

    Neuroblastoma and glioma cells were grown in the presence of [3H]galactose, and the incorporation of 3H into gangliosides and the transport of newly synthesized gangliosides to the cell surface were examined under different experimental conditions. A variety of drugs, including inhibitors of protein synthesis and energy metabolism, modulators of the cytoskeleton and the ionophore monensin, had no effect on the transport of newly synthesized GD1a in neuroblastoma cells. Only low temperature effectively blocked translocation to the plasma membrane. Monensin, however, had marked effects on the biosynthesis of gangliosides and neutral glycosphingolipids. Whereas incorporation of 3H into complex glycosphingolipids was reduced, labeling of glucosylceramide was increased in cells exposed to monensin. In addition, biosynthesis of the latter glycolipid was less susceptible to low temperatures than that of more complex ones. Previous studies have implicated the Golgi apparatus as the predominant site of glycosylation of gangliosides. As monensin has been reported to interfere with the Golgi apparatus, our results indicate that glucosylceramide may be synthesized at a site that is separate from the site where further glycosylation occurs. Once synthesis of a ganglioside is completed, transport of the molecule to the cell surface proceeds under conditions of cytoskeletal disruption, energy depletion and ionic inbalance , but not low temperature.

    Topics: Animals; Biological Transport; Cells, Cultured; Colchicine; Cycloheximide; Cytochalasin B; Glioma; Glycosphingolipids; Golgi Apparatus; Ionophores; Mice; Monensin; Neuroblastoma; Puromycin; Rats; Temperature; Vinblastine

1984
Multinucleation in response to cytochalasin B: a common feature in several human tumor cell lines.
    Cancer research, 1982, Volume: 42, Issue:7

    Human tumor cell lines derived from melanoma, glioblastoma, and carcinoma of the prostate, bladder, and kidney multinucleated in response to growth in cytochalasin B-supplemented medium, whereas cell lines derived from normal prostate, kidney, skin, lung, and other nonmalignant diseases remained predominantly binucleate under comparable conditions. The multinucleate cytochalasin B phenotype was dissociable from the anchorage-independent phenotype of tumor cells, suggesting that these markers of cellular transformation are under separate control. These results suggest that uncontrolled nuclear division by tumor cells may be a general marker of abnormal growth or regulation.

    Topics: Cell Line; Cell Nucleus; Cytochalasin B; Glioma; Humans; Male; Melanoma; Neoplasms; Prostate; Prostatic Hyperplasia; Prostatic Neoplasms; Urinary Bladder Neoplasms

1982
Uptake of methylmercury and inorganic mercury by mouse glioma and mouse neuroblastoma cells.
    Neurotoxicology, 1982, Volume: 3, Issue:4

    Methylmercury was taken up preferentially by mouse glioma and mouse neuroblastoma cells relative to inorganic mercury. Methylmercury uptake was depressed by lowering the cellular ATP level or the incubation temperature, while the uptake of inorganic mercury was not affected by these treatments. When the cells were treated with reagents such as cytochalasin B, colchicine and vinblastine which are known to affect membrane permeability, changes in permeability to methylmercury caused by these reagents were markedly different from those to inorganic mercury. Inorganic mercury above 2 x 10(-5)M caused the release of 2-deoxyglucose trapped in the cells and the amount of inorganic mercury taken up by the cells increased markedly at higher concentrations. Inorganic mercury thus appeared to move into the cells after disrupting the membrane barrier, while methylmercury can penetrate the cells without any noticeable damage to the barrier.

    Topics: Animals; Cells, Cultured; Colchicine; Cytochalasin B; Deoxyglucose; Glioma; Mercury; Methylmercury Compounds; Mice; Neoplasms, Experimental; Neuroblastoma; Vinblastine

1982
Translational mobility of concanavalin A receptors in normal and neoplastic glial cells.
    Acta neuropathologica, 1982, Volume: 58, Issue:3

    The dynamics of cell-associated Concanavalin A (Con A) in astrocytes of the newborn rat (RNA), the rat glioma (AC), and the human glioblastoma (GB) were studied in vitro by fluorescence and electron microscopy. Con A receptors on the cell surface were seen usually as a continuous thin layer, and Con A accumulations in fluorescence microscopy were actually Con A receptors on complicatedly infolded cell membrane and collection of Con A pinosomes. No capping occurred in the three types of glial cells. The translational movement of Con A receptors on the cell surface was rapid in the AC, slow in the RNA, and intermediate in the GB, and partly associated with Con A internalization. Con A pinosomes were more numerous in the RNA compared with those in the AC and the GB. Colchicine accelerated the translational mobility of surface Con A receptors more markedly in the AC and the GB than in the RNA. The translational movement Con A receptors, when treated with cytochalasin B, was retarded in the RNA and the GB and rather accelerated in the AC. Con A pinosomes were decreased in the three types of glial cells by treatment with colchicine or cytochalasin B.

    Topics: Animals; Astrocytes; Brain Neoplasms; Colchicine; Cytochalasin B; Glioma; Microscopy, Electron; Microscopy, Fluorescence; Neuroglia; Rats; Receptors, Concanavalin A

1982
Novel vesicular extrusions during cell spreading.
    Experientia, 1982, May-15, Volume: 38, Issue:5

    During the late stages of cell spreading in vitro, the cells extrude a vesicular material into the medium. This phenomenon was observed in human glia and glioma cells as well as in human diploid fibroblasts MRC-5 and WI-38 cells. This extrusion of vesicular material is inhibited by cytochalasin-B and colcemid suggesting the involvement of microfilaments and microtubules and the active nature of this event. It appears that the cells may be excreting damaged surface components by a mechanism similar to patching, capping and endocytosis.

    Topics: Cell Line; Cytochalasin B; Cytoskeleton; Demecolcine; Fibroblasts; Glioma; Humans; Microtubules; Neuroglia; Organoids

1982
Cytoskeletal structures and 3-hydroxy-3-methylglutaryl coenzyme A reductase in C-6 glial cells. A role for microfilaments.
    The Journal of biological chemistry, 1981, Feb-25, Volume: 256, Issue:4

    Topics: 2',3'-Cyclic-Nucleotide Phosphodiesterases; Acetyl-CoA Carboxylase; Animals; Cell Line; Cholesterol; Cytochalasin B; Cytochalasin D; Cytochalasins; Fatty Acid Synthases; Glioma; Hydroxymethylglutaryl CoA Reductases; Hydroxymethylglutaryl-CoA Synthase; Kinetics; NADPH-Ferrihemoprotein Reductase; Rats

1981
An investigation in vitro of the exocytosis of lysosomal enzymes from C6 glioma cells.
    Acta neuropathologica. Supplementum, 1981, Volume: 7

    The rates of exocytosis on the lysosomal hydrolase n-acetyl-beta D-glucosaminidase and beta-glucuronidase were measured in monolayer cultures of the C-6 glioma cell line. A comparison of the kinetics of release of the enzymes and the effects of cytochalasin B suggest that either intralysosomal localisation or the mechanism of release may be different for each enzyme. Evidence was obtained that exocytosis is accompanied by receptor-mediated endocytosis of hydrolases and the importance of the microtubular system in the maintenance of the exocytosis equilibrium was indicated by the effect of colchicine on the rate of extracellular accumulation of the enzymes.

    Topics: Acetylglucosaminidase; Animals; Cell Line; Colchicine; Cytochalasin B; Exocytosis; Glioma; Glucuronidase; Hexosaminidases; Lysosomes; Rats

1981
Effects of dibutyryl cyclic AMP and cytochalasin B on cultured human glioma cells.
    Zeitschrift fur mikroskopisch-anatomische Forschung, 1979, Volume: 93, Issue:3

    Cultured human glioma cells (138 MG) exposed to dibutyryl cyclic AMP (dbc-AMP; 0.1--5 mM) attained an arborized shape with thin processes extending from a rounded cell body. Cytochalasin B (CB; 1--1 muM) induced similar morphological changes. The processes in both dbc-AMP and CB treated cells were formed by retraction of the cell margin. Colchicine (1muM) completely and liver treated phalloidin (0.1 mg/ml) partially inhibited the morphological alterations induced by dbc-AMP and CB. Dbc-AMP was found to arrest cell movement, cell division and uptake of 2-deoxy-D-glucose. CB has the same effects but was more potent. The effects of dbc-AMP and CB could be due to interference with a common cellular structure, e.g. microfilaments.

    Topics: Bucladesine; Cell Movement; Cells, Cultured; Cytochalasin B; Cytoskeleton; Deoxyglucose; Drug Evaluation, Preclinical; Glioma; Humans; In Vitro Techniques; Microscopy, Electron, Scanning; Microtubules

1979
The effects of cytochalasin B and colchicine on cell motility and ultrastructure in primary cultures of malignant gliomas.
    Acta neuropathologica, 1978, Oct-13, Volume: 44, Issue:1

    Primary tissue cultures of human gliomas were treated with cytochalasin B (0.5--60 microgram/ml for 90 min). Cell motility was inhibited irreversibly in glial tumour cells, but the effect was reversible on the mesenchymal cells growing in culture in the lower dose range. Cell adhesion was considerably reduced as the dose was increased, as was the capacity for cells to spread on a surface from suspension. Low concentrations of cytochalasin B caused negligible cell death and little disruption of cell ultrastructure. However, increases in dose were accompanied by a greater predominance of rough endoplasmic reticulum and inclusions and aggregation of microfilament bundles. As seen by scanning electron microscopy, cytochalasin B caused the withdrawal of peripheral cell borders, disappearance of ruffles and the breakdown of cytoplasmic lamellae. Charateristic surface blebs and folds appeared in their place. By comparison, colchicine (1--10 microgram/ml) caused a less marked and non-specific reversible reduction in cell motility on both glial and mesenchymal cells. No significant change in cell adhesion or spreading took place even at high doses, although at all concentrations gross disruption of the cell surface took place with changes in ultrastructure characterised by loss of cytoplasmic microtubules and aggregation of 10 nm filaments.

    Topics: Brain Neoplasms; Cell Movement; Cell Survival; Colchicine; Connective Tissue; Cytochalasin B; Cytoskeleton; Endoplasmic Reticulum; Glioma; Humans; Microscopy, Electron; Microscopy, Electron, Scanning; Microtubules; Neuroglia

1978
Uptake of 3-O-methyl-D-glucose into cultured human glioma cells.
    Journal of neurochemistry, 1975, Volume: 24, Issue:2

    Topics: Biological Transport; Bucladesine; Cells, Cultured; Culture Media; Cyanides; Cytochalasin B; Glioma; Humans; Iodoacetates; Kinetics; Methylglucosides; Methylglycosides; Ouabain; Phloretin; Phlorhizin; Time Factors

1975
Cyclic AMP, membrane transport and cell division. I. Effects of various chemicals on cyclic AMP levels and rate of transport of neucleosides, hypoxanthine and deoxyglucose in several lines of cultured cells.
    Journal of cellular physiology, 1975, Volume: 85, Issue:2 Pt 1

    Nutrient transport rates and cyclic AMP levels have been implicated in the regulation of cell proliferation. In the present study, however, changes in intracellular cyclic AMP level in several lines of cultured cells (normal 3T3 and SV40 and polyomavirus-transformed 3T3 cells; 3T6, C6 GLIOMA, MOUSE L, and Novikoff rat hepatoma cells) by treatment with papaverine, prostaglandine E1 or isoproterenol did not correlate with the inhibition of the uridine, hypoxanthine or deoxyglucose transport rates by these chemicals. Transport inhibitions by above chemicals or Persantin or Cytochalasin B occurred in most cell lines in the absence of any measurable change in intracellular cyclic AMP concentration. Furthermore, treatment of several cell lines with 1 mM dibutyryl cyclic AMP had no immediate effect on the transport of uridine, thymidine or deoxyglucose, although the transport capacity of the cells for uridine and thymidine, but not that for deoxyglucose, decreased progressively with time of treatment. We also observed that the uridine transport system of all cell lines derived from 3T3 cells and the hypoxanthine transport system of L cells exhibited high degrees of resistance to inhibition by the various chemicals. On the other hand, deoxyglucose transport was inhibited to about the same extent by these chemicals in all the cell lines investigated.

    Topics: Animals; Biological Transport, Active; Bucladesine; Carcinoma, Hepatocellular; Cell Division; Cell Line; Cell Membrane; Cell Transformation, Neoplastic; Cells, Cultured; Cyclic AMP; Cytochalasin B; Deoxy Sugars; Deoxyglucose; Depression, Chemical; Dipyridamole; Glioma; Hypoxanthines; Isoproterenol; L Cells; Liver Neoplasms; Mice; Papaverine; Prostaglandins; Rats; Thymidine; Uridine

1975