cytochalasin-d has been researched along with Lymphoma* in 3 studies
3 other study(ies) available for cytochalasin-d and Lymphoma
| Article | Year |
|---|---|
Interactions between a lymphoma membrane-associated guanosine 5'-triphosphate-binding protein and the cytoskeleton during receptor patching and capping.
In this study we have used several complementary techniques to isolate and characterize a lymphoma membrane-associated 41-kDa protein that shares a number of structural and functional similarities with the alpha i subunit of the guanosine 5'-triphosphate (GTP)-binding protein (e.g., Gi alpha-like protein). In addition, using permeabilized lymphoma cells, we have found that: 1) GTP or GTP-tau-S augments, and pertussis toxin inhibits, phospholipase C (PLC) activity and receptor capping; and 2) the addition of lymphoma 41-kDa Gi alpha-like protein stimulates PLC activity and receptor patching/capping, and reverses the inhibitory effect of pertussis toxin on both activity and receptor patching/capping. Additional cytochemical and biochemical data indicate that the lymphoma 41-kDa protein is closely associated with several cytoskeletal proteins (e.g., actin, myosin, and fodrin) all of which colocalize under receptor cap structures. Furthermore, both the 41-kDa-mediated phospholipase C activity and receptor patching/capping are inhibited by cytochalasin D (a microfilament disrupting drug) and W-7 drug (a calmodulin inhibitor). Together, these data provide strong evidence for a functional association between the lymphoma membrane cytoskeleton and the 41-kDa (Gi alpha-like) protein. Specifically, this association appears to be required for the activation of phospholipase C that results in inositol triphosphate production, subsequent internal Ca2+ release, and finally surface receptor patching and capping. Topics: Animals; Antigens, Surface; Cell Line; Cytochalasin D; Cytoskeleton; GTP-Binding Proteins; Guanosine Triphosphate; Immunologic Capping; Lymphoma; Membrane Proteins; Mice; Molecular Weight; Peptide Mapping; Pertussis Toxin; Receptor Aggregation; Sulfonamides; Thy-1 Antigens; Tumor Cells, Cultured; Type C Phospholipases; Virulence Factors, Bordetella | 1990 |
Regulation of c-myc gene transcription in B lymphocytes: mechanisms of negative and positive control.
Topics: Animals; B-Lymphocytes; Cytochalasin D; Cytochalasins; Gene Expression Regulation; Lymphoma; Proto-Oncogenes; Transcription, Genetic; Tumor Cells, Cultured | 1988 |
Inhibition of host cellular ribonucleic acid synthesis by glycoprotein of mumps virus.
After infection with mumps virus, cellular ribonucleic acid synthesis of a murine lymphoma cell line, EL4, was appreciably depressed. The inactivation of viral infectivity by ultraviolet irradiation or the treatment of cells with mouse interferon did not abolish the inhibiting effect, suggesting that virus replication is not required for the depressed RNA synthesis. Envelope glycoproteins isolated from disrupted mumps virus caused inhibition of cellular RNA synthesis. The addition of low concentrations of specific antibody enhanced the inhibitory effect, probably through the formation of aggregates of glycoproteins. On the contrary, the glycoproteins showed no effect on RNA synthesis in the presence of cytochalasin D. Topics: Animals; Cell Line; Cell Transformation, Viral; Cytochalasin D; Cytochalasins; Kinetics; Lymphoma; Mice; Mumps virus; Transcription, Genetic; Ultraviolet Rays; Viral Envelope Proteins | 1984 |