INDUCTION OF TRYPTOPHANPYRROLASE IN THE TRANSPLANTABLE HEPATOMA CELLS 22a BY SPLENOCYTES SENSIBILIZED TO NORMAL CELL ANTIGENS

1981 ◽  
Vol 9 (2) ◽  
pp. 257P-257P
Author(s):  
M. D. Chernysheya ◽  
V. Ya. Fel
Keyword(s):  
Normal Cell ◽  
Hepatoma Cells ◽  
Transplantable Hepatoma

Stimulated Virus Production in Vinblastine and Cytochalasin-Induced Multinucleate Cells

1970 ◽  
Vol 28 ◽  
pp. 186-187
Author(s):  
Krishan Awtar
Keyword(s):  
Cell Division ◽  
Normal Cell ◽  
Virus Production ◽  
Multinucleate Cells ◽  
Daughter Cells ◽  
Cell Divisions ◽  
Nuclear Membranes ◽  
Division 2 ◽  
Vinblastine Sulfate

Exposure of cells to low sublethal but mitosis-arresting doses of vinblastine sulfate (Velban) results in the initial arrest of cells in mitosis followed by their subsequent return to an “interphase“-like stage. A large number of these cells reform their nuclear membranes and form large multimicronucleated cells, some containing as many as 25 or more micronuclei (1). Formation of large multinucleate cells is also caused by cytochalasin, by causing the fusion of daughter cells at the end of an otherwise .normal cell division (2). By the repetition of this process through subsequent cell divisions, large cells with 6 or more nuclei are formed.

Electron Microscopy and image analysis of nucleo-protein complexes

1994 ◽  
Vol 52 ◽  
pp. 88-89
Author(s):  
E. H. Egelman ◽  
X. Yu
Keyword(s):  
Electron Microscopy ◽  
Image Analysis ◽  
Normal Cell ◽  
Genetic Recombination ◽  
Protein Complexes ◽  
Chromosomal Rearrangements ◽  
Reca Protein ◽  
E Coli ◽  
Helical Polymer ◽  
Specific Protease

The RecA protein of E. coli has been shown to mediate genetic recombination, regulate its own synthesis, control the expression of other genes, act as a specific protease, form a helical polymer and have an ATPase activity, among other observed properties. The unusual filament formed by the RecA protein on DNA has not previously been shown to exist outside of bacteria. Within this filament, the 36 Å pitch of B-form DNA is extended to about 95 Å, the pitch of the RecA helix. We have now establishedthat similar nucleo-protein complexes are formed by bacteriophage and yeast proteins, and availableevidence suggests that this structure is universal across all of biology, including humans. Thus, understanding the function of the RecA protein will reveal basic mechanisms, in existence inall organisms, that are at the foundation of general genetic recombination and repair.Recombination at this moment is assuming an importance far greater than just pure biology. The association between chromosomal rearrangements and neoplasms has become stronger and stronger, and these rearrangements are most likely products of the recombinatory apparatus of the normal cell. Further, damage to DNA appears to be a major cause of cancer.

Generation of syngeneic murine hepatoma cells bearing features of human HCC for rapid anti-HCC drug screening

2020 ◽  
Author(s):  
L Kaps ◽  
A Klefenz ◽  
D Castven ◽  
JU Marquardt ◽  
N Choteschovsky ◽  
...  
Keyword(s):  
Drug Screening ◽  
Hepatoma Cells

Insulin stimulates accumulation and efflux of macromolecules in isolated nuclei from H35 hepatoma cells

Diabetes ◽  
1992 ◽  
Vol 41 (2) ◽  
pp. 194-201 ◽  
Author(s):  
A. P. Soler ◽  
R. M. Smith ◽  
L. Jarett
Keyword(s):  
Hepatoma Cells ◽  
Isolated Nuclei

Cytotoxic Effect of Pseudomonas aurogenosa Protease on Cancer Cells

2019 ◽  
Vol 10 (03) ◽  
Author(s):  
Ghanyia J. Shanyoor ◽  
Fatima R. Abdul ◽  
Nehad A. Taher ◽  
Ihsan A. Raheem
Keyword(s):  
Cell Line ◽  
Normal Cell ◽  
Cytotoxic Effect ◽  
Human Cancer ◽  
Skim Milk ◽  
Exchange Chromatography ◽  
Protease Production ◽  
Normal Cell Line ◽  
Protease Enzyme ◽  
Embryonic Fibroblast

About (20) Pseudomonas rogenosa isolate were experienced for their ability of protease production by calculating the diameter of lysis area after developing on skim milk agar medium (qualitatively ) and the results exhibited that only isolate no (5), was higher isolate for protease making of (26mm) of lysis area. Then, the protein concentration also identified by Bradford method and it was found of 0.16 mg/ ml , then purification was done by using an ion- exchange chromatography with DEAE sephadex G- 100 column and the results showed the presence of 1 peak of enzyme with 50 Kd of molecular weight 2 peaks of other proteins . we tried to investigate the invitro Cytotoxic effect of purified enzyme against two human cancer lines, HeP2 (Human larynx epidermed carcinoma ) , RD ( Rabdo- Sarcoma ) , and one normal cell line Ref ( Rat embryonic fibroblast ) . The cancer and normal cells were treated with different concentrations of protease enzyme ranging from ( 0.05, 0.1, 0.2, 0.4,0.8and 0.16 mg/ml) then incubated for additional 48h at 37C0 and the results showed highest toxicity ( 80.28%) of protease enzyme on RD , moderate cytotoxicity (45.52%) on Hep andslight toxicity ( 37.12% ) on normal cell line (Ref) in a concentration (0.8mg/ml).

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