Molecular and Cellular Effects of Heat-shock and Related Treatments of Mammalian Tissue-culture Cells

1982 ◽  
Vol 46 (0) ◽  
pp. 985-996 ◽  
Author(s):  
G. P. Thomas ◽  
W. J. Welch ◽  
M. B. Mathews ◽  
J. R. Feramisco
Keyword(s):  
Tissue Culture ◽  
Heat Shock ◽  
Mammalian Tissue ◽  
Cellular Effects ◽  
Culture Cells ◽  
Tissue Culture Cells

Sulfhydryl bond formation is a prerequisite for proper cycling of centrosomes and chromosomes in mammalian tissue culture cells

1993 ◽  
Vol 51 ◽  
pp. 342-343
Author(s):  
Heide Schatten ◽  
Neidhard Paweletz ◽  
Ron Balczon
Keyword(s):  
Tissue Culture ◽  
Cell Cycle Progression ◽  
Group Formation ◽  
Sulfhydryl Group ◽  
Mammalian Tissue ◽  
Mitotic Chromosomes ◽  
Microtubule Network ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Transmission Electron

To study the role of sulfhydryl group formation during cell cycle progression, mammalian tissue culture cells (PTK2) were exposed to 100¼M 2-mercaptoethanol for 2 to 6 h during their exponential phase of growth. The effects of 2-mercaptoethanol on centrosomes, chromosomes, microtubules, membranes and intermediate filaments were analyzed by transmission electron microscopy (TEM) and by immunofluorescence microscopy (IFM) methods using a human autoimmune antibody directed against centrosomes (SPJ), and a mouse monoclonal antibody directed against tubulin (E7). Chromosomes were affected most by this treatment: premature chromosome condensation was detected in interphase nuclei, and the structure in mitotic chromosomes was altered compared to control cells. This would support previous findings in dividing sea urchin cells in which chromosomes are arrested at metaphase while the centrosome splitting cycle continues. It might also support findings that certairt-sulfhydryl-blocking agents block cyclin destruction. The organization of the microtubule network was scattered probably due to a looser organization of centrosomal material at the interphase centers and at the mitotic poles.

scholarly journals Screens Using RNAi and cDNA Expression as Surrogates for Genetics in Mammalian Tissue Culture Cells

2005 ◽  
Vol 70 (0) ◽  
pp. 449-459 ◽  
Author(s):  
J. PEARLBERG ◽  
S. DEGOT ◽  
W. ENDEGE ◽  
J. PARK ◽  
J. DAVIES ◽  
...  
Keyword(s):  
Tissue Culture ◽  
Mammalian Tissue ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Cdna Expression

Cytoplasmic inheritance in mammalian tissue culture cells

In Vitro ◽  
1976 ◽  
Vol 12 (11) ◽  
pp. 758-776 ◽  
Author(s):  
Douglas C. Wallace ◽  
Y. Pollack ◽  
C. L. Bunn ◽  
J. M. Eisenstadt
Keyword(s):  
Tissue Culture ◽  
Cytoplasmic Inheritance ◽  
Mammalian Tissue ◽  
Culture Cells ◽  
Tissue Culture Cells

scholarly journals Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway through SENP3 and SENP5 proteases

2008 ◽  
Vol 183 (4) ◽  
pp. 589-595 ◽  
Author(s):  
Chawon Yun ◽  
Yonggang Wang ◽  
Debaditya Mukhopadhyay ◽  
Peter Backlund ◽  
Nagamalleswari Kolli ◽  
...  
Keyword(s):  
Tissue Culture ◽  
Ribosome Biogenesis ◽  
Mammalian Tissue ◽  
Hematopoietic Malignancies ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Egg Extracts ◽  
Protein B23 ◽  
Sumo Pathway

Ubiquitin-like protein/sentrin-specific proteases (Ulp/SENPs) mediate both processing and deconjugation of small ubiquitin-like modifier proteins (SUMOs). Here, we show that Ulp/SENP family members SENP3 and SENP5 localize within the granular component of the nucleolus, a subnucleolar compartment that contains B23/nucleophosmin. B23/nucleophosmin is an abundant shuttling phosphoprotein, which plays important roles in ribosome biogenesis and which has been strongly implicated in hematopoietic malignancies. Moreover, we found that B23/nucleophosmin binds SENP3 and SENP5 in Xenopus laevis egg extracts and that it is essential for stable accumulation of SENP3 and SENP5 in mammalian tissue culture cells. After either codepletion of SENP3 and SENP5 or depletion of B23/nucleophosmin, we observed accumulation of SUMO proteins within nucleoli. Finally, depletion of these Ulp/SENPs causes defects in ribosome biogenesis reminiscent of phenotypes observed in the absence of B23/nucleophosmin. Together, these results suggest that regulation of SUMO deconjugation may be a major facet of B23/nucleophosmin function in vivo.

scholarly journals Effect of heat shock on ribosome synthesis in Drosophila melanogaster.

1988 ◽  
Vol 8 (1) ◽  
pp. 91-95 ◽  
Author(s):  
J Bell ◽  
L Neilson ◽  
M Pellegrini
Keyword(s):  
Tissue Culture ◽  
Protein Synthesis ◽  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Ribosomal Protein Synthesis ◽  
Correct Processing

In Drosophila tissue culture cells, the synthesis of ribosomal proteins was inhibited by a 1-h 37 degrees C heat shock. Ribosomal protein synthesis was repressed to a greater extent than that of most other proteins synthesized by these cells at 25 degrees C. After a 1-h heat shock, when the cells were returned to 25 degrees C, the ribosomal proteins were much slower than most other 25 degrees C proteins to return to pre-heat shock levels of synthesis. Relative to one another, all the ribosomal proteins were inhibited and later recovered to normal levels of synthesis at the same rate and to the same extent. Unlike the ribosomal proteins, the precursor to the large rRNAs was continually synthesized during heat shock, although at a slightly reduced level, but was not processed. It was rapidly degraded, with a half-life of approximately 16 min. Pre-heat shock levels of synthesis, stability, and correct processing were restored only when ribosomal protein synthesis returned to at least 50% of that seen in non-heat-shocked cells.

Sign in / Sign up

Export Citation Format

Share Document