Lanthanum Chloride Promoted Proliferation with Enhanced S-phase Entry and Inhibited Potassium Currents of NIH 3T3 Cells

2011 ◽  
Vol 29 (7) ◽  
pp. 1411-1416
Author(s):  
Liping Zhang ◽  
Zhuoyu Li ◽  
Pin Yang
Keyword(s):  
Potassium Currents ◽  
S Phase ◽  
Lanthanum Chloride ◽  
3T3 Cells ◽  
Nih 3T3 ◽  
Phase Entry ◽  
Nih 3T3 Cells

scholarly journals Cellular Ras and Cyclin D1 Are Required during Different Cell Cycle Periods in Cycling NIH 3T3 Cells

1999 ◽  
Vol 19 (7) ◽  
pp. 4623-4632 ◽  
Author(s):  
Masahiro Hitomi ◽  
Dennis W. Stacey
Keyword(s):  
Cell Cycle ◽  
Dna Synthesis ◽  
Cyclin D1 ◽  
Cell Cycle Progression ◽  
Time Lapse ◽  
S Phase ◽  
3T3 Cells ◽  
Cycle Progression ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

ABSTRACT Novel techniques were used to determine when in the cell cycle of proliferating NIH 3T3 cells cellular Ras and cyclin D1 are required. For comparison, in quiescent cells, all four of the inhibitors of cell cycle progression tested (anti-Ras, anti-cyclin D1, serum removal, and cycloheximide) became ineffective at essentially the same point in G1 phase, approximately 4 h prior to the beginning of DNA synthesis. To extend these studies to cycling cells, a time-lapse approach was used to determine the approximate cell cycle position of individual cells in an asynchronous culture at the time of inhibitor treatment and then to determine the effects of the inhibitor upon recipient cells. With this approach, anti-Ras antibody efficiently inhibited entry into S phase only when introduced into cells prior to the preceding mitosis, several hours before the beginning of S phase. Anti-cyclin D1, on the other hand, was an efficient inhibitor when introduced up until just before the initiation of DNA synthesis. Cycloheximide treatment, like anti-cyclin D1 microinjection, was inhibitory throughout G1 phase (which lasts a total of 4 to 5 h in these cells). Finally, serum removal blocked entry into S phase only during the first hour following mitosis. Kinetic analysis and a novel dual-labeling technique were used to confirm the differences in cell cycle requirements for Ras, cyclin D1, and cycloheximide. These studies demonstrate a fundamental difference in mitogenic signal transduction between quiescent and cycling NIH 3T3 cells and reveal a sequence of signaling events required for cell cycle progression in proliferating NIH 3T3 cells.

scholarly journals CtIP Activates Its Own and Cyclin D1 Promoters via the E2F/RB Pathway during G1/S Progression

2006 ◽  
Vol 26 (8) ◽  
pp. 3124-3134 ◽  
Author(s):  
Feng Liu ◽  
Wen-Hwa Lee
Keyword(s):  
Cyclin D1 ◽  
Rna Polymerase Ii ◽  
Cell Cycle Progression ◽  
S Phase ◽  
Mutant Form ◽  
3T3 Cells ◽  
Primary Mouse ◽  
Rb Pathway ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

ABSTRACT Cell cycle progression from G1 to S phase is mainly controlled by E2F transcription factors and RB family proteins. Previously we showed that the presence of CtIP is essential for G1/S transition in primary mouse blastocysts, as well as in NIH 3T3 cells. However, how CtIP executes this function remains to be elucidated. Here we show that in NIH 3T3 cells the expression of CtIP is regulated by the E2F/RB pathway during late G1 and S phases. The presence of wild-type CtIP, but not the E157K mutant form, which failed to interact with RB, enhanced its own promoter activity. Chromatin immunoprecipitation analysis indicated that the recruitment of CtIP to its promoter occurs concomitantly with TFIIB, a component of the RNA polymerase II complex, and with dissociation of RB from the promoter during late G1 and G1/S transition. Similar positive regulation of cyclin D1 expression by CtIP was also observed. Consistently, cells expressing the CtIP(E157K) protein alone exhibited growth retardation, an increase in the G1 population, and a decrease in the S-phase population. Taken together, these results suggest that, contrary to the postulated universal corepressor role, CtIP activates a subset of E2F-responsive promoters by releasing RB-imposed repression and therefore promotes G1/S progression.

scholarly journals S-phase induction and transformation of quiescent NIH 3T3 cells by microinjection of phospholipase C.

1989 ◽  
Vol 86 (10) ◽  
pp. 3659-3663 ◽  
Author(s):  
M. R. Smith ◽  
S. H. Ryu ◽  
P. G. Suh ◽  
S. G. Rhee ◽  
H. F. Kung
Keyword(s):  
Phospholipase C ◽  
S Phase ◽  
3T3 Cells ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

scholarly journals Peptide modulators of Src activity in G1 regulate entry into S phase and proliferation of NIH 3T3 cells

2007 ◽  
Vol 352 (2) ◽  
pp. 423-430 ◽  
Author(s):  
Vidya Mamidipudi ◽  
Laura D. Miller ◽  
Daria Mochly-Rosen ◽  
Christine A. Cartwright
Keyword(s):  
S Phase ◽  
3T3 Cells ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

scholarly journals Requirement of phosphatidylinositol 3-kinase-dependent pathway and Src for Gas6-Axl mitogenic and survival activities in NIH 3T3 fibroblasts.

1997 ◽  
Vol 17 (8) ◽  
pp. 4442-4453 ◽  
Author(s):  
S Goruppi ◽  
E Ruaro ◽  
B Varnum ◽  
C Schneider
Keyword(s):  
Tyrosine Kinase ◽  
Specific Inhibitor ◽  
S Phase ◽  
Phosphatidylinositol 3 Kinase ◽  
3T3 Cells ◽  
Src Tyrosine Kinase ◽  
Survival Effect ◽  
Nih 3T3 ◽  
Nih 3T3 Cells ◽  
Phosphatidylinositol 3

Gas6 is a secreted protein previously identified as the ligand of the Axl receptor tyrosine kinase. We have shown that Gas6 is able to induce cell cycle reentry of serum-starved NIH 3T3 cells and to efficiently prevent apoptosis after complete growth factor removal, a survival effect uncoupled from Gas6-induced mitogenesis. Here we report that the mitogenic effect of Gas6 requires phosphatidylinositol 3-kinase (PI3K) activity since it is abrogated both by the specific inhibitor wortmannin and by overexpression of the dominant negative P13K p85 subunit. Consistently, Gas6 activates the P13K downstream targets S6K and Akt, whose activation is abrogated by addition of wortmannin. Moreover, rapamycin treatment blocks Gas6-induced entry into the S phase of serum-starved NIH 3T3 cells. We also demonstrate the requirement of Src tyrosine kinase for Gas6 signalling since stable or transient expression of a catalytically inactive form of Src significantly inhibited Gas6-stimulated entry into the S phase. Accordingly, Gas6 addition to serum-starved NIH 3T3 cells causes activation of the intrinsic Src kinase activity. When specifically analyzed in a survival assay, these elements were found to be required for the survival effect of Gas6. Taken together, the evidence presented here identifies elements involved in the Gas6 transduction pathway that are responsible for its antiapoptotic effect and suggests that Src is involved in the events regulating cell survival.

scholarly journals A transforming ras gene can provide an essential function ordinarily supplied by an endogenous ras gene.

1986 ◽  
Vol 6 (5) ◽  
pp. 1843-1846 ◽  
Author(s):  
A G Papageorge ◽  
B M Willumsen ◽  
M Johnsen ◽  
H F Kung ◽  
D W Stacey ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
S Phase ◽  
3T3 Cells ◽  
Ras Gene ◽  
Mutant Proteins ◽  
Ras Protein ◽  
Ras Genes ◽  
Essential Function ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

Microinjection of monoclonal antibody Y13-259, which reacts with all known mammalian and yeast ras-encoded proteins, has previously been shown to prevent NIH 3T3 cells from entering the S phase (L. S. Mulcahy, M. R. Smith, and D. W. Stacey, Nature [London] 313:241-243, 1985). We have now found several transformation-competent mutant v-rasH genes whose protein products in transformed NIH 3T3 cells are not immunoprecipitated by this monoclonal antibody. These mutant proteins are, however, precipitated by a different anti-ras antibody. Each of these mutants lacks Met-72 of v-rasH. In contrast to the result for cells transformed by wild-type v-rasH, Y13-259 microinjection of NIH 3T3 cells transformed by these mutant ras genes did not prevent the cells from entering the S phase. These results imply that a transformation-competent ras gene can supply a normal essential function for NIH 3T3 cells. When the proteins encoded by the mutant ras genes were overproduced in Escherichia coli, several mutant proteins that lacked Met-72 failed to bind Y13-259 in a Western blot. However, a ras protein from a mutant lacking amino antibody, but a ras protein from a mutant lacking amino acids 72 to 84 did not. These results suggest that Y13-259 may bind to a higher ordered structure that has been restored in the mutant lacking amino acids 72 to 82.

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