scholarly journals C-Raf-1 Protein Kinase Is Not Essential for Ras Transformation of Mouse Embryo Fibroblasts

2003 ◽  
Vol 2 (1) ◽  
pp. 74-76 ◽  
Author(s):  
Anjali K. Gupta ◽  
Eric Bernhard ◽  
Vincent J. Bakanauskas ◽  
George J. Cerniglia ◽  
Ruth J. Muschel ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Mouse Embryo ◽  
Mouse Embryo Fibroblasts ◽  
Embryo Fibroblasts

scholarly journals 5′-AMP-Activated Protein Kinase (AMPK) Is Induced by Low-Oxygen and Glucose Deprivation Conditions Found in Solid-Tumor Microenvironments

2006 ◽  
Vol 26 (14) ◽  
pp. 5336-5347 ◽  
Author(s):  
Keith R. Laderoute ◽  
Khalid Amin ◽  
Joy M. Calaoagan ◽  
Merrill Knapp ◽  
Theresamai Le ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Mouse Embryo ◽  
Cellular Response ◽  
Null Mouse ◽  
Low Oxygen ◽  
Tumor Microenvironments ◽  
Mouse Embryo Fibroblasts ◽  
Embryo Fibroblasts ◽  
Amp Activated Protein Kinase

ABSTRACT Low oxygen gradients (hypoxia and anoxia) are important determinants of pathological conditions under which the tissue blood supply is deficient or defective, such as in solid tumors. We have been investigating the relationship between the activation of hypoxia-inducible factor 1 (HIF-1), the primary transcriptional regulator of the mammalian response to hypoxia, and 5′-AMP-activated protein kinase (AMPK), another regulatory system important for controlling cellular energy metabolism. In the present study, we used mouse embryo fibroblasts nullizygous for HIF-1α or AMPK expression to show that AMPK is rapidly activated in vitro by both physiological and pathophysiological low-oxygen conditions, independently of HIF-1 activity. These findings imply that HIF-1 and AMPK are components of a concerted cellular response to maintain energy homeostasis in low-oxygen or ischemic-tissue microenvironments. Finally, we used transformed derivatives of wild-type and HIF-1α- or AMPKα-null mouse embryo fibroblasts to determine whether AMPK is activated in vivo. We obtained evidence that AMPK is activated in authentic hypoxic tumor microenvironments and that this activity overlaps with regions of hypoxia detected by a chemical probe. We also showed that AMPK is important for the growth of this tumor model.

scholarly journals Alphavirus Minus-Strand Synthesis and Persistence in Mouse Embryo Fibroblasts Derived from Mice Lacking RNase L and Protein Kinase R

2003 ◽  
Vol 77 (3) ◽  
pp. 1801-1811 ◽  
Author(s):  
Dorothea L. Sawicki ◽  
Robert H. Silverman ◽  
Bryan R. Williams ◽  
Stanley G. Sawicki
Keyword(s):  
Protein Kinase ◽  
Mouse Embryo ◽  
Rnase L ◽  
Minus Strand ◽  
Protein Kinase R ◽  
Persistent Infections ◽  
Mouse Embryo Fibroblasts ◽  
Mosquito Cells ◽  
Embryo Fibroblasts ◽  
Alphavirus Infection

ABSTRACT We report our studies to probe the possible role of the host response to double-stranded RNA in cessation of alphavirus minus-strand synthesis. Mouse embryo fibroblasts (MEF) from Mx1-deficient mice that also lack either the protein kinase R (PKR) or the latent RNase L or both PKR and RNase L were screened. In RNase L-deficient but not wild-type or PKR-deficient MEF, there was continuous synthesis of minus-strand templates and the formation of new replication complexes producing viral plus strands. Inhibiting translation caused minus-strand synthesis to stop and a loss of transcription activity of the mature replication complexes. This turnover of replication complexes that were stable in cells containing RNase L suggested that RNase L plays some role, albeit possibly indirect, in the formation of stable replication complexes during alphavirus infection. In addition, confluent monolayers of RNase L-deficient murine cells readily established persistent infections and were not killed. This phenotype is contrary to what has been observed for infection in vertebrate cells with a presumably functional RNase L gene and more resembled alphavirus replication in Aedes mosquito cells, in which the activity of replication complexes making plus stands was also found to decay with inhibition of translation.

scholarly journals 32 C-RAF-1 protein kinase is not essential for ras transformation in mouse embryo fibroblasts

1999 ◽  
Vol 45 (3) ◽  
pp. 163
Author(s):  
A.K. Gupta ◽  
E.J. Bernhard ◽  
V.J. Bakanauskas ◽  
A. Zimmer ◽  
R.J. Muschel ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Mouse Embryo ◽  
Mouse Embryo Fibroblasts ◽  
Embryo Fibroblasts

scholarly journals Rapamycin-independent IGF2 expression in Tsc2-null mouse embryo fibroblasts and human lymphangioleiomyomatosis cells

PLoS ONE ◽  
2018 ◽  
Vol 13 (5) ◽  
pp. e0197105 ◽  
Author(s):  
Blanca E. Himes ◽  
Kseniya Obraztsova ◽  
Lurong Lian ◽  
Maya Shumyatcher ◽  
Ryan Rue ◽  
...  
Keyword(s):  
Mouse Embryo ◽  
Null Mouse ◽  
Mouse Embryo Fibroblasts ◽  
Embryo Fibroblasts ◽  
Igf2 Expression

Effects of lipopolysaccharide and RU 41740 on prostaglandin production and proliferation of mouse embryo fibroblasts in culture

1984 ◽  
Vol 15 (1-2) ◽  
pp. 66-68
Author(s):  
P. Weinling ◽  
S. Durant ◽  
P. Smets ◽  
R. Zalisz ◽  
D. Duval ◽  
...  
Keyword(s):  
Mouse Embryo ◽  
Prostaglandin Production ◽  
Mouse Embryo Fibroblasts ◽  
Embryo Fibroblasts

SWAP-70 contributes to spontaneous transformation of mouse embryo fibroblasts

2016 ◽  
Vol 345 (2) ◽  
pp. 150-157 ◽  
Author(s):  
Yu-Tzu Chang ◽  
Chung-Li Shu ◽  
Jing-Yang Lai ◽  
Ching-Yu Lin ◽  
Chih-Pin Chuu ◽  
...  
Keyword(s):  
Mouse Embryo ◽  
Spontaneous Transformation ◽  
Mouse Embryo Fibroblasts ◽  
Embryo Fibroblasts

scholarly journals Differential ability of a T-antigen transport-defective mutant of simian virus 40 to transform primary and established rodent cells.

1985 ◽  
Vol 5 (5) ◽  
pp. 1043-1050 ◽  
Author(s):  
R E Lanford ◽  
C Wong ◽  
J S Butel
Keyword(s):  
Cell Lines ◽  
Mouse Embryo ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
T Antigen ◽  
Wild Type ◽  
Mouse Embryo Fibroblasts ◽  
Established Cell Lines ◽  
Established Cell ◽  
Embryo Fibroblasts

The transforming potential and oncogenicity of a simian virus 40 (SV40) mutant affecting T-antigen (T-ag), SV40(cT)-3, was examined in an effort to dissect T-ag functions in transformation. SV40(cT)-3 has a point mutation at nucleotide 4434 that abolishes the transport of T-ag to the nucleus but does not affect its association with the cell surface. Transfection-transformation assays were performed with primary cells and established cell lines of mouse and rat origin. The efficiency of transformation for established cell lines by SV40(cT)-3 was comparable to that of wild-type SV40, indicating that transformation of established cell lines can occur in the absence of detectable amounts of nuclear T-ag. Transformation of primary mouse embryo fibroblasts by SV40(cT)-3 was markedly influenced by culture conditions; the relative transforming frequency was dramatically reduced in assays involving focus formation in low serum concentrations or anchorage-independent growth. Immunofluorescence tests revealed that the transformed mouse embryo fibroblasts partially transport the mutant cT-ag to the cell nucleus. Transformed cell lines induced by SV40(cT)-3 did not differ in growth properties from wild-type transformants. SV40(cT)-3 was completely defective for the transformation of primary baby rat kidney cells, a primary cell type unable to transport the mutant T-ag to the nucleus. The intracellular localization of cellular protein p53 was found to mimic T-ag distribution in all the transformants analyzed. The mutant virus was weakly oncogenic in vivo: the induction of tumors in newborn hamsters by SV40(cT)-3 was reduced in incidence and delayed in appearance in comparison to wild-type SV40. These observations suggest that cellular transformation is regulated by both nuclear and surface-associated forms of SV40 T-ag.

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