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3T3 Cells

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Ronald C Montelaro – One of the best experts on this subject based on the ideXlab platform.

Iris L. Sun – One of the best experts on this subject based on the ideXlab platform.

H. Löw – One of the best experts on this subject based on the ideXlab platform.

  • Bombesin stimulates transplasma-membrane electron transport by Swiss 3T3 Cells
    Biochimica et biophysica acta, 1994
    Co-Authors: Iris L. Sun, Frederick L. Crane, H. Löw
    Abstract:

    Bombesin, a mitogenic neuropeptide, stimulates transplasmalemma reduction of diferric transferrin or ferricyanide by Swiss 3T3 Cells. The stimulation of diferric transferrin reduction occurs in the range of bombesin concentrations that stimulate proliferation of Swiss 3T3 Cells. Diferric transferrin reduction by the 3T3 Cells is accompanied by increased proton release from the Cells and bombesin increases the diferric transferrin-stimulated proton release twofold. Insulin increases the diferric transferrin reductase response and increases growth stimulation with bombesin. The effect of bombesin on the transmembrane electron transport is a new aspect of its effect on the plasma membrane in addition to increase in phosphatidylinositol turnover and protein kinase c activation. The electron transport can provide an independent mechanism of activation of the Na+H+ exchange or it can change the redox state of pyridine nucleotide in the cytoplasm.

  • Modification of transplasma membrane oxidoreduction by SV40 transformation of 3T3 Cells.
    Journal of bioenergetics and biomembranes, 1991
    Co-Authors: H. Löw, Frederick L. Crane, C. Grebing, Monica Isaksson, Annika Lindgren, Iris L. Sun
    Abstract:

    Transformation of 3T3 Cells by SV40 virus changes the properties of the transplasma membrane electron transport activity which can be assayed by reduction of external ferric salts. After 42 h of culture and before the growth rate is maximum, the transformed Cells have a much slower rate of ferric reduction. The change in activity is expressed both by change inKm andVmax for ferricyanide reduction. The change in activity is not based on surface charge effect or on tight coupling to proton release or on intracellular NADH concentration. With transformation by SV40 virus infection the expression of transferrin receptors increases, which correlates with greater diferric transferrin stimulation of the rate of ferric ammonium citrate reduction in transformed SV40-3T3 Cells than in 3T3 Cells.

Baoshan Zhang – One of the best experts on this subject based on the ideXlab platform.

  • replication of equine infectious anemia virus in engineered mouse nih 3T3 Cells
    Journal of Virology, 2009
    Co-Authors: Baoshan Zhang, Ronald C Montelaro
    Abstract:

    We employed the equine lentivirus equine infectious anemia virus (EIAV) to investigate the cellular restrictions for lentivirus replication in murine NIH 3T3 Cells. The results of these studies demonstrate that NIH 3T3 Cells expressing the EIAV receptor ELR1 and equine cyclin T1 supported productive replication of EIAV and produced infectious virions at levels similar to those found in a reference permissive equine cell line. The studies presented here demonstrate, for the first time, differential levels of restriction for EIAV and human immunodeficiency virus type 1 (HIV-1) replication in murine Cells and suggest that these differences can be exploited to reveal critical virus-cell interactions required for HIV-1 assembly and budding of lentivirus particles.

David A. Foster – One of the best experts on this subject based on the ideXlab platform.

  • MARCKS protein is transcriptionally down-regulated in v-Src-transformed BALB/c 3T3 Cells.
    The Journal of biological chemistry, 1992
    Co-Authors: C K Joseph, S A Qureshi, D J Wallace, David A. Foster
    Abstract:

    Abstract Activation of protein kinase C (PKC) by tumor-promoting phorbol esters leads to the phosphorylation of an 80-kilodalton PKC substrate (known as MARCKS) in murine fibroblasts. In BALB/c 3T3 Cells stably transformed by v-Src, phorbol esters were unable to induce phosphorylation of MARCKS. Western blot analysis and in vitro kinase assays showed that both PKC protein levels and kinase activity were unchanged in v-Src-transformed relative to the parental nontransformed BALB/c 3T3 Cells. However, MARCKS protprotein levels were reduced in v-Src-transformed Cells relative to nontransformed Cells. MARCKS RNA levels were also correspondingly reduced in v-Src-transformed Cells. Nuclear “run-on” assays showed decreased transcription of MARCKS in v-Src-transformed Cells. Thus, the absence of MARCKS in v-Src-transformed Cells could be explained by a down-regulation of MARCKS transcription. Inhibiting the protein tyrosine kinase activity of v-Src with herbimycin A restored MARCKS RNA levels, MARCKS transcription, and MARCKS protprotein, suggesting that down-regulation of MARCKS in v-Src-transformed BALB/c 3T3 Cells is a direct effect of v-Src.

  • marcks protein is transcriptionally down regulated in v src transformed balb c 3T3 Cells
    Journal of Biological Chemistry, 1992
    Co-Authors: C K Joseph, S A Qureshi, D J Wallace, David A. Foster
    Abstract:

    Abstract Activation of protein kinase C (PKC) by tumor-promoting phorbol esters leads to the phosphorylation of an 80-kilodalton PKC substrate (known as MARCKS) in murine fibroblasts. In BALB/c 3T3 Cells stably transformed by v-Src, phorbol esters were unable to induce phosphorylation of MARCKS. Western blot analysis and in vitro kinase assays showed that both PKC protein levels and kinase activity were unchanged in v-Src-transformed relative to the parental nontransformed BALB/c 3T3 Cells. However, MARCKS protprotein levels were reduced in v-Src-transformed Cells relative to nontransformed Cells. MARCKS RNA levels were also correspondingly reduced in v-Src-transformed Cells. Nuclear “run-on” assays showed decreased transcription of MARCKS in v-Src-transformed Cells. Thus, the absence of MARCKS in v-Src-transformed Cells could be explained by a down-regulation of MARCKS transcription. Inhibiting the protein tyrosine kinase activity of v-Src with herbimycin A restored MARCKS RNA levels, MARCKS transcription, and MARCKS protprotein, suggesting that down-regulation of MARCKS in v-Src-transformed BALB/c 3T3 Cells is a direct effect of v-Src.