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MeSH Review

BALB 3T3 Cells

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Disease relevance of BALB 3T3 Cells


High impact information on BALB 3T3 Cells


Chemical compound and disease context of BALB 3T3 Cells


Biological context of BALB 3T3 Cells


Anatomical context of BALB 3T3 Cells


Associations of BALB 3T3 Cells with chemical compounds

  • Both forms of PDGF bind to the transfected receptor, stimulate the receptor tyrosine kinase activity, and elicit a mitogenic response in a manner that was indistinguishable from the responses of Balb/c 3T3 cells to AA and BB forms of PDGF can be attributed to a single type of receptor and show that the AA form, like the BB form, is a true mitogen [25].
  • PRomotion of smooth surface tumorigenicity by phorbol myristate acetate in Balb/3T3 cells and Balb/3T3 T proadipocytes [26].
  • Tertiary amine local anesthetics (dibucaine, tetracaine, procaine) reversibly affect the morphology of untransformed BALB/3T3 cells and the organization of membrane-associated cytoskeletal elements [27].
  • We show that in density-arrested BALB/c 3T3 cells PDGF and PMA induce a rapid, transient, cycloheximide-independent loss of EGF binding activity [28].
  • Tertiary amine local anesthetics facilitated concanavalin A-induced redistribution of lectin receptors on murine BALB/3T3 cells and enhanced the susceptibility of these cells to agglutination by concanavalin A [29].

Gene context of BALB 3T3 Cells

  • In antiproliferative assays, the compound was approximately 30-fold more potent in inhibiting PDGF-mediated growth of v-sis-transformed BALB/c 3T3 cells relative to inhibition of EGF-dependent BALB/Mk cells, interleukin-3-dependent FDC-P1 cells, and the T24 bladder carcinoma line [30].
  • When tested in vivo using highly tumorigenic v-sis- and human c-sis-transformed BALB/c 3T3 cells, CGP 53716 showed antitumor activity at well-tolerated doses [30].
  • The release of functional HB-EGF was assessed by evaluation of its proliferative effects on the HB-EGF-sensitive Balb/c 3T3 cell line [31].
  • However, its expression was down-regulated in quiescent BALB/3T3 cells and was rapidly induced by reintroduction of serum, conditions where PGC-1 was not detected [32].
  • DAB389 GRP did not inhibit protein synthesis in untransfected BALB/3T3 cells [33].

Analytical, diagnostic and therapeutic context of BALB 3T3 Cells


  1. Loss of Fv-1 restriction in Balb/3T3 cells following infection with a single N tropic murine leukemia virus particle. Duran-Troise, G., Bassin, R.H., Rein, A., Gerwin, B.I. Cell (1977) [Pubmed]
  2. Transforming growth factor(s) production enables cells to grow in the absence of serum: an autocrine system. Kaplan, P.L., Anderson, M., Ozanne, B. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  3. Identification of a negative regulatory element that inhibits c-mos transcription in somatic cells. Zinkel, S.S., Pal, S.K., Szeberényi, J., Cooper, G.M. Mol. Cell. Biol. (1992) [Pubmed]
  4. Differential responsiveness of normal and simian virus 40-transformed BALB/c 3T3 cells to retinoic acid: rapid enhancement of epidermal growth factor receptor binding in a simian virus 40-3T3 variant. Chen, J.K., Li, L.W., Mioh, H. Cancer Res. (1987) [Pubmed]
  5. Nickel compounds act through phosphatidylinositol-3-kinase/Akt-dependent, p70(S6k)-independent pathway to induce hypoxia inducible factor transactivation and Cap43 expression in mouse epidermal Cl41 cells. Li, J., Davidson, G., Huang, Y., Jiang, B.H., Shi, X., Costa, M., Huang, C. Cancer Res. (2004) [Pubmed]
  6. Platelet-derived growth factor and double-stranded ribonucleic acids stimulate expression of the same genes in 3T3 cells. Zullo, J.N., Cochran, B.H., Huang, A.S., Stiles, C.D. Cell (1985) [Pubmed]
  7. Anchorage-independent colony formation of SV40 transformed BALB/c-3T3 cells in serum-free medium: role of cell- and serum-derived factors. McClure, D.B. Cell (1983) [Pubmed]
  8. Isolation and characterization of a siderophore-like growth factor from mutants of SV40-transformed cells adapted to picolinic acid. Fernandez-Pol, J.A. Cell (1978) [Pubmed]
  9. Mycoplasmas induce collagenase in BALB/c 3T3 cells. Kluve, B., Merrrick, W.C., Stanbridge, E.J., Gershman, H. Nature (1981) [Pubmed]
  10. Murine immune response to cells transfected with human MUC1: immunization with cellular and synthetic antigens. Apostolopoulos, V., Xing, P.X., McKenzie, I.F. Cancer Res. (1994) [Pubmed]
  11. Involvement of PLAGL2 in activation of iron deficient- and hypoxia-induced gene expression in mouse cell lines. Furukawa, T., Adachi, Y., Fujisawa , J., Kambe, T., Yamaguchi-Iwai, Y., Sasaki, R., Kuwahara, J., Ikehara, S., Tokunaga, R., Taketani, S. Oncogene (2001) [Pubmed]
  12. Heparan sulfates of mouse cells. Analysis of parent and transformed 3T3 cell lines. Underhill, C.B., Keller, J.M. J. Cell. Physiol. (1977) [Pubmed]
  13. Neuromedin B receptor activation causes tyrosine phosphorylation of p125FAK by a phospholipase C independent mechanism which requires p21rho and integrity of the actin cytoskeleton. Tsuda, T., Kusui, T., Jensen, R.T. Biochemistry (1997) [Pubmed]
  14. Characterization of the receptor for cholera toxin and Escherichia coli heat-labile toxin in rabbit intestinal brush borders. Griffiths, S.L., Finkelstein, R.A., Critchley, D.R. Biochem. J. (1986) [Pubmed]
  15. The cytomegalovirus m155 gene product subverts natural killer cell antiviral protection by disruption of H60-NKG2D interactions. Lodoen, M.B., Abenes, G., Umamoto, S., Houchins, J.P., Liu, F., Lanier, L.L. J. Exp. Med. (2004) [Pubmed]
  16. Molecular cloning and expression of the functional gene encoding the M2 subunit of mouse ribonucleotide reductase: a new dominant marker gene. Thelander, M., Thelander, L. EMBO J. (1989) [Pubmed]
  17. Nuclear posttranscriptional processing of thymidine kinase mRNA at the onset of DNA synthesis. Gudas, J.M., Knight, G.B., Pardee, A.B. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  18. Platelet-derived growth factor induces rapid and sustained tyrosine phosphorylation of phospholipase C-gamma in quiescent BALB/c 3T3 cells. Wahl, M.I., Olashaw, N.E., Nishibe, S., Rhee, S.G., Pledger, W.J., Carpenter, G. Mol. Cell. Biol. (1989) [Pubmed]
  19. Autocrine induction of major histocompatibility complex class I antigen expression results from induction of beta interferon in oncogene-transformed BALB/c-3T3 cells. Offermann, M.K., Faller, D.V. Mol. Cell. Biol. (1989) [Pubmed]
  20. Ras mediates the activation of phospholipase D by v-Src. Jiang, H., Lu, Z., Luo, J.Q., Wolfman, A., Foster, D.A. J. Biol. Chem. (1995) [Pubmed]
  21. Progesterone and 17 alpha-hydroxyprogesterone. Novel stimulators of calcium influx in human sperm. Blackmore, P.F., Beebe, S.J., Danforth, D.R., Alexander, N. J. Biol. Chem. (1990) [Pubmed]
  22. Seminal plasma factors that cause large elevations in cellular cyclic GMP are C-type natriuretic peptides. Chrisman, T.D., Schulz, S., Potter, L.R., Garbers, D.L. J. Biol. Chem. (1993) [Pubmed]
  23. Insulin-like growth factor-I stimulates diacylglycerol production via multiple pathways in Balb/c 3T3 cells. Kojima, I., Kitaoka, M., Ogata, E. J. Biol. Chem. (1990) [Pubmed]
  24. Recombinant human betacellulin. Molecular structure, biological activities, and receptor interaction. Watanabe, T., Shintani, A., Nakata, M., Shing, Y., Folkman, J., Igarashi, K., Sasada, R. J. Biol. Chem. (1994) [Pubmed]
  25. A common PDGF receptor is activated by homodimeric A and B forms of PDGF. Escobedo, J.A., Navankasatussas, S., Cousens, L.S., Coughlin, S.R., Bell, G.I., Williams, L.T. Science (1988) [Pubmed]
  26. PRomotion of smooth surface tumorigenicity by phorbol myristate acetate in Balb/3T3 cells and Balb/3T3 T proadipocytes. Scott, R.E., Boone, C.W. J. Natl. Cancer Inst. (1981) [Pubmed]
  27. Effects of local anesthetics on cell morphology and membrane-associated cytoskeletal organization in BALB/3T3 cells. Nicolson, G.L., Smith, J.R., Poste, G. J. Cell Biol. (1976) [Pubmed]
  28. Platelet-derived growth factor modulates epidermal growth factor receptors by a mechanism distinct from that of phorbol esters. Olashaw, N.E., O'Keefe, E.J., Pledger, W.J. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  29. Local anesthetics affect transmembrane cytoskeletal control of mobility and distribution of cell surface receptors. Poste, G., Papahadjopoulos, D., Nicolson, G.L. Proc. Natl. Acad. Sci. U.S.A. (1975) [Pubmed]
  30. Selective inhibition of the platelet-derived growth factor signal transduction pathway by a protein-tyrosine kinase inhibitor of the 2-phenylaminopyrimidine class. Buchdunger, E., Zimmermann, J., Mett, H., Meyer, T., Müller, M., Regenass, U., Lydon, N.B. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  31. Heparin-binding epidermal growth factor-like growth factor/diphtheria toxin receptor expression by acute myeloid leukemia cells. Vinante, F., Rigo, A., Papini, E., Cassatella, M.A., Pizzolo, G. Blood (1999) [Pubmed]
  32. Pgc-1-related coactivator, a novel, serum-inducible coactivator of nuclear respiratory factor 1-dependent transcription in mammalian cells. Andersson, U., Scarpulla, R.C. Mol. Cell. Biol. (2001) [Pubmed]
  33. Inhibition of protein synthesis in small cell lung cancer cells induced by the diphtheria toxin-related fusion protein DAB389 GRP. vanderSpek, J.C., Sutherland, J.A., Zeng, H., Battey, J.F., Jensen, R.T., Murphy, J.R. Cancer Res. (1997) [Pubmed]
  34. The adenovirus E1A protein overrides the requirement for cellular ras in initiating DNA synthesis. Stacey, D.W., Dobrowolski, S.F., Piotrkowski, A., Harter, M.L. EMBO J. (1994) [Pubmed]
  35. Differences in the metabolism of 12-O-[3H]tetradecanoylphorbol-13-acetate and [3H]phorbol-12,13-didecanoate by cells in culture. O'Brien, T.G., Saladik, D. Cancer Res. (1980) [Pubmed]
  36. The design, expression, and characterization of human insulin-like growth factor II (IGF-II) mutants specific for either the IGF-II/cation-independent mannose 6-phosphate receptor or IGF-I receptor. Sakano, K., Enjoh, T., Numata, F., Fujiwara, H., Marumoto, Y., Higashihashi, N., Sato, Y., Perdue, J.F., Fujita-Yamaguchi, Y. J. Biol. Chem. (1991) [Pubmed]
  37. alpha-Actinin and vinculin are PIP2-binding proteins involved in signaling by tyrosine kinase. Fukami, K., Endo, T., Imamura, M., Takenawa, T. J. Biol. Chem. (1994) [Pubmed]
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