NIH 3T3 cells

LiNASSiER c, PIERRE M, LE PECQ J B and PIERRE J (1990) Mechanism of action in NIH-3T3 cells of genistein, an inhibitor of EGF receptor tyrosine kinase activity. Biochem Pharmacol. 39 (1) 187-93. 

Weitzman, S., Schmeichel, C., Turk, P., Stevens, C., Tolsma, S. and Bouck, N. (1988). Phagocyte-mediated carcinogenesis DNA from phagocyte-transformed C3H lOTl/2 cells can transform NIH/3T3 cells. Ann. N. York Acad. Sci. 551, 103-109. 

Figure 6. The c-mos negative regulatory element (NRE). Nucleotide positions of the NRE are shown relative to the spermatocyte transcription start site, taken as 280 base pairs upstream of the c-mos ATG (see Fig. 4). The endpoints of the NRE are defined by deletions that allow c-mos expression in NIH 3T3 and other somatic cells. Mutations of the sequences designated by boxes 1,2, and 3 also allow c-mos transcription in NIH 3T3 cells, indicating that these sequences represent functional elements within the NRE. Boxes 1 and 2 are similar to sequences upstream of the protamine (Prot) promoter that inhibit in vitro transcription in HeLa cell extracts. A sequence just upstream of box 2 is also similar to a putative repressor-binding site in the regulatory region of Pgk2.

It should be noted that the NRE defined in these experiments is distinct from the previously described c-mos UMS sequence (Blair et al., 1984 Wood et al., 1984). The UMS is located approximately 1.4 kb upstream of the c-mos spermatocyte promoter and was identified because it blocked activation of c-mos transforming potential by insertion of retroviral promoters. It is thought to act as a transcriptional terminator, blocking transcription of c-mos initiated at upstream sequences. However, both the spermatocyte and oocyte transcription initiation sites are substantially downstream of the UMS. Moreover, the presence or absence of the UMS does not affect c-mos expression in either microin-jected oocytes (Pal et al., 1991) or transfected NIH 3T3 cells (Zinkel et al., 1992). It thus appears unlikely that the UMS functions as a negative regulator of c-mos transcription from either the spermatocyte or oocyte promoters in somatic cells. 

Cowley, S., Paterson, H., Kemp, R, and Marshall, C J. 1994. Activation of MAP kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH 3T3 cells. Cell 77 841-52. 

Another important question is whether exocytosis occurs after CNT internalization. Evidence of exocytosis of DNA-coated SWNTs in fibroblast (NIH-3T3) cells was recently presented [148]. The exocytosis rate was close to that of endocytosis after a minor temporary offset, thus keeping the accumulation of SWNTs inside the cell below the cytotoxic levels. 

Single-particle tracking of endocytosis and exocytosis of single-walled carbon nanotubes in NIH-3T3 cells. Nano Letters, 8 (6), 1577-1585. 

Banerjee S, Segal A. 1986. Iruvitro transformation of C3H/10T1/2 and NIH/3T3 cells by acrylonitrile and acrylamide. Cancer Lett 32 293-304. 

Platelet-activating factor is a transcriptional activator of cyclooxygenase-2. PAF induces mouse COX-2-promoter-driven luciferase activity transfected in neuroblastoma cells, such as NG108-15 or SH-SY5Y, and in NIH 3T3 cells (Fig. 33-5). The intracellular PAF antagonist BN 50730 inhibits PAF activation of this construct [41]. 

I. Transfection of Genes Encoding Proteases Enhances Metastasis. Transfection of different cell types with the genes for either uPA or CD confers or enhances the metastatic ability of the recipient cells. This has been shown for uPA in mouse L cells, ras-transformed NIH 3T3 cells, and murine B16 mela-... 

A3. Axelrod, J. H., Reich, R., and Miskin, R., Expression of human recombinant plasminogen activator enhances invasion and experimental metastasis of H-ras-transformed NIH 3T3 cells. Mol. Cell. Biol. 9, 2133-2141 (1989). 

Rong, S., S. Segal, M. Anver, J. H. Resau, and G. F. Vande Woude. 1994. Invasiveness and metastasis of NIH 3T3 cells induced by Met-hepatocyte growth factor/scatter factor autocrine stimulation. Proc Natl Acad Sci USA 91(11) 4731— 5. 

While no in vivo activity has been reported in an Abl-dependent CML model, AZD0530 was active in a xenograft model using Src-transformed NIH 3T3 cells and in an orthotopic model of pancreatic cancer, two Src-dependent models. The results of a Phase I trial in normal volunteers have been disclosed and AZD0530 was tolerated when administered at doses of up to 250 mg [156,157]. While it appears that the initial efficacy trial for AZD0530 will be as an anti-invasive agent for the treatment of metastatic bone disease, this compound probably also has potential for use in CML. 

Acs P, Wang QJ, Bogi K, Marquez AM, Lorenzo PS, Biro T, Szallasi Z, Mushinski JF, Blumberg PM (1997) Both the catalytic and regulatory domains of protein kinase C chimeras modulate the proliferative properties of NIH 3T3 cells. J Biol Chem 272 28793-28799... 

Crespo P, Mischak H, Gutkind JS (1995) Overexpression of mammalian protein Idnase C-zeta does not affect the growth characteristics of NIH 3T3 cells. Bio-chem Biophys Res Commun 213 266-272... 

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