Eppley Institute for Research in Cancer and Allied Diseases

About: Eppley Institute for Research in Cancer and Allied Diseases is a based out in . It is known for research contribution in the topics: Pancreatic cancer & Cancer. The organization has 965 authors who have published 1396 publications receiving 58994 citations.

Population density alters the responsiveness of GH4C1 pituitary tumor cells to 17β-estradiol

Abstract: In this study we have examined the effect of population density on the ability of 17α-estradiol (E2) to induce PRL mRNA, DNA synthesis, and progesterone receptor in GH4C1 pituitary tumor cells. These parameters were examined at three subconfluent population densities that varied over a 4- fold range. The culture medium was changed daily in these experiments to reduce the possibility of nutrient depletion, medium toxification, or E2 metabolism. At the low population density, a 5-day treatment with E2 at a concentration of 1.0 nM resulted in an 8.1-fold increase in the level of PRL mRNA, as measured by the cytosolic dot blot procedure. At the intermediate density, E2 induced PRL mRNA 2.4-fold. At the high density, the level of PRL mRNA was reduced by 50% in response to 5 days of treatment with E2. The cytosolic dot blot procedure would reflect changes in the level of PRL mRNA per cell as well as changes in the number of cells per culture. Therefore, the level of (8-actin mRNA was also measured, assuming tha...

Changes to crystals of Escherichia coli β-galactosidase during room-temperature/low-temperature cycling and their relation to cryo-annealing

Abstract: Flash-cooling of macromolecular crystals often compromises diffraction quality by increasing the mosaicity. In some cases, cycling the crystal between low temperature (LT) and room temperature (RT) can reverse this increase in mosaicity. Previous studies of RT/LT cycling have focused on the quality of the crystal as it was repeatedly returned to the LT state. Here, crystal quality is explored not only at LT but also when the crystal is returned to RT. The domain model is used to extract information about crystal order from reflection profiles measured from crystals of Escherichia coli β-galactosidase at both temperatures. Despite optimization of the cryocooling protocol, the mosaicity increases by about sixfold with cooling and is anisotropic at both temperatures. The mosaicity increase is the consequence of a decrease in domain volume, an increase in the variation of domain cell dimensions and an increase in the angular spread between domains. Upon rewarming, the mosaicity recovers substantially, including the somewhat surprising recovery of domain volume, but incompletely. Over multiple RT/LT cycles disorder in both states increases, which appears to mainly arise from radiation damage, although a contribution from cool–thaw processes cannot be ruled out. The analysis further suggests that LT disorder is governed by variability inherent in the cooling process combined with the overall history of the crystal. In contrast, RT disorder appears to be governed principally by the overall history of the crystal. This suggests that with these particular crystals under the experimental conditions used, particularly at high-intensity synchrotron X-ray sources, RT/LT cycling annealing protocols should involve few cycles so as to limit the hysteresis in both temperature states while taking advantage of the inherent variability in the cooling process that may result in improved crystal order at LT.

Bacterial mutagenicity of extracts of the baked and raw Agaricus bisporus mushroom.

Abstract: Aqueous extracts of baked and raw Agaricus bisporus (AB) mushroom were tested for mutagenic activity in Salmonella typhimurium strains TA1535 and TA1537. The extracts were studied with and without metabolic activation by Aroclor-induced rat liver S9 mix. The extracts of the baked and raw AB exhibited a dose related mutagenic activity with and without activation in strain TA1535. Similar findings were obtained in strain TA1537, although the net revertant values were of lower magnitude. Because humans mainly consume the cultivated mushroom AB in baked form, the implications of the findings are self-evident.

CTDP1 regulates breast cancer survival and DNA repair through BRCT-specific interactions with FANCI.

Abstract: BRCA1 C-terminal domains are found in a specialized group of 23 proteins that function in the DNA damage response to protect genomic integrity. C-terminal domain phosphatase 1 (CTDP1) is the only phosphatase with a BRCA1 C-terminal domain in the human proteome, yet direct participation in the DNA damage response has not been reported. Examination of the CTDP1 BRCA1 C-terminal domain-specific protein interaction network revealed 103 high confidence interactions enriched in DNA damage response proteins, including FANCA and FANCI that are central to the Fanconi anemia DNA repair pathway necessary for the resolution of DNA interstrand crosslink damage. CTDP1 expression promotes DNA damage-induced FANCA and FANCD2 foci formation and enhances homologous recombination repair efficiency. CTDP1 was found to regulate multiple aspects of FANCI activity, including chromatin localization, interaction with γ-H2AX, and SQ motif phosphorylations. Knockdown of CTDP1 increases MCF-10A sensitivity to DNA interstrand crosslinks and double-strand breaks, but not ultraviolet radiation. In addition, CTDP1 knockdown impairs in vitro and in vivo growth of breast cancer cell lines. These results elucidate the molecular functions of CTDP1 in Fanconi anemia interstrand crosslink repair and identify this protein as a potential target for breast cancer therapy.