1-5-bis(2-methoxy-4-nitro-5-sulfophenyl)-3-((phenylamino)carbonyl)formazan and Prostatic-Neoplasms

1-5-bis(2-methoxy-4-nitro-5-sulfophenyl)-3-((phenylamino)carbonyl)formazan has been researched along with Prostatic-Neoplasms* in 3 studies

Other Studies

3 other study(ies) available for 1-5-bis(2-methoxy-4-nitro-5-sulfophenyl)-3-((phenylamino)carbonyl)formazan and Prostatic-Neoplasms

ArticleYear
ErbB-4 may control behavior of prostate cancer cells and serve as a target for molecular therapy.
    The Prostate, 2007, Jun-01, Volume: 67, Issue:8

    To assess ErbB-4 expression in advanced human prostate cancer (PC) cell lines, the role of ErbB-4 in motility, migration, and proliferative/tumorigenic potential of PC cells, and efficacy of anti-ErbB-4 monoclonal antibody (Mab) treatment on PC cells in vitro and tumor growth in vivo.. Established advanced human PC cell lines (PC-3, Cl-1, and Du-145) were evaluated for ErbB-4 expression. Several Cl-1 cell line clones expressing various levels of ErbB-4 were isolated, their motility, migration capacity, and in vitro proliferation as well as survival following Mab treatment were evaluated. Tumorigenicity and proliferation capacity of these clones in vivo and efficacy of Mab treatment on tumor growth were estimated by measurements of subcutaneous tumors developed in nude mice.. PC cell lines studied express ErbB-4. Both PC-3 and Du-145 cell lines express high ErbB-4 levels; only 50% of Cl-1 cells express ErbB-4 with large heterogeneity. Cl-1 sub-clones highly expressing ErbB-4 showed increased cell motility, migration, and proliferation rate in vitro and enhanced growth in vivo, compared to clones with low ErbB-4 expression. Mab treatment inhibited the growth of cells expressing high but not low ErbB-4 levels in vitro and decreased the growth of subcutaneous tumors in nude mice generated by ErbB-4 highly expressing cells.. High expression of ErbB-4 in prostate cancer Cl-1 cell clones correlated with high proliferative and migration capacity and high tumorigenic potential. The inhibitory effect of Mab on cell proliferation and on subcutaneous tumor growth suggests ErbB-4's potential as a target for molecular anticancer therapy.

    Topics: Animals; Antibodies, Monoclonal; Blotting, Western; Cell Growth Processes; Cell Line, Tumor; Cell Movement; Cell Survival; Female; Formazans; Humans; Immunohistochemistry; Male; Mice; Mice, Nude; Oncogene Proteins v-erbB; Prostatic Neoplasms; Specific Pathogen-Free Organisms

2007
Neuropeptides bombesin and calcitonin inhibit apoptosis-related elemental changes in prostate carcinoma cell lines.
    Cancer, 2002, Jan-15, Volume: 94, Issue:2

    Etoposide-induced apoptosis in prostate carcinoma cells is associated with changes in the elemental content of the cells. The authors previously reported that calcitonin and bombesin inhibited etoposide-induced apoptosis in these cells. In the current study, the authors investigated whether these neuropeptides block the etoposide-induced changes in elemental content.. Cells from the PC-3 and Du 145 prostate carcinoma cell lines were grown either on solid substrates or on thin plastic films on titanium electron microscopy grids, and they were exposed to etoposide for 48 hours in the absence or presence of calcitonin and bombesin. After the exposure, the cells were frozen and freeze dried, and their elemental content was analyzed by energy-dispersive X-ray microanalysis in both in the scanning electron microscope and the scanning transmission electron microscope.. Etoposide treatment consistently induced an increase in the cellular Na concentration and a decrease in the cellular K concentration, resulting in a marked increase of the Na/K ratio and also an increase in the phosphorus:sulphur (P/S) ratio. Both bombesin and calcitonin inhibited the etoposide-induced changes in the cellular Na/K ratio, and calcitonin, but not bombesin, inhibited the changes in the P/S ratio. No significant elemental changes were found with bombesin or calcitonin alone.. The neuropeptides bombesin and calcitonin, which inhibited etoposide-induced apoptosis, also inhibited the etoposide-induced elemental changes in prostate carcinoma cells. This important fact strengthens the link between apoptosis and changes in the intracellular elemental content. This correlation provides an objective basis for the study of neuropeptide target points and may be helpful for alternative therapeutic protocols using neuropeptide inhibitors in the treatment of patients with advanced prostatic carcinoma.

    Topics: Absorptiometry, Photon; Antineoplastic Agents, Phytogenic; Apoptosis; Bombesin; Calcitonin; Calcium; Cell Division; Drug Resistance, Neoplasm; Etoposide; Flow Cytometry; Formazans; Humans; In Situ Nick-End Labeling; Male; Phosphorus; Potassium; Prostatic Neoplasms; Sodium; Sulfur; Tumor Cells, Cultured

2002
A conditionally replicative adenovirus with enhanced infectivity shows improved oncolytic potency.
    Clinical cancer research : an official journal of the American Association for Cancer Research, 2001, Volume: 7, Issue:1

    The absence or the presence of low levels of the Coxsackievirus and adenovirus receptor (CAR) on several tumor types might limit the efficacy of recently proposed tumor-specific or conditionally replicative adenoviruses (CRAds). To address this issue, we used a genetic modification of the fiber knob in the context of an E1A-defective CRAd to allow CAR-independent target cell infection as a means to enhance oncolytic potency. Such infectivity-enhanced CRAd showed higher replication, more efficient infection, and lysis of tumor cells in vitro. Of note, the improved antitumor effect of the fiber-modified CRAd could be demonstrated in vivo. We conclude that the combination of genomic modification to achieve tumor-selective replication and capsid modification to enhance infectivity yields more potent oncolytic adenoviruses for use in cancer treatment.

    Topics: Adenoviridae; Adenovirus E1A Proteins; Animals; Cell Division; Female; Formazans; Genetic Vectors; Humans; Immunologic Tests; In Vitro Techniques; Luciferases; Lung Neoplasms; Male; Mice; Mice, Nude; Oligopeptides; Prostatic Neoplasms; Retinoblastoma Protein; Time Factors; Transplantation, Heterologous; Tumor Cells, Cultured; Virus Replication; Viruses

2001
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