Effect Of Ethidium On The Morphology, Antiviral Activity And Subcellular-distribution Of Poly R(a-u)
agents; binding; Cell Biology; complex; delivery; dna; double-stranded-rna; human interferon; induction; inhibition; microscopy
Jamison J M; Gilloteaux J J; Adrian M; Summers J L
Cell Biology International
1993
1993-12
Journal Article or Conference Abstract Publication
<a href="http://doi.org/10.1006/cbir.1993.1042" target="_blank" rel="noreferrer noopener">10.1006/cbir.1993.1042</a>
Pertubation of beta1 integrin function using anti-sense or function-blocking antibodies on corneal cells grown on fibronectin and tenascin.
Animals; Antisense/*pharmacology; Cattle; Cell Adhesion; Cell Culture Techniques/*methods; Cells; Chick Embryo; Chickens; Complementary/metabolism; Cornea/*cytology; Cultured; DNA; Dose-Response Relationship; Drug; Fibronectins/*metabolism; Fluorescence; Immunohistochemistry; Integrin beta1/*metabolism/*physiology; Integrins/metabolism; Microscopy; Oligonucleotides; Protein Binding; Retroviridae/genetics; Tenascin/*metabolism
During corneal development, neural crest derivatives from the periocular mesenchyme migrate into the cornea and differentiate into corneal fibroblasts. During this time, these cells interact with a variety of extracellular matrices for proper orientation and development. In the present studies, we have examined the interaction of beta(1) integrins on periocular mesenchyme cells (POM) and corneal fibroblasts (CF) with fibronectin and tenascin by perturbing the function of this integrin. POM and CF attached and spread to a much greater extent on fibronectin than on tenascin. An antibody against beta(1) integrin, CSAT, decreased spreading and attachment, and resulted in a lack of immuno-detectable beta(1) integrin in focal adhesions on fibronectin; few beta(1) positive focal adhesions were observed in cells grown on tenascin. An anti-sense retroviral construct decreased endogenous levels of beta(1) integrin protein, and caused decreased attachment and spreading as well as sparse, disorganized focal adhesions. These data indicate that in vitro, both POM and CF have beta(1) integrins that interact with fibronectin and allow them to attach and spread, while tenascin is anti-adhesive. Further studies using both of these experimental paradigms will clarify whether these interactions also occur in vivo.
Doane Kathleen J; Bhattacharya Raka; Marchant Jeff
Cell biology international
2002
1905-6
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
<a href="http://doi.org/10.1006/cbir.2001.0818" target="_blank" rel="noreferrer noopener">10.1006/cbir.2001.0818</a>
Synergistic antitumour activity of vitamins C and K3 against human prostate carcinoma cell lines.
Adenosine Triphosphate/biosynthesis; Antineoplastic Agents/*pharmacology/toxicity; Antineoplastic Combined Chemotherapy Protocols/pharmacology; Ascorbic Acid/*pharmacology/toxicity; Carcinoma/*metabolism; Catalase/pharmacology; Cultured; DNA; Humans; Hydrogen Peroxide/metabolism; Lipid Peroxidation; Male; Neoplasm Proteins/biosynthesis; Neoplasm/biosynthesis; Prostatic Neoplasms/*metabolism; Sulfhydryl Compounds/analysis; Tumor Cells; Vitamin K/*pharmacology/toxicity
Vitamins C, K3 (VC, VK3) and a VC/VK3 combination with a VC:VK3 ratio of 100:1 were assayed for their antitumour activity against two human prostatic carcinoma cell lines. Co-administration of the vitamins enhanced the antitumour activity 5- to 20-fold even with a 1 h exposure time. While exogenous catalase destroyed the antitumour activity, hydrogen peroxide-induced lipid peroxidation was negligible. Analysis of cellular ATP and thiol levels as well as DNA and protein synthesis revealed: a transient increase in ATP production, a decrease in DNA synthesis, an increase in protein synthesis and a decrease in thiol levels. These results suggested that the increased cytotoxicity of the vitamin combination was due to redox cycling and increased oxidative stress.
Venugopal M; Jamison J M; Gilloteaux J; Koch J A; Summers M; Hoke J; Sowick C; Summers J L
Cell biology international
1996
1996-12
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
<a href="http://doi.org/10.1006/cbir.1996.0102" target="_blank" rel="noreferrer noopener">10.1006/cbir.1996.0102</a>
Subcellular localization and antiviral activity of carminic acid/poly r(A-U) combinations.
Antiviral Agents/*pharmacology; Carmine/*analogs & derivatives/pharmacokinetics/pharmacology; Cell Nucleolus/metabolism; Cells; Chromatin/metabolism; Cultured; Doxorubicin/pharmacology; Drug Combinations; Drug Synergism; Fluorescence; Humans; Interferon-beta/biosynthesis/physiology; Microscopy; Phase-Contrast; Poly A-U/*pharmacokinetics/*pharmacology; Vesicular stomatitis Indiana virus/drug effects/growth & development; Viral Plaque Assay
Carminic acid (CAR) enhances the antiviral activity of poly r(A-U) twelve-fold without increasing interferon induction, inactivating the vesicular stomatitis virus or inducing host cell cytotoxicity. Phase contrast photomicrographs of human foreskin fibroblasts (HSF) incubated with CAR alone, poly r(A-U) alone or with a CAR/poly r(A-U) combination illustrate that the CAR/poly r(A-U) combinations display altered subcellular distribution with the CAR being localized in the nucleoli and chromatin. Phase contrast and fluorescence photomicrographs of adriamycin (ADR)-treated and ADR/poly r(A-U)-treated HSF cells corroborate these findings. These results suggest that modulation of one or more nucleolar processes may be responsible for the enhanced antiviral activity.
Krabill K; Jamison J M; Gilloteaux J; Summers J L
Cell biology international
1993
1993-10
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
<a href="http://doi.org/10.1006/cbir.1993.1014" target="_blank" rel="noreferrer noopener">10.1006/cbir.1993.1014</a>