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  • Chemotherapy  (1)
  • Exotoxin  (1)
  • Pseudomonas exotoxin  (1)
  • 1990-1994  (3)
  • 1
    ISSN: 1476-5535
    Keywords: Epidermal growth factor ; Exotoxin ; Cancer
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Transforming growth factor-alpha (TGFα)-pseudomonas exotoxin-40 (PE40) is a chimeric protein consisting of an N-terminal TGFα domain fused to a C-terminal 40-kDa segment of the pseudomonas exotoxin A protein. TGFα-PE40 exhibits the receptor binding activity of TGFα and the cell killing activity of PE40. In the current study, we report that a modified TGFα-PE40 derivative significantly prolongs the survival of nude mice bearing tumors derived from cell lines which express the epidermal growth factor receptor (EGFR). In addition, the therapeutic benefit of this protein is mediated by specific binding to the EGF receptor. These results indicate that a therapeutic window exists in vivo for the use of some growth factor-toxin fusion proteins as anticancer agents.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-6881
    Keywords: Chemotherapy ; ATP ; drug transport ; colchicine ; actinomycin D ; doxorubicin ; vinblastine ; vincristine ; introns ; evolution ; P-glycoprotein ; transmembrane domains ; MDR1 gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Multidrug resistance in animal cells is defined as the simultaneous resistance to a variety of compounds which appear to be structurally and mechanistically unrelated. One type of multidrug resistance is characterized by the decreased accumulation of hydrophobic natural product drugs, a phenotype which is mediated by an ATP-dependent integral membrane multidrug transporter termed P-glycoprotein or P170. The gene coding for P170 is calledMDR. The nucleotide-binding domain of P-glycoprotein shares sequence homology with a family of bacterial permease ATP-binding components. In addition, P170 as a whole is structurally very similar to a number of prokaryotic and eukaryotic proteins believed to be involved in transport activities. This review summarizes our current knowledge of the molecular biology and clinical significance ofMDR expression and P-glycoprotein transport activity, as well as some theories about the function of this protein in normal cells.
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  • 3
    ISSN: 1432-1335
    Keywords: Pseudomonas exotoxin ; TGFα ; Rat bladder carcinoma ; Human bladder carcinoma
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A protein formed by fusion of transforming growth factor α withPseudomonas exotoxin (TGFα-PE40) has been shown to have the ability to kill or inhibit the growth of several carcinoma cell lines. This study was designed to evaluate thein vitro cytotoxic effects of TGFα-PE40 on rat and human bladder carcinoma cell lines with different biological potential, and normal rat urothelial cells. The rat cell lines used were D44c, LMC19, and MYU3L, which were established in our laboratory. Human cell lines used were RT4, T24, and 253J. As a normal control, we used the first-passage culture of normal rat bladder urothelium (RU-P1). We examined the number and affinity of epidermal growth factor receptors (EGFR) in these cells, the ability of TGFα-PE40 to bind EGFR, and the cytotoxic effect of TGFα-PE40 and PE40. Rat cell lines, D44c, LMC19, and MYU3L (EGFR=4.9×103–11.4×103/cell) had ED50 values (the concentration of TGFα-PE40 needed to reduce the viable cell population by 50%) of 180 pM, 540 pM and 6000 pM respectively; forc 1 (the concentration required to achieve complete inhibition of growth under continuous serum stimulation) TGFα-PE40 concentrations of 104 pM, 104 pM and higher than 104 pM respectively were required. Human cell lines, RT4, T24, and 253J (EGFR=32×103–126×103/cell) had ED50 values of 20 pM, 66 pM, and 330 pM respectively and T24 showedc 1 values of 103 pM. RU-P1 (EGFR =92.6×103/cell) had the highest ED50 value of 8000 pM. These data indicate that the susceptibility to TGFα-PE40 does not always depend on the number of EGFR, that cells having a relatively small number of EGFR respond well to TGFα-PE40, and that normal urothelial cells are more resistant to TGFα-PE40 than are cancer cells. The differential effect of TGFα-PE40 on normal and neoplastic cells provides a rational basis for its use in vivo to control tumor growth.
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