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  • Bifidobacteria  (1)
  • Signal transduction pathways  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Cancer chemotherapy and pharmacology 44 (1999), S. 355-361 
    ISSN: 1432-0843
    Keywords: Keywords Apoptosis ; Antimicrotubule agents ; Bcl-2 phosphorylation ; Protein kinases ; Signal transduction pathways
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Purpose: Microtubules are important cytoskeletal components involved in many cellular events. Antimicrotubule agents including polymerizing agents (paclitaxel and docetaxel) and depolymerizing drugs (vincristine, vinorelbine, and estramustine phosphate) are widely used either alone or in combination with other anticancer drugs. These antimicrotubule agents are promoters of apoptosis in cancer cells. In this review, we discuss the role of bcl-2 family genes in the regulation of apoptosis, and summarize effects of microtubule targeting agents on apoptotic signal transduction pathways. Conclusion: Disruption of microtubule structure by antimicrotubule drugs results in induction of tumor suppressor gene p53 and inhibitor of cyclin-dependent kinases, p21WAF1/CIP1 (p21), and activation/inactivation of several protein kinases including Ras/Raf, PKC/PKA I/II, MAP kinases, and p34cdc2. These protein kinases are associated directly or indirectly with phosphorylation of bcl-2. Phosphorylation of bcl-2 and the elevations of p53 and p21 lead to apoptosis. New pathways of antitumor agents could be directed at this p53, p21 and bcl-2/bax function, and may enhance the effect of existing agents.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-6776
    Keywords: Bifidobacteria ; α-galactosidase ; high-yield production ; melibiose ; raffinose
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Bifidobacteria assimilated raffinose about 4-fold more effectively than other intestinal bacteria, and α-galactosidase was active in all strains of Bifidobacteria tested. The enzyme activity of Bifidobacterium breve grown on raffinose was highly and specifically increased. Its activity was 30-fold higher than that of B. breve grown on glucose. Melibiose was also effective for production of the enzyme. The enzyme was purified to homogeneity from B. breve. It is a homodimer with Mr of about 160 kDa, and its optimum pH for activity of 5.5–6.5. The enzyme showed strict substrate specificity for α-galactoside although it had slight activity for α-glucoside. It hydrolysed stachyose, melibiose (Km = 2 mM) and raffinose (Km = 0.7 mM).
    Type of Medium: Electronic Resource
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