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  • 1
    ISSN: 0263-6484
    Keywords: Amiodarone neuropathy ; Na-, K-ATPase ; Mg2-ATPase ; rat brain synaptosomes ; p-nitrophenyl phosphatase ; ion transport in CNS ; ATP turnover in CNS ; ouabain binding ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Amiodarone hydrochloride is a diiodinated antiarrhythmic agent widely used in the treatment of cardiac disorders. With the increasing use of amiodarone, several untoward effects have been recognized and neuropathy following amiodarone therapy has recently been reported. The present studies were carried out to study the effect of amiodarone on rat brain synaptosomal ATPase in an effort to understand its mechanism of action. Na+, K+-ATPase and oligomycin sensitive Mg2+ ATPase activities were inhibited by amiodarone in a concentration dependent manner with IC50 values of 50 μM and 10 μM respectively. [3H]ouabain binding was also decreased in a concentration dependent manner with an IC50 value of 12 μM, and 50 μM amiodarone totally inhibited [3H]ouabain binding. Kinetics of [3H]ouabain binding studies revealed that amiodarone inhibition of [3H]ouabain binding is competitive. K+-activated p-nitrophenyl phosphatase activity showed a maximum inhibition of 32 per cent at 200 μM amiodarone. Synaptosomal ATPase activities did not show any change in rats treated with amiodarone (20mg kg-1 day-1) for 6 weeks, when compared to controls. The treatment period may be short, since the reported neurological abnormalities in patients were observed during 3-5 years of treatment. The present results suggest that amiodarone induced neuropathy may be due to its interference with sodium dependent phosphorylation of Na+, K+-ATPase reaction, thereby affecting active ion transport phenomenon and oxidative phosphorylation resulting in low turnover of ATP in the nervous system.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 23 (1989), S. 81-90 
    ISSN: 0021-9304
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: One aim of this in vitro investigation was to determine the effect of substituting four phenols and two methacrylates with vinyl functions on the dentin bond strengths of several new experimental dentin bonding agents. Another objective was to determine the effect of postextraction age and dentin level within the tooth on tensile bond strengths of these toluene diisocyanate-derived adhesives. Extracted third molars were divided into postextraction age groups and sectioned into three slices ∼400 m̈m thick. The four substituted phenols were: eugenol, o-methoxyphenol, o-chlorophenol, and p-cresol. Substituted methacrylates with vinyl ligands were 2-hydroxyethyl methacrylate (HEMA) and 6-hydroxyhexyl methacrylate (HHMA). Results showed that adhesives made with o-chlorophenol, p-cresol, and methoxyphenol with HEMA were the best, while those made with eugenol and HHMA were the worst. The post extraction age of the tooth and the dentin depth had no consistent effect on most adhesive bond strengths which were generally around 10.3 MPa (1500 psi).
    Additional Material: 7 Ill.
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 3 (1985), S. 267-272 
    ISSN: 0263-6484
    Keywords: Plictran ; synaptosomes ; Ca2+ATPase ; calmodulin ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Effect of tricyclohexylhydroxytin (plictran) on Ca2+-ATPase activity was studied in rat brain synaptosomes under in vitro and in vivo conditions. Plictran inhibited basal Ca2+-ATPase activity with an IC50 value of 6 nM suggesting its interaction with calcium transport phenomenon. Plictran inhibited calmodulin (CaM) activated Ca2+-ATPase in a concentration-dependent manner. A complete reversal of calmodulin activation of Ca2+-ATPase was observed with 2-3 nM plictran. A 50 per cent decrease of CaM activated Ca2+-ATPase was observed with 0·5 nM plictran, a concentration at which no significant effect was observed on basel enzyme activity. Of all the brain fractions studied, calmodulin levels in P2 fractions alone were reduced significantly to about 75 per cent of control values in plictran treated rats. The synaptosomal Ca2+-ATPase was also decreased by 35 per cent, 42 per cent and 65 per cent in 10, 20 and 40 mg plictran kg-1 day-1 treated rats for 3 days respectively. The activity levels of Ca2+-ATPase in 10 and 20 mg plictran kg-1day-1 treated rats were restored to normal level by exogenously added calmodulin. These results suggest that plictran may disrupt synaptic function by altering calcium and calmodulin regulated processes in the central nervous system.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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