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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 354 (1996), S. 431-436 
    ISSN: 1432-1912
    Keywords: Key words 2 ; 3-butanedione-monoxime ; Negative ; inotropic effect ; Phosphorylation ; Phosphatase ; Phospholamban ; Inhibitory subunit of troponin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We studied the mechanisms of action of a negative inotropic compound, 2,3-butanedione-monoxime (BDM), which has been suggested to be a cardioprotective agent. In guinea-pig papillary muscles the negative inotropic effect of BDM started at 100 μmol/l amounting to 18.32±2.09% of predrug value at 10 mmol/l without any effects on time parameters (n = 12, each). 30 mmol/l BDM totally abolished force of contraction; this effect was reversible after washout. In the presence of the phosphatase-inhibitor cantharidin (30 μmol/l) the concentration response curve on force of contraction was shifted to higher concentrations of BDM. 100 mmol/l BDM decreased the phosphorylation state of the inhibitory subunit of troponin (TnI) and phospholamban (PLB) in [32P]-labeled guinea-pig ventricular myocytes to 76.5±4.7% and 49.7±4.2%, respectively (n = 7). Furthermore, BDM enhanced the activity of phosphorylase phosphatases in guinea-pig ventricular homogenates amounting to a stimulation to 203.5±10.4% at 100 mmol/l whereas type 1 phosphorylase phosphatase activity increased only by 24.5% (n = 5). PLB phosphatase activity was enhanced to 155.9±11.7% by 100 mmol/l BDM (n = 5). It is concluded that the effects of BDM on contractile parameters are accompanied by decreased phosphorylation of the cardiac regulatory proteins TnI and PLB which could in part be due to activation of type 1 or 2A phosphatase activity. Hence, it is suggested that BDM affects the phosphorylation state of TnI and PLB not directly, but via activation of their phosphatases.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 354 (1996), S. 431-436 
    ISSN: 1432-1912
    Keywords: 2,3-butanedione-monoxime ; Negative inotropic effect ; Phosphorylation ; Phosphatase ; Phospholamban ; Inhibitory subunit of troponin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We studied the mechanisms of action of a negative inotropic compound, 2,3-butanedione-monoxime (BDM), which has been suggested to be a cardioprotective agent. In guinea-pig papillary muscles the negative inotropic effect of BDM started at 100 μmol/l amounting to 18.32±2.09% of predrug value at 10 mmol/l without any effects on time parameters (n = 12, each). 30 mmol/l BDM totally abolished force of contraction; this effect was reversible after washout. In the presence of the phosphatase-inhibitor cantharidin (30 μmol/l) the concentration response curve on force of contraction was shifted to higher concentrations of BDM. 100 mmol/l BDM decreased the phosphorylation state of the inhibitory subunit of troponin (TnI) and phospholamban (PLB) in [32P]-labeled guinea-pig ventricular myocytes to 76.5±4.7% and 49.7±4.2%, respectively (n = 7). Furthermore, BDM enhanced the activity of phosphorylase phosphatases in guinea-pig ventricular homogenates amounting to a stimulation to 203.5±10.4% at 100 mmol/l whereas type 1 phosphorylase phosphatase activity increased only by 24.5% (n = 5). PLB phosphatase activity was enhanced to 155.9±11.7% by 100 mmol/l BDM (n = 5). It is concluded that the effects of BDM on contractile parameters are accompanied by decreased phosphorylation of the cardiac regulatory proteins TnI and PLB which could in part be due to activation of type 1 or 2A phosphatase activity. Hence, it is suggested that BDM affects the phosphorylation state of TnI and PLB not directly, but via activation of their phosphatases.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 3
    ISSN: 1435-1463
    Keywords: Brain banking ; post mortem research ; schizophrenia ; affective disorders ; European consensus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The sophisticated analysis of and growing information on the human brain requires that acquisition, dissection, storage and distribution of rare material are managed in a professional way. In this publication we present the consensus of the European work group 〉European Dementia and Schizophrenia Network〈, granted by the BIOMED I project of the EU, on minimal neuropathological and clinical requirements to include brains of patients with schizophrenia and affective disorders in post mortem studies. The description of clinical prerequisites in different EU countries and institutions is followed by a consensus on tissue handling, a consensus on minimal neuropathological criteria and a consensus on minimal clinical diagnostic criteria including clinical vignette, family, social, educational/professional and general medical histories, general physical history including neurostatus, neurological, psychiatric, medication and general pathological histories, psychostatus, laboratory tests and a history provided by family/health care giver questionaire. This publication should give help to interconnect different European brain bank centers on a basis of standarized protocols.
    Type of Medium: Electronic Resource
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