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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 309 (1979), S. 179-190 
    ISSN: 1432-1912
    Keywords: Antiarrhythmic drug ; Procainamide ; Cardiac transmembrane action potential ; $$\dot V_{\max }$$ membrane potential relationship ; Reactivation of $$\dot V_{\max }$$
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Effects of procainamide (PA), 0.18, 0.37 and 0.74 mmol/l, on the transmembrane potential were studied in isolated guinea-pig papillary muscles, superfused with modified Tyrode's solution (external K concentration, [K]o=5.4 mmol/l) at the basic driving rate of 1 Hz. PA, at 0.37 mmol/l, significantly reduced the maximum rate of rise of action potential ( $$\dot V_{\max }$$ ) with no change in the resting potential. When 2.7 mmol/l [K]o of the superfusate was exchanged for 15 mmol/l [K]o solution a decrease in $$\dot V_{\max }$$ induced by 0.37 mmol/l PA became more prominent with decrease in resting potential. The reduction of $$\dot V_{\max }$$ at steady state was less at lower driving rates (0.25 and 0.5 Hz) and more at higher driving rates (2–5 Hz) than at 1 Hz in 2.7, 5.4 and 10.0 mmol/l [K]o solution. Such changes were enhanced concentration-dependently by PA at 5.4 mmol/l [K]o. Also, the changes became more significant with an increase in [K]o from 2.7 mmol/l to 5.4 mmol/l and then to 10.0 mmol/l. The recovery process of $$\dot V_{\max }$$ proceeded with two components. The time course of the slow component seen in the $$\dot V_{\max }$$ of the first response after interruption of basic driving stimulation at 1 Hz, followed an approximate monoexponential function. The time constants were 6.3, 4.4 and 5.8 s in the presence of 0.18, 0.37 and 0.74 mmol/l PA at 5.4 mmol/l [K]o and 3.4 and 3.7 s both in the presence of 0.37 mmol/l PA at 2.7 and 10.0 mmol/l [K]o. $$\dot V_{\max }$$ values after 30 or 60 s interruption of stimulation were 80–92% of the predrug $$\dot V_{\max }$$ value at 1 Hz. The time constants of the first component, estimated by the peeling-off methods at the driving rate of 0.1 Hz, were 11, 31 and 5–22 ms in the presence of 0.37 mmol/l at 5.4, 10.0 and 2.7 mmol/l [K]o and did not differ significantly from the time constants in control preparations. The results were found to be consistent, to a certain extent, with the model proposed by Hondeghem and Katzung (1977).
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0878
    Keywords: Caldesmon ; Actin ; Immunocytochemistry ; Small intestine ; Smooth muscle ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The distribution of caldesmon (a calmodulin-binding, F-actin-interacting protein) (Sobue et al. 1982) and of actin was studied in the rat's small intestine by means of light-microscopic immunocytochemistry. Positive immunostaining for caldesmon was seen in smooth muscle cells of the intestinal wall, and of blood vessels, and in the apical portion of the absorptive epithelial cells. The immunoreactivity in goblet cells was difficult to recognize. The positive reaction to immunostaining for actin showed almost the same pattern as that for caldesmon. These results suggest that this calmodulin-binding protein may play an important role in the control of actin-myosin interaction in smooth muscle cells and in non-muscle cells.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0878
    Keywords: Thyroid ; Immunocytochemistry ; Caldesmon ; Actin ; Endocytosis ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The distribution of caldesmon (a calmodulin-binding, F-actin interacting protein; Sobue et al. 1982) and actin was studied in the rat thyroid gland by means of light-microscopic immunocytochemistry, and the fine-structural distribution of actin filaments was examined by use of heavy meromyosin (HMM). Caldesmon and actin were demonstrated in the apical cytoplasm of almost all the follicle epithelial cells in normal as well as TSH-treated animals. Immunoreactivities for both caldesmon and actin showed almost the same pattern in localization. The smooth muscle cells of the blood vessels were also positive for caldesmon and actin. By electron microscopy, numerous actin filaments decorated by HMM and running perpendicularly or randomly to the apical surface were recognized in the apical cytoplasm of the follicle epithelial cell. These results suggest that caldesmon and actin, in conjugation with calmodulin, play a role in the regulation of cellular activity such as exocytosis and endocytosis in the apical portion of the follicle epithelial cell.
    Type of Medium: Electronic Resource
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