Cold-induced decrease of K+ conductance and its inhibition by a calmodulin antagonist, W-7, in Paramecium tetraurelia.
نویسندگان
چکیده
Under voltage clamp, Paramecium tetraurelia was used to examine the cold-induced inward current and its inhibition by a calmodulin antagonist, W-7 [N-(6 aminohexyl)-5-chloro-1-naphthalenesulphonamide]. Cooling of the cell caused an inward current. The amplitude of the current was increased as the membrane potential was made more positive than the resting potential, and it was significantly blocked by using CsCl-filled electrodes and tetraethylammonium in the bath solution, suggesting that the current was accompanied mainly by a decrease in K+ conductance. The cold-induced inward current was reversibly inhibited by the external application of W-7 in a concentration-dependent manner. EGTA-microinjection into the cell also reduced the current. These results indicate that the decrease in K+ conductance induced by cooling is Ca(2+)-dependent and is inhibited by W-7.
منابع مشابه
Defect of cold-sensitive response in calmodulin mutants of Paramecium and the restoration by cyclic nucleotide.
Wild type and calmodulin mutants (cam) of Paramecium tetraurelia were examined for cold-sensitive responses. Among mutants tested, cam12 and cam13 mutants, which have substitutions in N-terminal lobe of calmodulin molecule, reduced both responses in the swimming and the membrane potential. Under voltage clamp conditions, the cooling stimulus to the wild type cell induced a transient inward curr...
متن کاملCa-induced K+-outward current in Paramecium tetraurelia.
Late K-outward currents upon membrane depolarization were recorded in Paramecium tetraurelia under a voltage clamp. A Ca-induced K-outward component is demonstrated by subtracting the value of the outward current in a pawn A mutant lacking functional Ca-channels (pwA500). The Ca-induced K-outward current activates slowly, reaching a peak after 100 to 1000 ms. The current then remains steady or ...
متن کاملANTICALMODULIN DRUGS DUE TO THE NET EFFECTS CANNOT ANTAGONIZE DIBUTYRYL-CAMP-MEDIATED SUPPRESSION OF DE NOVO SYNTHESIZED LIPID SECRETION IN BOTH CULTURED MCARDLE CELLS AND RAT HEPATOCYTES
The effects and interaction between cAMP-analogue dibutyryl-cAMP and calmodulin antagonists were investigated on de novo synthesis and secretion of lipids in cultures of hepatoma McArdle-RH7777 cells and normal rat hepatocytes. Dibutyryl cAMP caused a significant decrease in the secretion of de novo synthesized triacyl [3H] glycerol in both cultures of McArdle cells and rat hepatocytes. The ...
متن کاملPresence and indirect immunofluorescent localization of calmodulin in Paramecium tetraurelia
In this paper we demonstrate the presence and localization of calmodulin, a calcium-dependent regulatory protein, in the ciliated protozoan Paramecium tetraurelia. Calmodulin is demonstrated by several criteria: (a) the ability of whole cell Paramecium extracts to stimulate mammalian phosphodiesterase activity, (b) the presence of an acidic, thermostable, 17,000-dalton polypeptide whose mobilit...
متن کاملSubplasmalemmal Ca-stores in Paramecium tetraurelia : Iientification and characterisation of a sarco(endo)plasmic reticulum-like Ca2+-ATPase by phosphoenzyme intermediate formation and its inhibition by caffeine
Considering increasing interest in calcium stores in protozoa, including parasitic forms, and specifically in subplasmalemmal stores in higher eukaryotes, we have isolated subplasmalemmal calcium stores (alveolar sacs) from the ciliated protozoan, Paramecium tetraurelia. Using antibodies against established sarco(endo)plasmic reticulum Caz+-ATPases (SERCAs) we detected in Western blots of subce...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Cell structure and function
دوره 22 6 شماره
صفحات -
تاریخ انتشار 1997