Literature DB >> 6245166

Membrane currents of pawn mutants of the pwA group in Paramecium tetraurelia.

Y Satow, C Kung.   

Abstract

Membrane currents were recorded from the wild type and two pawn mutants of the pwA complementation group in Paramecium tetraurelia under a voltage clamp. Most currents are not changed by the mutations. Transient inward currents of a leaky mutant, pwA132, upon step depolarizations are less than those in the wild type. The inward transient is completely lacking in a non-leaky mutant, pwA500. The time course of the residual inward currents in the leaky mutant is not significantly different from that of wild type. The voltage sensitivity of the Ca channels in the leaky mutant is also similar to that of wild type. The inward currents upon membrane hyperpolarizations in the mutants show normal characteristics in the presence or absence of external K+. With sufficiently large, prolonged depolarization, outward currents progressively develop in the wild type but decay in the mutants. The simplest conclusion we can draw is that the pwA mutations reduce the number of functional Ca channels but do not change the channel characteristics. From the conductance measurements, 45% of the Ca channels remain in the leaky mutant pwA132, and none remain in the non-leaky mutant pwA500. By subtracting the outward currents of pwA500 from the slow and prolonged outward currents of the wild type, we have tentatively separated a Ca-induced K+ current from the voltage-dependent K+ current. The time courses of these two currents differ by two orders of magnitude.

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Year:  1980        PMID: 6245166     DOI: 10.1242/jeb.84.1.57

Source DB:  PubMed          Journal:  J Exp Biol        ISSN: 0022-0949            Impact factor:   3.312


  16 in total

1.  Purification of a soluble protein controlling ca channel activity in paramecium.

Authors:  N Haga; M Forte; R Ramanathan; Y Saimi; M Takahashi; C Kung
Journal:  Biophys J       Date:  1984-01       Impact factor: 4.033

2.  Electrophysiological evidence suggests a defective Ca2+ control mechanism in a new Paramecium mutant.

Authors:  T C Evans; T Hennessey; D L Nelson
Journal:  J Membr Biol       Date:  1987       Impact factor: 1.843

3.  Possible reduction of surface charge by a mutation in Paramecium tetraurelia.

Authors:  Y Satow; C Kung
Journal:  J Membr Biol       Date:  1981-04-30       Impact factor: 1.843

4.  Calmodulin defects cause the loss of Ca2(+)-dependent K+ currents in two pantophobiac mutants of Paramecium tetraurelia.

Authors:  R R Preston; M A Wallen-Friedman; Y Saimi; C Kung
Journal:  J Membr Biol       Date:  1990-04       Impact factor: 1.843

5.  Isolation and characterization of paramecium mutants defective in their response to magnesium.

Authors:  R R Preston; C Kung
Journal:  Genetics       Date:  1994-07       Impact factor: 4.562

6.  Mutant analysis shows that the Ca2+-induced K+ current shuts off one type of excitation in Paramecium.

Authors:  Y Saimi; R D Hinrichsen; M Forte; C Kung
Journal:  Proc Natl Acad Sci U S A       Date:  1983-08       Impact factor: 11.205

7.  The cloning by complementation of the pawn-A gene in Paramecium.

Authors:  W J Haynes; B Vaillant; R R Preston; Y Saimi; C Kung
Journal:  Genetics       Date:  1998-06       Impact factor: 4.562

8.  Mutational alteration of membrane phospholipid composition and voltage-sensitive ion channel function in paramecium.

Authors:  M Forte; Y Satow; D Nelson; C Kung
Journal:  Proc Natl Acad Sci U S A       Date:  1981-11       Impact factor: 11.205

9.  Veratridine triggers exocytosis in Paramecium cells by activating somatic Ca channels.

Authors:  H Plattner; C Braun; N Klauke; S Länge
Journal:  J Membr Biol       Date:  1994-11       Impact factor: 1.843

10.  Ciliary membrane vesicles of paramecium contain the voltage-sensitive calcium channel.

Authors:  J Thiele; J E Schultz
Journal:  Proc Natl Acad Sci U S A       Date:  1981-06       Impact factor: 11.205

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