Transient light-induced changes in ion channel and proton pump activities in the plasma membrane of tobacco mesophyll protoplasts

1997 ◽  
Vol 48 (314) ◽  
pp. 1623-1630 ◽  
Author(s):  
M Blom-Zandstra
Keyword(s):  
Plasma Membrane ◽  
Ion Channel ◽  
Proton Pump ◽  
Mesophyll Protoplasts ◽  
Induced Changes

scholarly journals Transient light-induced changes in ion channel and proton pump activities in the plasma membrane of tobacco mesophyll protoplasts

1997 ◽  
Vol 48 (9) ◽  
pp. 1623-1630 ◽  
Author(s):  
Margaretha Blom-Zandstra ◽  
Hans Koot ◽  
Joke van Hattum ◽  
Sake A. Vogelzang
Keyword(s):  
Plasma Membrane ◽  
Ion Channel ◽  
Proton Pump ◽  
Mesophyll Protoplasts ◽  
Induced Changes

Evidence for a plasma membrane proton pump in phloem cells of higher plants.

1991 ◽  
Vol 1 (1) ◽  
pp. 121-128 ◽  
Author(s):  
ND DeWitt ◽  
JF Harper ◽  
MR Sussman
Keyword(s):  
Plasma Membrane ◽  
Proton Pump ◽  
Higher Plants ◽  
Plasma Membrane Proton Pump

ADP-ribose gates the fertilization channel in ascidian oocytes

1998 ◽  
Vol 275 (5) ◽  
pp. C1277-C1283 ◽  
Author(s):  
Martin Wilding ◽  
Gian Luigi Russo ◽  
Anthony Galione ◽  
Marcella Marino ◽  
Brian Dale
Keyword(s):  
Plasma Membrane ◽  
Ion Channel ◽  
Reversal Potential ◽  
Ciona Intestinalis ◽  
Second Messenger ◽  
Tetraacetic Acid ◽  
Independent Manner ◽  
Unitary Conductance ◽  
Intracellular Ca ◽  
Hydrolysis Of

We report an ion channel in the plasma membrane of unfertilized oocytes of the ascidian Ciona intestinalis that is directly gated by the second messenger ADP-ribose. The ion channel is permeable to Ca2+ and Na+ and is characterized by a reversal potential between 0 and +20 mV and a unitary conductance of 140 pS. Preinjection of the Ca2+ chelator 1,2-bis(2-aminophenoxy)ethane- N, N, N′, N′-tetraacetic acid (BAPTA) or antagonists of intracellular Ca2+ release channels into oocytes did not inhibit the ADP-ribose current, demonstrating that the channel is activated in a Ca2+-independent manner. Both the fertilization current and the current induced by the injection of nicotinamide nucleotides are blocked by nicotinamide, suggesting that the ADP-ribose channel is activated at fertilization in a nicotinamide-sensitive manner. These data suggest that ascidian sperm trigger the hydrolysis of nicotinamide nucleotides in the oocyte to ADP-ribose and that this mechanism is responsible for the production of the fertilization current.

IP3 receptor purified from liver plasma membrane is an (1,4,5)IP3 activated and (1,3,4,5)IP4 inhibited calcium permeable ion channel

Cell Calcium ◽  
1995 ◽  
Vol 17 (2) ◽  
pp. 141-153 ◽  
Author(s):  
Martin Mayrleitner ◽  
Rainer Schäfer ◽  
Sidney Fleischer
Keyword(s):  
Plasma Membrane ◽  
Ion Channel ◽  
Ip3 Receptor ◽  
Liver Plasma Membrane

scholarly journals Chronic PKC Activation Inhibits the Repolarizing Cardiac Current by Decreasing the Functional ion Channel Expression at the Plasma Membrane

2011 ◽  
Vol 100 (3) ◽  
pp. 284a
Author(s):  
Kaleef Williams ◽  
Jin O-Uchi ◽  
Angelica Martinez Perez ◽  
Coeli M.B. Lopes
Keyword(s):  
Plasma Membrane ◽  
Ion Channel ◽  
Channel Expression ◽  
Pkc Activation

Impaired alanine uptake by basolateral liver plasma membrane vesicles from rats consuming ethanol

1991 ◽  
Vol 261 (6) ◽  
pp. G913-G920
Author(s):  
D. J. Smith ◽  
S. A. Ploch
Keyword(s):  
Plasma Membrane ◽  
Lipid Composition ◽  
Cholesterol Content ◽  
Ethanol Consumption ◽  
Chronic Ethanol ◽  
Transport Systems ◽  
Liver Plasma Membrane ◽  
Alanine Transport ◽  
Chronic Ethanol Consumption ◽  
Induced Changes

Chronic ethanol consumption reduces alanine transport by rat basolateral liver plasma membrane (blLPM) vesicles; however, the mechanism for this effect remains uncertain. It may be related to the ethanol-induced changes in blLPM fluidity and lipid composition; alternatively ethanol might reduce the number of transporters in the blLPM. To investigate the effect of blLPM fluidity and lipid composition on Na(+)-dependent alanine uptake these parameters were altered in vitro. Increasing the blLPM fluidity had no effect on Na(+)-dependent alanine uptake by blLPM vesicles or the activity of amino acid transport systems, A and ASC. Because ethanol is known to reduce the blLPM cholesterol content, the influence of altering blLPM cholesterol on alanine transport by these membranes was investigated next. Neither an increase nor a decrease of the cholesterol content of the blLPM altered Na(+)-dependent alanine uptake or the activity of system A or ASC. Finally, the influence of chronic ethanol consumption on the specific binding of [3H]alanine to blLPM was studied. The dissociation constant for alanine binding to blLPM from ethanol-fed rats and their pair-fed controls was similar (1.9 +/- 0.2 vs. 2.0 +/- 0.3 mM); however, the maximal binding capacity for alanine was significantly (P less than 0.05) lower in the blLPM from ethanol-fed rats (316 +/- 53 pmol/mg protein) compared with their pair-fed controls (527 +/- 79 pmol/mg protein). These studies do not support the hypothesis that ethanol-induced changes in blLPM fluidity are responsible for the impaired alanine transport; they do suggest that ethanol may reduce the

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