Maitotoxin converts the plasmalemmal Ca pump into a Ca -permeable nonselective cation channel
نویسندگان
چکیده
William G. Sinkins, Mark Estacion, Vikram Prasad, Monu Goel, Gary E. Shull, Diana L. Kunze, and William P. Schilling Department of Physiology and Biophysics, and Neuroscience, and Rammelkamp Center for Education and Research, Case Western Reserve University School of Medicine, Cleveland; and the Department of Molecular Genetics, Biochemistry and Microbiology, University of Cincinnati College of Medicine, Cincinnati, Ohio
منابع مشابه
Maitotoxin converts the plasmalemmal Ca(2+) pump into a Ca(2+)-permeable nonselective cation channel.
Maitotoxin (MTX) activates Ca(2+)-permeable nonselective cation channels and causes a dramatic increase in cytosolic free Ca(2+) concentration ([Ca(2+)](i)) in every cell examined to date, but the molecular identity of the channels involved remains unknown. A clue came from studies of a structurally related marine toxin called palytoxin (PTX). PTX binds to the plasmalemmal Na(+)-K(+)-ATPase (NK...
متن کاملMaitotoxin-induced cell death cascade in bovine aortic endothelial cells: divalent cation specificity and selectivity.
The maitotoxin (MTX)-induced cell death cascade in bovine aortic endothelial cells (BAECs), a model for Ca(2+) overload-induced toxicity, reflects three sequential changes in plasmalemmal permeability. MTX initially activates Ca(2+)-permeable, nonselective cation channels (CaNSC) and causes a massive increase in cytosolic free Ca(2+) concentration ([Ca(2+)](i)). This is followed by the opening ...
متن کاملMaitotoxin activates a nonselective cation channel and a P2Z/P2X7-like cytolytic pore in human skin fibroblasts.
Maitotoxin (MTX), a potent cytolytic agent, activates Ca2+ entry via nonselective cation channels in virtually all types of cells. The identity of the channels involved and the biochemical events leading to cell lysis remain unknown. In the present study, the effect of MTX on plasmalemmal permeability of human skin fibroblasts was examined. MTX produced a time- and concentration-dependent incre...
متن کاملProperties of a store-operated nonselective cation channel in airway smooth muscle.
Passive depletion of internal Ca(2+) stores in airway smooth muscle (ASM) activates nonselective cation channels (NSCCs) that mediate capacitative Ca(2+) entry. However, the single channel properties of these cation channels have yet to be resolved and their regulation by cytosolic Ca(2+) levels ([Ca(2+)](i)) still remains unclear. NSCC currents and changes in [Ca(2+)](i) during passive depleti...
متن کاملIdentification of cyclic GMP-activated nonselective Ca2+-permeable cation channels and associated CNGC5 and CNGC6 genes in Arabidopsis guard cells.
Cytosolic Ca(2+) in guard cells plays an important role in stomatal movement responses to environmental stimuli. These cytosolic Ca(2+) increases result from Ca(2+) influx through Ca(2+)-permeable channels in the plasma membrane and Ca(2+) release from intracellular organelles in guard cells. However, the genes encoding defined plasma membrane Ca(2+)-permeable channel activity remain unknown in...
متن کامل