What question did this study set out to answer?

To determine how quinine and the neurotoxin apamin affect calcium-dependent potassium permeability across mammalian liver cells and erythrocytes.

August 1, 1981The Journal of PhysiologyOpen Access

Effects of quinine and apamin on the calcium‐dependent potassium permeability of mammalian hepatocytes and red cells.

View Full Paper

Ask AI

Bookmark

Authors

GBGillian M. BurgessUniversité Paris-Sud MCM ClaretUniversité Paris-Sud DJD. H. JenkinsonTrinity College Dublin

Discussion

Member takes

Implication

Laboratory study reveals differential blockade of calcium-activated potassium channels by quinine and apamin in mammalian hepatocytes and erythrocytes, indicating distinct channel subtypes.

Key Points

To determine how quinine and the neurotoxin apamin affect calcium-dependent potassium permeability across mammalian liver cells and erythrocytes.
Monitored extracellular potassium and radioactive tracer fluxes (45Ca and 42K) in isolated hepatocytes and liver slices from guinea-pigs, rabbits, and rats.
Stimulated cells using ATP, noradrenaline, amidephrine, or the divalent cation ionophore A23187 with or without quinine and apamin.
Tested red blood cells and resealed erythrocyte ghosts with apamin (10–1000 nM) and quinine (200–1000 µM) to compare tissue sensitivity.
Quinine (1 mM) and apamin (10 nM) markedly suppressed the rapid loss of potassium (up to 10–25% of cell content) induced by ATP, noradrenaline, or A23187 in guinea-pig and rabbit liver cells without altering calcium movements.
Rat hepatocytes exhibited net potassium uptake rather than potassium loss following stimulation, a response markedly reduced by ouabain.
Quinine inhibited calcium-dependent potassium permeability in red blood cells, whereas apamin exerted no inhibitory effect in intact red blood cells or on either side of erythrocyte ghost membranes.

Cite This Study

Burgess et al. (1981) studied this question.

synapsesocial.com/papers/6a7027763ce530166bc2bf91 https://doi.org/10.1113/jphysiol.1981.sp013814

View Full Paper

Ask AI

Bookmark

August 1, 1981The Journal of PhysiologyOpen Access

Effects of quinine and apamin on the calcium‐dependent potassium permeability of mammalian hepatocytes and red cells.

View Full Paper

Ask AI

Bookmark

Authors

GBGillian M. BurgessUniversité Paris-Sud MCM ClaretUniversité Paris-Sud DJD. H. JenkinsonTrinity College Dublin

Discussion

Member takes

Implication

Laboratory study reveals differential blockade of calcium-activated potassium channels by quinine and apamin in mammalian hepatocytes and erythrocytes, indicating distinct channel subtypes.

Key Points

To determine how quinine and the neurotoxin apamin affect calcium-dependent potassium permeability across mammalian liver cells and erythrocytes.
Monitored extracellular potassium and radioactive tracer fluxes (45Ca and 42K) in isolated hepatocytes and liver slices from guinea-pigs, rabbits, and rats.
Stimulated cells using ATP, noradrenaline, amidephrine, or the divalent cation ionophore A23187 with or without quinine and apamin.
Tested red blood cells and resealed erythrocyte ghosts with apamin (10–1000 nM) and quinine (200–1000 µM) to compare tissue sensitivity.
Quinine (1 mM) and apamin (10 nM) markedly suppressed the rapid loss of potassium (up to 10–25% of cell content) induced by ATP, noradrenaline, or A23187 in guinea-pig and rabbit liver cells without altering calcium movements.
Rat hepatocytes exhibited net potassium uptake rather than potassium loss following stimulation, a response markedly reduced by ouabain.
Quinine inhibited calcium-dependent potassium permeability in red blood cells, whereas apamin exerted no inhibitory effect in intact red blood cells or on either side of erythrocyte ghost membranes.

Cite This Study

Burgess et al. (1981) studied this question.

synapsesocial.com/papers/6a7027763ce530166bc2bf91 https://doi.org/10.1113/jphysiol.1981.sp013814

Also Consider

Synapse has enriched 3 closely related papers on similar clinical questions. Consider them for comparative context:

View Full Paper

Ask AI

Bookmark