Search PubMed⌕ Search

Biomedical subjects

A C Hall

Publications and source records attributed to A C Hall.

At least 73 records · Page 4Linked to original sources
PubMed1991

KCl cotransport in HbAA and HbSS red cells: activation by intracellular acidity and disappearance during maturation.

Low intracellular pH was shown to be a potent activator of the KCl cotransport system in HbSS red cells, and in reticulocyte-rich fractions of HbAA red cells. Rheological experiments indicated that cell dehydration via the KCl cotransporter in response to low pH decreased the filterability of HbSS red cells. In vitro maturation experiments showed that the KCl cotransport system was rendered cryptic rapidly, in contrast to choline transport, and serine transport via system ASC, which disappeared much more slowly.

Anemia, Sickle Cell↗
PubMed1991

Effects of low ionic strength media on passive human red cell monovalent cation transport.

1. The effect of low ionic strength media on the residual, i.e. (ouabain + bumetanide + Ca2+)-insensitive, K+ influx was characterized in human red blood cells. 2. This K+ flux was enhanced significantly in isotonic solutions of low ionic strength using sucrose to maintain constant osmolarity. This effect was found for fresh red blood cells as well as for stored (bank) red blood cells. However, the absolute magnitude of K+ influx in solutions of low ionic strength was halved for stored red blood cells. 3. Anion replacement of Cl- by CH3SO4- did not affect residual K+ fluxes, showing that Cl- -dependent transport pathways (e.g. the KCl co-transporter) are not involved in the low ionic strength effect. 4. The enhanced K+ influx in low ionic strength media was reversible when the cells were resuspended in a solution of physiological ionic strength. 5. K+ influx measured in light and dense fractions of erythrocytes (separated by centrifugation and corresponding to samples enriched with either 'young' or 'mature' red cells) showed that the low ionic strength effect does not change markedly with cell age. 6. Low ionic strength media elevated residual, i.e. (ouabain + bumetanide + Ca2+)-insensitive, influx of both K+ and Na+ by about the same amount. In both cases the flux was linear with concentration in the range investigated (0.25-10 mM). No significant increase in the uptake of the cations Ca2+ and lysine in low ionic strength solutions could be found. 7. In CH3SO4- -containing solutions of physiological ionic strength the residual K+ influx was almost independent of cell volume, whereas this flux in CH3SO4- -containing solutions of low ionic strength declined as cell volume was increased. 8. K+ flux measurements in solutions of different external pH, where NaCl was replaced by sodium gluconate or sodium glucuronate, showed that the reduced ionic strength is of more importance for the enhanced residual K+ influx than the changed transmembrane potential or the changed intracellular pH. However, a small pH dependence could be found, the K+ flux passing through a minimum around pHi 7.3. 9. Hydrostatic pressure enhanced the residual K+ flux in media of low ionic strength synergistically, so that very large fluxes (greater than 10 mmol (1 cells)-1 h-1) were obtained at 40 MPa. The apparent activation volumes (delta V*) for the pressure-sensitive K+ flux were -108 and -69 ml mol-1 in low ionic strength or physiological ionic strength solutions respectively.(ABSTRACT TRUNCATED AT 400 WORDS)

Biological Transport↗
PubMed1990

Selective inhibitors of KCl cotransport in human red cells.

Two analogues of the loop diuretics furosemide and bumetanide have been identified as differential inhibitors of KCl and NaKCl cotransport systems, assayed by measuring K+ influx in 'young' human red cells. H25 inhibited both NaKCl and KCl cotransport, with I50% values of 0.03 and 30 microM respectively; H74 had no effect on NaKCl cotransport, even at 0.3 mM, but inhibited KCl cotransport with an I50% of 75 microM. These compounds are therefore useful for resolving the two transport systems.

Anemia, Sickle Cell↗
PubMed1990

Factors affecting the activation and inactivation of KCl cotransport in 'young' human red cells.

KCl transport plays an important role in the control of 'young' red cell volume and hence MCHC. The activity of this pathway declines rapidly during maturation in vitro irrespective of whether the transporter is functioning or not. The presence of plasma retards the rate at which the transporter becomes cryptic; N-ethyl maleimide can restore transport activity. Low pH is more effective as an activator of the transporter than hypotonicity, suggesting that protons stimulate the transporter directly rather than via a change in cell volume.

Biological Transport↗
PubMed1989

Potassium transport in monkey erythrocytes.

K transport in Rhesus and Cynomolgus monkey erythrocytes has been characterised and compared to that in human erythrocytes. Transport due to the NaK pump, residual (diffusional) leak, volume-, pressure- and N-ethyl-maleimide-stimulated KCl system and internal Ca2+-stimulated K channel were similar to that in man but in the monkey it differed, in lacking the loop-diuretic-sensitive NaKCl cotransport system.

Animals↗
PubMed1988

Human red cell volume regulation in hypotonic media.

1. There is substantial evidence for a volume-sensitive KCl cotransport system in young human RBC. 2. The KCl cotransport system becomes latent on cell maturation. 3. There is a correlation between the activation of the KCl cotransporter by either pressure, NEM, ghosting or in certain anemias with disc/cup cell shape change. 4. The stretch-activated KCl transporter may be coupled to some component of the cell cytoskeleton.

Animals↗
PubMed1987

Passive potassium transport in human red cells.

The effect of procedures known to stimulate the volume-sensitive KC1 pathway has been studied in human red cells. This system is functional in young, but not mature cells and may mediate large fluxes in individuals with large fractions of reticulocytes. The pathway is apparently latent in mature cells, but may be unmasked by certain procedures suggesting that the transporter is not lost from the membrane during cell maturation.

Biological Transport↗
PubMed1986

Effects of high hydrostatic pressure on 'passive' monovalent cation transport in human red cells.

The effects of high hydrostatic pressure (up to 400 ATA) on the 'passive' (defined as ouabain + bumetanide + EGTA-insensitive) influx and efflux of radiotracer cations (K+ Rb+, Na+, Cs+) has been studied in human red cells suspended at different medium tonicities giving altered cell volumes. Under all conditions studied, cation permeability was raised at pressure, and at least two distinct components were found to comprise this flux. Thus, increasing pressure caused a generalized increase in cation permeability which was unaffected by the anion present, demonstrated linear concentration dependence, and was reduced with cell swelling, and stimulated a specific KCl pathway which was Cl- dependent, demonstrated saturation kinetics with raised [K]0 and was increased with cell swelling. High hydrostatic pressure caused a significant alteration to red cell morphology from the normal biconcave disc to cup-shaped forms and it is proposed that this is associated with the unmasking of the volume-sensitive KCl system.

Biological Transport, Active↗
PubMed1986

The temperature dependence of passive potassium permeability in mammalian erythrocytes.

The effect of temperature on the "passive" permeability of mammalian plasma membranes to K+, measured as the residual flux in the presence of ouabain and bumetanide, was investigated in erythrocytes of several species. Without Ca2+ in the medium, only human red cells demonstrated the "paradoxical" rise in passive flux at low temperature (i.e., below 12 degrees C) seen by other workers. In the other species no such effect was apparent; K+ influx decreased progressively with cooling down to 0 degree C. Below 18.5 degrees C the apparent energy of activation (Ea) was very low--close to that for free diffusion in water--for red cells of all species except human. Above 18.5 degrees C the Ea was much greater and was also more variable amongst the red cells of the species chosen. Neither the inhibitors used nor cell volume changes during incubation accounted for the absence of the paradoxical effect in the species studied here. A rise in permeation of K+ with cooling can, however, be produced by the addition of Ca2+ to the medium, probably by activation of the Ca2+-sensitive K+ channel. This effect would account for previous reports of a paradoxical effect in dog and rat erythrocytes.

Animals↗
PubMed1985

Measurement and stoichiometry of bumetanide-sensitive (2Na:1K:3Cl) cotransport in ferret red cells.

The bumetanide-sensitive uptake of Na+, K+(Rb+) and Cl- has been measured at 21 degrees C in ferret red cells treated with (SITS + DIDS) to minimize anion flux via capnophorin (Band 3). During the time course of the influx experiments tracer uptake was a first-order rate process. At normal levels of external Na+ (150 mM) the bumetanide-sensitive uptake of K+ was dependent on Cl- and represented almost all of the K+ uptake, the residual flux demonstrating linear concentration dependence. The uptake of Na+ and Cl- was only partially inhibited by bumetanide indicating that pathways other than (Na + K + Cl) cotransport participate in these fluxes. The diuretic-sensitive uptake of Na+ or Cl- was, however, abolished by the removal of K+ or the complementary ion indicating that bumetanide-sensitive fluxes of Na+, K+ and Cl- are closely coupled. At very low levels of [Na]o (less than 5 mM) K+ influx demonstrated complex kinetics, and there was evidence of the unmasking of a bumetanide-sensitive Na+-independent K+ transport pathway. The stoichiometry of bumetanide-sensitive tracer uptake was 2Na:1K:3Cl both in cells suspended in a low and a high K+-containing medium. The bumetanide-sensitive flux was markedly reduced by ATP depletion. We conclude that a bumetanide-sensitive cotransport of (2Na:1K:3Cl) occurs as an electroneutral complex across the ferret red cell membrane.

4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid↗
PubMed1984

Differential effects of temperature on three components of passive permeability to potassium in rodent red cells.

The effect of temperature on ouabain-insensitive fluxes of K+ was characterized in red cells from a non-hibernator (guinea-pig) and a hibernator (thirteen-lined ground squirrel). The residual K+ influx which remains in the presence of ouabain and bumetanide, and which is linearly dependent on [K+]o was the same in the erythrocytes of the two species at low temperature (5 degrees C). At 5 degrees C co-transport of K+ was abolished in guinea-pig red cells but was still present in ground squirrel red cells. In guinea-pig cells, ouabain-and-bumetanide-insensitive K+ flux was increased by Ca2+ at low temperatures. This flux was inhibited by quinine and selective for K+ over Na+, indicating activation of the Ca2+-sensitive K+ pathway (Gárdos channel). Ouabain-and-bumetanide-insensitive K+ permeability in red cells from the ground squirrel was insensitive to Ca2+ added to the medium at low temperature. When ground squirrel red cells were depleted of ATP or treated with A23187, Ca2+ induced a flux which was inhibitable by quinine. Hence, ground squirrel red cells possess Gárdos channels. The temperature sensitivity of the K+ channels was assessed using A23187-mediated K+ influx as a measure of Gárdos channel activation. The influence of temperature on the Ca2+-stimulated K+ fluxes under these conditions was indistinguishable between the two species. It is concluded that K+ loss through the Ca2+-sensitive K+ channel is minimal in hibernators' erythrocytes because of more efficient regulation of cytoplasmic Ca2+ during cold storage.

Adenosine Triphosphate↗
PubMed1982

Pressure and temperature effects on human red cell cation transport.

The effects of hydrostatic pressure and temperature on the three components of K+ uptake in human red cells have been investigated, using ouabain and bumetanide to distinguish between the pump, passive diffusion and cotransport. The pressure sensitivity for passive diffusion has been shown to depend on the counter-ion present. The order of this effect, Cl- greater than Br- greater than NO3- greater than I-, is the same as for the ionic partial molal volumes and the Hofmeister series. We have analyzed our experimental results thermodynamically, and propose a model for the activated transition-state complex of the potassium ion which involves the loss of water molecules from the secondary hydration shell, cosphere II.

Anions↗