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Biomedical subjects

M J Selwyn

Publications and source records attributed to M J Selwyn.

At least 19 recordsLinked to original sources
PubMed1993

Inorganic phosphate is the major component of the thermostable cytoplasmic fraction which stimulates mitochondrial anion uniport.

A low molecular weight thermostable cytoplasmic fraction isolated from rat liver homogenate when pre-incubated with mitochondria increases the rate at which anions enter mitochondria via the pH-dependent anion-conducting channel in the inner membrane. The crude fraction obtained by centrifuging and heating the liver homogenate was purified by gel filtration and chromatography on DEAE-cellulose. The resulting factor is stable to heating at 100 degrees C, freeze-drying and extremes of pH. Inorganic phosphate co-purified with activity and activity was lost when the phosphate was removed by barium salt precipitation. A pure sample of KH2PO4 produced stimulation of anion conductivity. These results show that the major portion of the activity which stimulates anion uniport can be accounted for by the presence of phosphate in the crude and purified fractions. Mersalyl blocks stimulation when added before, but not when added after, incubation with phosphate which shows that the stimulation is produced by phosphate in the mitochondrial matrix. The proposed role of this factor in thyroid hormone action is discussed in the light of its identification as inorganic phosphate.

Animals↗
PubMed1993

The pH-dependent anion-conducting channel of the mitochondrial inner membrane is potently inhibited by zinc ions.

Zinc is a potent reversible inhibitor of the pH-dependent anion-conducting channel in the mitochondrial inner membrane, 50% inhibition was produced by 1.5 microM added Zn2+ at which point free Zn2+ was < or = 10(-8) M. Inhibition by Zn2+ is rapid but can be prevented or rapidly reversed by excess EDTA. Concentrations of Zn2+ higher than 4 microM caused reversal of inhibition to a variable extent depending on the anion. Under these conditions Zn2+ did not inhibit ribose entry, the phosphate transporter, or the pH-insensitive component of the NO3- uniport.

Animals↗
PubMed1993

Effect of buffers and osmolality on anion uniport across the mitochondrial inner membrane.

The effects of buffers and osmolality of the suspending medium on the pH-dependent anion uniport across the inner membrane of isolated rat liver mitochondria have been studied using the light scattering technique to measure passive osmotic swelling. In contrast to some other transport processes the rates of entry of chloride and other anions via the anion-conducting channel decreased steeply with increasing solute concentration. This effect appears to be a result of increased osmolality or decreased matrix volume rather than inhibition by the anion since it was also produced by increasing the osmolality by addition of non-penetrant solutes. The effects of some pH buffers on the mitochondrial anion-conducting channel were also investigated. Some zwitterionic buffers had little effect other than that produced by increasing osmolality but Tricine, Popso and Caps produced marked additional inhibition of anion uniport and several other zwitterionic buffers were also inhibitory. The correlation between increased anion conductivity and increased matrix volume supports the proposal that this channel functions in regulation of the volume of the mitochondrial matrix.

Alkanesulfonates↗
PubMed1993

The high-affinity Ca(2+)-ATPase from rat parotid plasma membranes is an ectoenzyme: solubilization and characterization of the Ca(2+)-ATPase activity.

A high-affinity Ca(2+)-ATPase was solubilized from rat parotid plasma membranes and purified by concanavalin A and DEAE-cellulose chromatography. The properties of the purified high-affinity Ca(2+)-ATPase are very different from those of the parotid plasma membrane ATP-dependent Ca2+ pump but appear to be similar to those of a rat liver cell adhesion protein which exhibits high-affinity ecto-Ca(2+)-ATPase activity.

Animals↗
PubMed1992

An evaluation of exposure time and temperature in the thermocycling of dental restorative materials.

This study indicates that some current procedures used in thermocycling dental restorative materials would not produce the desired thermal gradient in the specimens. The shortfall in gradient depends on the size of the specimen, the dwell time in the baths and whether the baths are stirred or not. The desired thermal gradient of 50 degrees C can be approximated with a dwell time of 60 s in well-circulated water baths at 5 degrees C and 55 degrees C. For critical studies a dwell time of 90 s is recommended.

Dental Materials↗
PubMed1990

Calcium ion activation of the anion-conducting channel in the rat liver mitochondrial inner membrane.

Stimulation of the rat liver mitochondrial inner-membrane anion-conducting channel by aeration is dependent on the concentration of Ca2+ ions in the assay medium. Ca2+ activates anion conduction in both aerated and non-energised mitochondria but acts over a wider concentration range and produces a greater increase in anion-conductivity in aerated mitochondria. EGTA reverses Ca2+ stimulation but takes several seconds to act, indicating slow release of Ca2+ from the activation site possibly on the matrix side of the inner mitochondrial membrane. It is suggested that this channel may respond to hormone-induced changes in cytosolic Ca2+ concentration.

Aerobiosis↗
PubMed1990

Respiratory inhibitors and uncouplers prevent the aeration-induced increase in mitochondrial anion conductivity.

1. When mitochondria are stirred in air the rate of anion conductivity increases, this effect being enhanced by the addition of respiratory substrate. 2. This effect is reversible if the mitochondria are stored for a period of time under N2. 3. The aeration-induced increase in mitochondrial anion conductivity can also be prevented by the addition of respiratory inhibitors rotenone and antimycin A, as well as by 30 microM-cyanide. 4. A decrease in this aeration-induced anion conductivity can also be observed upon the addition of the uncouplers carbonyl cyanide p-(trifluoromethoxy)phenylhydrazone (2 microM) and 2,4-dinitrophenol (100 microM). 5. Simultaneous measurements of mitochondrial anion conductivity and membrane potential show a relationship between the level of membrane potential and anion conductivity. 6. It is suggested that the level of membrane potential is either directly or indirectly responsible for the level of mitochondrial anion conductivity.

Aerobiosis↗
PubMed1988

Palmitoyl-CoA inhibits the mitochondrial inner membrane anion-conducting channel.

Palmitoyl-CoA is shown here to inhibit the pH-dependent anion-conducting channel (IMAC) in the inner membrane of rat liver mitochondria, with half-maximal inhibition at 2.4 microM. It has little effect on the transport of ribose, thiocyanate and glutamate. Palmitic acid and palmitoyl-carnitine stimulate the entry of all the above metabolites. CoASH and carnitine have no effect on chloride uniport. Palmitoyl-CoA and the IMAC may have a role in controlling thermogenesis in liver mitochondria.

Acyl Coenzyme A↗
PubMed1988

Respiration driven C1- uptake by submitochondrial particles.

Both Mg2+ and oligomycin are required for the establishment of a membrane potential and the uptake of Cl- in submitochondrial particles prepared from rat liver. The effect of oligomycin is considered to be due to blocking of H+ conduction through exposed F0 channels of the ATPase complex whereas Mg2+ may more directly affect the anion-conducting channel.

Animals↗
PubMed1982

Inhibition of electrogenic anion entry into rat liver mitochondria by N,N'-dicyclohexylcarbodiimide.

The carboxyl group reagent dicyclohexylcarbodiimide inhibits the electrogenic entry of Cl- and NO3-into rat liver mitochondria at alkaline pH. The inhibition is time dependent and 50% inhibition is obtained by the addition of 3-4 nmol DCCD/mg protein. The blockage of the pH-dependent anion-conducting pore appears to be unrelated to the other known actions of DCCD on rat liver mitochondria but seems similar to its effect on the uncoupling protein of brown adipose tissue.

Animals↗
PubMed1982

Studies on the nature of the high-affinity trialkyltin binding site of rat liver mitochondria.

1. The proteolipid fraction isolated from rat liver mitochondria pretreated with [3H]triphenyltin chloride is enriched in triphenyltin compared with the original mitochondria. 2. Part of this [3H]triphenyltin is eluted with a protein of Mr 5000-6000 on Sephadex LH20 chromatography. 2. Mössbauer spectra of the proteolipid fraction treated with 119Sn-enriched triethyltin chloride show a doublet which corresponds closely with that assigned previously [Farrow & Dawson (1978) Eur. J. Biochem. 86. 85-95] to the absorption of triethyltin bound to the high-affinity binding site of the mitochondrial ATPase.

Animals↗
PubMed1977

Permeability of the mitochondrial membrane to bicarbonate ions.

Osmotic-swelling techniques show that HCO3- enters mitochondria by an electrogenic process, effectively HCO3- uniport, under non-energized conditions. This mode of translocation accounts for previous reports of non-entry of HCO3- in experiments with energy-linked Ca2+ uptake. The effects of HCO3- on mitochondrial respiration are reported and discussed.

Animals↗
PubMed1976

Effects of triphenylsulphonium ions on mitochondria. Inhibition of adenosine triphosphatase activity.

Triphenylsulphonium ions inhibit mitochondrial oxidative phosphorylation and adenosine triphosphatase activity. The site of action is on the soluble F1 adenosine triphosphatase component. Triphenylsylphonium ions also inhibit electron transfer in the NAD-cytochrome b region of the respiratory chain. In both types of inhibition, triphenylsulphonium ions are effective at low concentrations, half-maximal inhibition being produced by a concentration of about 20-30 muM. These effects resemble the effects of alkylguanidines on mitochondria and are discussed in relation to the effects of alkylguanidines and other lipophilic cations such as ethidium and dibenzyldimethylammonium ions. A modification of the purification procedure for the soluble mitochondrial adenosine triphosphatase [Beechey, Hubbard, Linnett, Mitchell & Munn (1975) Biochem. J. 148, 533-537] IS DESCRIBED, WHICH YIELDS A PREPARATION WITH A HIGHER SPECIFIC ACTIVITY AND SHOWING FEWER BANDS IN GEL ELECTROPHORESIS.

Adenosine Triphosphatases↗