Stimulation of Calcium ATPase by Insulin, Glucagon, Cyclic AMP and Cyclic GMP in Triton X-100 Extracts of Purified Rat Liver Plasma Membrane

Hf, Hope-Gill; Nanda,

doi:10.1055/s-0028-1095813

Cited by 28 publications

(4 citation statements)

References 2 publications

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“…1A cGMP Pools and Ca 2ϩ Homeostasisaction is direct or as a result of cGMP-dependent protein kinase. Results from earlier work on the heart (46), on smooth muscle (47,48), and in hepatocytes (49) indicate that cGMP can also stimulate Ca 2ϩ efflux. Whether efflux is stimulated or inhibited may depend on how the cGMP signal is transduced downstream of cGMP synthesis in a particular cell type.…”

Section: Discussionmentioning

confidence: 86%

Activation of the Particulate and Not the Soluble Guanylate Cyclase Leads to the Inhibition of Ca2+ Extrusion through Localized Elevation of cGMP

Zolle

Lawrie²,

Simpson³

2000

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 86%

Activation of the Particulate and Not the Soluble Guanylate Cyclase Leads to the Inhibition of Ca2+ Extrusion through Localized Elevation of cGMP

Zolle

Lawrie²,

Simpson³

2000

Journal of Biological Chemistry

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“…Abnormal (Ca2++Mg2+)-ATPase activity in membranes from non-insulin-dependent diabetic rats has been suggested as contributing to the impaired insulin action seen in these animals [12,13,16]. Liver and kidney cells contain specific insulin receptors [28][29][30][31], (Ca2+ + Mg2+)-ATPase activity [16,32] and are known sites for insulin action [33,34]. Therefore, plasma membranes obtained from these tissues were studied to investigate a possible role of membrane phospholipid in the abnormal activity of (Ca2+ + Mg2+)-ATPase in the diabetic rats.…”

Section: Discussionmentioning

confidence: 99%

Plasma membrane phospholipid content in non-insulin-dependent streptozotocin-diabetic rats — effect of insulin

et al. 1988

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The activity of (Ca 2-+ Mg 2 +)-ATPase is impaired in kidney basolateral membranes from non-insulin-dependent streptozotocin-diabetic rats. To study the possible role of changes in membrane phospholipid content in the malfunction of this enzyme in kidney membranes of the diabetic animals, phospholipid (phosphatidic acid, phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, phosphatidylserine, and sphingomyelin) content was measured in kidney and liver membranes obtained from non-insulin-dependent diabetic rats. Total phospholipid content was similar in liver and kidney membranes of diabetic and control rats (595+47 versus 624+29 in liver and 469+22 versus 458__+ 17 nmol Pi/mg protein in kidney respectively). Phosphatidylethanolamine content in kidney and liver membranes of diabetic rats was lower than in control rats (87.7___ 1.8 versus 96.4 + 2.2 nmol Pi/mg protein, p < 0.01 and 87.1 + 3.7 versus 101.8 + 3.5, p < 0.02 respectively). Phosphatidylinositol content was higher in kidney (28.0+0.6 versus 23.9+2.1, p< 0.02) but not liver membranes from diabetic rats.The in vitro direct effect of insulin on the phospholipid content in kidney membranes was also measured. Physiologic concentrations of insulin (718 pmol/l for 30 min) increased the phosphatidic acid content in membranes from control but not from diabetic rats by 34.2% (p <0.02). This rise was readily measurable after 3 min of exposure to insulin. Insulin did not induce a significant change in the content of any other phospholipid in membranes from control or diabetic rats.These differences in phospholipid content demonstrated in isolated membranes obtained from non-insulin-dependent diabetic and control rats, before and after exposure to insulin, may explain, in part, the impaired function of the (Ca2+ + Mf+)-ATPase observed previously in kidney membranes of the diabetic rats.

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“…The sigmoidal nature of plots of R12 as a function of Q2, and of R32 as a function of Q2 or Q3, may reflect complex kinetics (Vinogradov & Scarpa, 1973;Reed & Bygrave, 1975;Ferreira & Lew, 1976;Black et al, 1981;Famulski & Carafoli, 1982;Muallem & Karlish, 1982) for the interaction of Ca2+ with Ca2+ transporters, including the postulated plasma-membrane (Ca2+ + Mg2+)-dependent ATPase (Garnett & Kemp, 1975;Hope-Gill & Nanda, 1979;Lotersztajn et al, 1981;Iwasa et al, 1982;Kraus-Friedmann et al, 1982), the fact that Q2 and Q3 represent total rather than free Ca +, the presence of more than one type of transporter for the transfer of Ca2+ between two given compartments, and/or the possibility that changes in the structure and properties of the plasma membrane are induced at very low (Kolb & Adam, 1976;Loewenstein, 1981) or very high concentrations of extracellular Ca2+.…”

Section: Kinetics Ofintracellular Ca2+-transportprocessesmentioning

confidence: 99%

A kinetic investigation of the effects of adrenaline on 45Ca2+ exchange in isolated hepatocytes at different Ca2+ concentrations, at 20° C and in the presence of inhibitors of mitochondrial Ca2+ transport

Parker¹,

Barritt²,

Wadsworth³

1983

Biochemical Journal

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The effects of adrenaline on 45Ca2+-exchange curves for isolated hepatocytes incubated under various steady-state conditions were investigated. Kinetic analysis showed that the simplest compartment configuration consistent with each set of data was a series configuration of a three-compartment closed system comprising compartment 1 (C1), the extracellular medium, and two kinetically distinct compartments of cellular exchangeable Ca2+, C2 and C3 (C1 = C2 = C3). Subcellular fractionation of hepatocytes labelled with 45Ca2+ at 0.1 mM-Ca2+ indicated that C3 includes exchangeable Ca2+ in the mitochondria and endoplasmic reticulum. The following results were obtained from experiments conducted at 37 degrees C at five different extracellular Ca2+ concentrations. For both untreated and adrenaline-treated cells, plots of the flux from C1 to C2 as a function of the extracellular Ca2+ concentration were best described by straight lines consistent with Ca2+ influx across the plasma membrane being a diffusion process. Adrenaline increased the value of the permeability constant for Ca2+ influx by 40%. For untreated cells, plots of the flux between C2 and C3 as a function of the concentrations of Ca2+ in these compartments approached a plateau at high Ca2+ concentrations. Adrenaline caused a 3-fold increase in the concentration of Ca2+ that gives half-maximal rate of Ca2+ transport from C2 to C3. At 1.3 mM extracellular Ca2+, a decrease in incubation temperature from 37 degrees C to 20 degrees C decreased the quantity of Ca2+ in C3 and the flux and fractional transfer rates for the transport of Ca2+ between C2 and C3. At 20 degrees C adrenaline increased the quantity of Ca2+ in C3 and the fractional transfer rates for the transfer of Ca2+ from C1 to C2, and from C2 to C3. At 37 degrees C and 2.4 mM extracellular Ca2+, antimycin A plus oligomycin decreased the quantity of Ca2+ in C3 and increased the fractional transfer rate for the transport of Ca2+ from C3 to C2. In the presence of antimycin A and oligomycin, adrenaline did not increase the quantity of Ca2+ in C2 or the flux and fractional transfer rate for the transport of Ca2+ from C1 to C2, whereas these parameters were increased in the absence of the inhibitors.

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Stimulation of Calcium ATPase by Insulin, Glucagon, Cyclic AMP and Cyclic GMP in Triton X-100 Extracts of Purified Rat Liver Plasma Membrane

Cited by 28 publications

References 2 publications

Activation of the Particulate and Not the Soluble Guanylate Cyclase Leads to the Inhibition of Ca2+ Extrusion through Localized Elevation of cGMP

Activation of the Particulate and Not the Soluble Guanylate Cyclase Leads to the Inhibition of Ca2+ Extrusion through Localized Elevation of cGMP

Plasma membrane phospholipid content in non-insulin-dependent streptozotocin-diabetic rats — effect of insulin

A kinetic investigation of the effects of adrenaline on 45Ca2+ exchange in isolated hepatocytes at different Ca2+ concentrations, at 20° C and in the presence of inhibitors of mitochondrial Ca2+ transport

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