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I Schulz

Publications and source records attributed to I Schulz.

At least 109 records · Page 6Linked to original sources
PubMed1982

Calcium uptake into acini from rat pancreas: evidence for intracellular ATP-dependent calcium sequestration.

Intracellular ATP-dependent Ca2+-sequestration mechanisms were studied in isolated dispersed rat pancreatic acini following treatment with saponin or digitonin to disrupt their plasma membranes. In the presence of 45Ca2+ concentrations less than 10(-6) mol/liter, addition of 5 mmol/liter ATP caused a rapid increase in 45Ca2+ uptake exceeding the control by fivefold. ADP mimicked the ATP effect by 50 to 60%, whereas other nucleotides such as AMP-PNP, AMP-PCP, CTP, UTP, ITP, GTP, cAMP and cGMP did not. Maximal ATP-promoted Ca2+ uptake was obtained at 10(-5) mol/liter Ca2+. Inhibition of Ca2+ uptake by mitochondrial inhibitors was dependent on the Ca2+ concentration, indicating the presence of different Ca2+ storage systems. Whereas the apparent half-saturation constant found for mitochondrial Ca2+ uptake was approximately 4.5 X 10(-7) mol/liter, in the presence of antimycin and oligomycin (nonmitochondrial uptake) it was approximately 1.4 X 10(-8) mol/liter. In the absence of Mg2+ both ATP- and ADP-promoted Ca2+ uptake was nearly abolished. The Ca2+ ionophore and mersalyl blocked Ca2+ uptake, Electron microscopy showed electron-dense precipitates in the rough endoplasmic reticulum of saponin-treated cells in the presence of Ca2+, oxalate and ATP, which were absent in intact cells and in saponin-cells without ATP or pretreated with A23187. The data suggest the presence of mitochondrial and nonmitochondrial ATP-dependent C2+ storage systems in pancreatic acini. The latter is likely to be located in the rough endoplasmic reticulum.

Adenosine Diphosphate↗
PubMed1981

Analysis of Ca2+ fluxes and Ca2+ pools in pancreatic acini.

45Ca2+ movements have been analysed in dispersed acini prepared from rat pancreas in a quasi-steady state for 45Ca2+. Carbamyl choline (carbachol; Cch) caused a quick 45Ca2+ release that was followed by a slower 45Ca2+ 'reuptake'. Subsequent addition of atropine resulted in a further transient increase in cellular 45Ca2+. The data suggest the presence of a Cch-sensitive 'trigger' pool, which could be refilled by the antagonist, and one or more intracellular 'storage' pools. Intracellular Ca2+ sequestration was studied in isolated acini pretreated with saponin to disrupt their plasma membranes. In the presence of 45Ca2+ (1 microM), addition of ATP at 5 mM caused a rapid increase in 45Ca2+ uptake exceeding the control by fivefold. Maximal ATP-promoted Ca2+ uptake was obtained at 10 microM Ca2+ (half-maximal at 0.32 microM Ca2+). In the presence of mitochondrial inhibitors it was 0.1 microM (half-maximal at 0.014 microM). 45Ca2+ release could still be induced by Cch but the subsequent reuptake was missing. The latter was restored by ATP and atropine caused further 45Ca2+ uptake. Electron microscopy showed electron-dense precipitates in the rough endoplasmic reticulum of saponin-treated cells in the presence of Ca2+, oxalate and ATP which were absent in intact cells or cells pretreated with A23187. The data suggest the presence of a plasma membrane-bound Cch-sensitive 'trigger' Ca2+ pool and ATP-dependent Ca2+ storage systems in mitochondria and rough endoplasmic reticulum of pancreatic acini. It is assumed that Ca2+ is taken up into these pools after secretagogue-induced Ca2+ release.U

Adenosine Triphosphate↗
PubMed1981

Effect of La3+ on secretagogue-induced Ca2+ fluxes in rat isolated pancreatic acinar cells.

Addition of 0.1 mmol/l of La3+ to pancreatic acinar cells increased both the rate and extent of 45Ca+ uptake. Addition of 0.3 mmol/l La3+ did not change cellular 45Ca2+, whereas 1, 2, and 5 mmol/l gradually decreased it. If carbamylcholine (CCh) or the octapeptide of cholecystokinin-pancreozymin (CCK-OP) was added in the presence of low La3+ concentrations (0.1 and 0.3 mmol/l) to 45Ca2+-equilibrated cells, secretagogue-induced 45Ca2+ release-reuptake was not inhibited. At 1 and 2 mol/l of La3+, however, secretagogue-induced 45Ca2+ release was abolished, whereas uptake of 45Ca2+ was still increased by CCK-OP and CCh. At 5 mmol/l La3+, the effects of secretagogues were completely abolished. In the presence of 2 mmol/l La3+, the atropine-induced 45Ca2+ uptake in CCh-pretreated cells and the dibutyryl guanosine 3',5'-cyclic monophosphate-induced 45Ca2+ uptake in CCK-OP-pretreated cells were highly reduced. The data are interpreted to support our assumption that CCK-OP and CCh increase the plasma membrane permeability to Ca2+ in pancreatic acinar cells in addition to their action to initiate release of CA2+ from an intracellular Ca2+ trigger pool.

Animals↗
PubMed1980

Effect of atropine, ouabain, antimycin A, and A23187 on "trigger Ca2+ pool" in exocrine pancreas.

45Ca2+ fluxes have been analyzed in dispersed acinar cells prepared from rat pancreas. Sudden addition of carbamylcholine (CCh) to 45Ca2+-preloaded acinar cells at quasi-steady state for 45Ca2+ resulted in a quick 45Ca2+ release followed by a slower 45Ca2+ reuptake with net accumulation of 45Ca2+. Subsequent sudden addition of atropine caused a further transient increase in cellular 45Ca2+ followed by a slow decrease to a steady-state value. 45Ca2+ release could not be evoked a second time by pancreozymin when prestimulated with CCh. However, if CCh stimulation was abolished by an interposed step of atropine, restimulation by cholecystokinin-pancreozymin was possible. Addition of A23187 or antimycin A to cells induced a fast decrease in cellular 45Ca2+. This effect was not additive to the CCh effect. In ouabain-pretreated cells, the CCh-induced sudden loss of cellular 45Ca2+ was blocked by 60%. The following slow reuptake of 45Ca2+ was blocked completely. Subsequent addition of atropine caused a fast uptake of cellular 45Ca2+ with no secondary decline. The data are consistent with the following model: acetylcholine releases Ca2+ from a cellular "trigger pool" into the cytosol located in or near the cell membrane. Then Ca2+ is extruded from the cell via Ca2+ pumps partly by a Na+-dependent Ca2+ transport system (quick phase of 45Ca2+ release). Subsequently, due to increased Ca2+ permeability of the plasma membrane as induced by acetylcholine, Ca2+ influx occurs and Ca2+ is taken up from the cytosol into intracellular Ca2+ pools (slow 45Ca2+ reuptake phase). Atropine causes refilling of the trigger Ca2+ pool and return of the increased Ca2+ permeability of the plasma membrane back to the unstimulated state.

Amylases↗
PubMed1980

Messenger role of calcium in function of pancreatic acinar cells.

Enzyme secretion from the exocrine pancreas is elicited by a) cholinergic stimulants, b) hormones belonging to the family of pancreozymin, c) some amphibian peptides such as bombesin, eledoisin, and physalaemin, and d) secretin and vasoactive intestinal polypeptide. Whereas the mechanism of the group d hormones in stimulating enzyme secretion involves adenosine 3',5'-cyclic monophosphate, the others seem to use a common pathway involving Ca2+ as intracellular messenger and probably guanosine 3',5'-cyclic monophosphate as modulator of their action. Their effects can be ascribed to two processes. One pathway involves release of Ca2+ from an intracellular store that is most likely located in the plasma membrane. This phase is independent of extracellular Ca2+ and leads to a rise of guanosine 3',5'-cyclic monophosphate. The other pathway is characterized by an increased permeability of the plasma membrane for Ca2+ and is necessary for sustained secretion. Both pathways lead to an increase cytosolic-free Ca2+ concentration. Ca2+ is either directly involved in fusion of zymogen granules with the luminal cell membrane or triggers events that lead to exocytosis. Furthermore, augmented cytosolic-free calcium concentration a) increased the plasma membrane permeability for Na+, Cl-, and K+, which leads to depolarization of the cell, and b) induces uncoupling of neighboring acinar cells.

Animals↗
PubMed1979

Ca2+ control of electrolyte permeability in plasma membrane vesicles from cat pancreas.

The influence of Ca2+ and other cations on electrolyte permeability has been studied in isolated membrane vesicles from cat pancreas. Ca2+ in the micromolar to millimolar concentration range, as well as Mg2+, Sr2+, Mn2+ and La3+ at a tested concentration 10(-4) M, increased Na+ permeability when applied at the vesicle inside. When added to the vesicle outside, however, they decreased Na+ permeability. Ba2+ was effective from the outside but not from the vesicle inside. When Ca2+ was present at both sides of the membrane, Na+ efflux was not affected as compared to that in the absence of Ca2+. Monovalent cations such as Rb+, Cs+, K+, Tris+ and choline+ decreased Na+ permeability when present at the vesicle outside at a concentration range of 10 to 100 mM. Increasing Na+ concentrations from 10 to 100 mM at the vesicle inside increased Na+ permeability. The temperature dependence of Na+ efflux revealed that the activation energy increased in the lower temperature range (0 to 10 degrees C) when Ca2+ was present at the outside or at both sides, but not when present at the vesicle inside only or in the absence of Ca2+. The results suggest that the Ca2+ outside effect is due to binding of calcium to negatively charged phospholipids with a consequent reduction of both fluidity and Na+ permeability of the membrane. The Ca2+-inside effect most likely involves interaction with proteins with consequent increase in Na+ permeability. The data are consistent with current hypotheses on secretagogue-induced fluid secretion in acinar cells of the pancreas according to which secretagogues elicit NaCl and fluid secretion by liberating Ca2+ from cellular membranes and by stimulating Ca2+ influx into the cell. The increased intracellular Ca2+ concentration in turn increases the contraluminal Na+ permeability which leads to NaCl influx. The luminal sodium pump finally transports Na+ ions into the lumen.

Animals↗
PubMed1978

Studies on isolated subcellular components of cat pancreas. III. Alanine-sodium cotransport in isolated plasma membrane vesicles.

Transport of alanine was studied in isolated plasma membrane vesicles from cat pancreas using a rapid filtration technique. The uptake is osmotically sensitive and the kinetics of L-alanine transport are biphasic showing a saturable and a nonsaturable component. The saturable component is seen only when a sodium gradient directed from the medium to the vesicular space is present. Under this condition an overshooting uptake of L-but not of D-alanine occurs. The Na+ gradient stimulated uptake of L-alanine is inhibited by L-serine and L-leucine and stimulated when the membrane vesicles had been preloaded with L-alanine, L-serine or L-leucine. The ionophore monensin inhibits stimulation of uptake caused by a sodium gradient. In the presence of valinomycin or carbonyl cyanide p-trifluoromethoxyphenylhydrazone (CFCCP), the sodium-dependent transport is augmented in vesicles preloaded with K2SO4 or H+ ions (intravesicular pH 5.5), respectively. In the presence of different anions, the Na+-dependent transport is stimulated according to increasing anionic penetration through membrane (lipid solubility). We conclude that a sodium dedpendent electrogenic amino acid transport system is present in pancreatic plasma membranes.

Alanine↗
PubMed1977

Studies on isolated subcellular components of cat pancreas. I. Isolation and enzymatic characterization.

Pancreas of the cat was fractionated into its subcellular components by centrifugation through an exponential ficoll-sucrose density gradient in a zonal rotor. This enables a preparation of four fractions enriched in plasma membranes, endoplasmic reticulum, mitochondria and zymogen granules, respectively. The first fraction, enriched by 9- to 15-fold in the plasma membrane marker enzymes, hormone-stimulated adenylate cyclase, (Na+K+)-ATPase, and 5'-nucleotidase, is contaminated by membranes derived from endoplasmic reticulum but is virtually free from mitochondrial and zymogen-granule contamination. The second fraction from the zonal gradient shows only moderate enrichment of the above marker enzymes but contains a considerable quantity of plasma membrane marker enzymes and represents mostly rough endoplasmic reticulum. The third fraction contains the bulk of mitochondria and the fourth mainly zymogen granules as assessed by electron microscopy and marker enzymes for both mitochondria and zymogen granules, namely succinic dehydrogenase, trypsin and amylase. Further purification of the plasma membrane fractions by differential and sucrose step-gradient centrifugation yields plasma membranes enriched 40-fold in basal and hormone-stimulated adenylate cyclase and (Na+K+)-ATPase.

Adenosine Triphosphatases↗
PubMed1977

Calcium ion uptake induced by cholinergic and alpha-adrenergic stimulation in isolated cells of rat salivary glands.

Adrenaline (10(-5) M) and carbamylcholine (10(-4) M) stimulate 45Ca2+ uptake into isolated cells of rat submandibular galnd and parotid glands. In the presence of the alpha-adrenoreceptor blocking agent phentolamine, adrenaline stimulation of 45Ca2+ uptake is abolished. The beta-adrenergic stimulant isoproterenol has no effect on 45Ca2+ uptake. Carbamylcholine induced 45Ca2+ uptake is inhibited by atropine. The Ca2+ ionophore A23187 stimulates 45Ca2+ uptake, whereas dibutyryl cyclic adenosine 3',5'-monophosphate and dibutyryl cyclic guanosine 3',5'-monophosphate have no effect on 45Ca2+ uptake. A graphical analysis of the 45Ca2+ uptake curves reveals at least two phases: a fast phase and a slow phase, both of which are stimulated by adrenaline and carbamylcholine. The 45Ca-exchangeable pool size is increased by adrenaline and carbamylcholine in both the fast and the slow phases. These results suggest that alpha-adrenergic and cholinergic agonists act by increasing the rate of Ca2+ transfer into the cells of the parotid and submandibular salivary glands most probably through an increase of the cell membrane permeability for Ca2+.

Amylases↗