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C Schudt

Publications and source records attributed to C Schudt.

68 records · Page 4Linked to original sources
PubMed1979

Regulation of glycogen synthesis in rat-hepatocyte cultures by glucose, insulin and glucocorticoids.

The changes in glycogen content and in its rate of synthesis in two-day-old primary cultures of rat hepatocytes were assessed under various conditions. Hepatocytes cultivated in serum-free and hormone-free medium switch from glycogen degradation to glycogen deposition at 10.3 mM glucose. After pretreatment of the cells with glucocorticoids this threshold was reduced, in the absence or presence of insulin, to 5.4 or 1.2 mM glucose, respectively. The rate of glycogen synthesis in the presence of 10 mM glucose was amplified from 5 nmol x h-1 x mg protein-1 to 20 nmol glucose x h-1 x mg protein-1 after pretreatment with triamcinolone. Glucagon pretreatment also significantly increased the subsequent glycogen synthesis rate. Insulin addition accelerated glycogen synthesis about twofold regardless of the pretreatment. The dose-response relationship between insulin concentration and glycogen synthesis rate showed half-maximal effect at 0.62 +/- 0.22 nM (mean +/- S.D.) insulin. Pretreatment of hepatocytes with glucocorticoids, glucagon, insulin or combinations of these hormones did not significantly change the concentration which gives the half-maximal effect.

Animals↗
PubMed1979

Hormonal regulation of glucokinase in primary cultures of rat hepatocytes.

Glucokinase activity in rat hepatocyte cultures declined with a half-time, t1/2, of 32 h during 3 days under serum-free conditions. Addition of insulin and triamcinolone to the culture medium prevented this decay. Glucokinase levels in hepatocytes derived from fasted rats could be elevated from 7.4 to 16.4 mU/mg protein in the presence of insulin and triamcinolone. In 2-day-old cultures glucokinase was induced in the presence of both hormones with a half time, t1/2, of 5.1 h. In cultures treated for 2 days with triamcinolone, insulin induced a 80% increase of glucokinase even in the absence of glucocorticoids. Insulin induction was dependent on protein synthesis but occurred in the absence of RNA synthesis. Glucocorticoid action, however, depended on RNA synthesis suggesting that glucocorticoids control transcription. Insulin evoked half-maximal effects at 3 nM and dexamethasone and triamcinolone at 0.1 and 1 nM respectively. Degradation of glucokinase was initiated in 2-day-old hepatocytes after removal of triamcinolone and insulin. Protein synthesis was essential for the onset of degradation and glucagon did not affect the rate of glucokinase degradation.

Animals↗
PubMed1978

Fusion of isolated myoblast plasma membranes. An approach to the mechanism.

Fusion of plasma membranes isolated from myoblasts grown in culture has been investigated. 1. Membrane fusion was specifically dependent of Ca2+ at physiological concentrations. However, at higher concentrations of cations, fusion could be triggered not only by Ca2+, but by Mg2+ and Sr2+ as well. 2. The amount of fusion was directly proportional to temperature. 3. Fusion was found to depend on the state of maturation of the myoblast membranes. 4. Experiments with chemically and enzymatically modified membranes and with membranes derived from myoblasts grown in the presence of inhibitors of protein biosynthesis suggest the participation of proteinaceous membrane components in the fusion mechanism.

Animals↗
PubMed1978

Cellular recognition by rat liver cells of neuraminidase-treated erythrocytes. Demonstration and analysis of cell contacts.

Freshly isolated rat liver cells adhere firmly to neuraminidase-treated rat or mouse erythrocytes but not to untreated erythrocytes. Binding between cells occurs only in the presence of calcium and is specially inhibited by D-galactose. We therefore suggest that cell adherence is mediated by a galactose-specific hepatic membrane receptor. Ultrastructural analysis of contact regions revealed point-like interactions between hepatic microvilli and erythrocytes and no broad areas of membrane contact. When liver cells are cultivated in vitro they lose their ability to bind erythrocytes within 24 h.

Animals↗
PubMed1977

Regulation of glycogen synthase interconversion in cultured muscle cells: actions of insulin, calcium, ionophore A 23187 and cytochalasin B.

The glycogen content of cultured chick embryo breast muscle cells changes during their development and can be reduced by starvation. It is demonstrated that the rate of glucose incorporation into glycogen and the degree of interconversion of glycogen synthase are controlled by the actual glycogen content. Stimulation of both corresponding activities by insulin is found in fused and in unfused cells. The insulin response depends on the extracellular calcium concentration and can be mimicked by the ionophore A 23187. These metabolic effects as well as calcium efflux data confirm the hypothesis that insulin acts on its enzyme target via increased cytoplasmic calcium concentration. Cytochalasin B is shown to inhibit the interconversion but does not interfere with the insulin-induced increase of the mitochondrial calcium pool or with the acceleration of the calcium efflux out of 45C-preloaded myotubes.

Animals↗
PubMed1976

Physical properties of muscle cell membranes during fusion. A fluorescence polarization study with the ionophore A23187.

1. The fluorescence polarization of A23187 is used to detect physical changes in myoblast membranes produced by Ca2+ concentrations which are able to trigger fusion. Temperature scans reveal a Ca2+-dependent fluidity increase in the microenvironment of the ionophore above 37 degree C. 2. Time-dependent polarization measurements show two different effects. The first one consists of a fast polarization increase which reaches its maximum after 5-10 min. This change could be explained by a Ca2+-induced phase separation of acidic and neutral phospholipids in the membrane. The second effect is a slow polarization decrease over 2-3 h subsequent to the fast increase. 3. The information derived from the fluorescence polarization is in accordance with the characteristics of the fusion of myoblast cells regarding the dependence on Ca2+ concentration, the inhibition by Mg2+ and lysolecithin as well as a typical temperature of 35-37 degree C where fusion rate changes abruptly.

Animals↗
PubMed1976

Insulin action on glucose transport and calcium fluxes in developing muscle cells in vitro.

The glucose transport system of developing muscle cells in vitro is described. Uptake experiments showed stereospecificity but no saturation or competition. Km-values for early myoblasts could not be determined; with progressive development, the absolute amount of uptake increases and becomes insulin sensitive. Km-values of about 13 mM basal and 32 mM for insulin stimulation were determined and discussed with respect to the glucose transport mechanism. Basal and insulin-dependent transport were shown to be dependent on the presence of calcium in the medium. Moreover, the ionophore A 23187 could be shown to mimic the insulin effect on glucose uptake. 45Ca saturation and desaturation experiments showed that insulin enhances the "mitochondrial" calcium pool by 35% and increases the apparent "cytoplasmic" efflux rate constant by 50%. We propose that insulin increases the free cytoplasmic calcium concentration, which may be the intracellular signal for the stimulation of glucose transport.

Animals↗
PubMed1975

Calcium-related changes of enzyme activities in energy metabolism of cultured embryonic chick myoblasts and myotubes.

Changes in activity of enzymes involved in energy metabolism have been determined in unfused, fused as well as in fusion-inhibited chick embryo muscle cells in vitro. Functionally related enzymes which supposedly are coded by "gene clusters" show a similar degree and rate of enzyme activity increase. Hexokinase and glucose-6-phosphate dehydrogenase reveal only slight activity changes during muscle cell development under the conditions studied. The elevation of phosphofructokinase can be distinguished from that of the other glycolytic enzymes by its higher rate of increase and from that of phosphorylase by its time-course of activity change. The Ca2+ dependence of the phosphorylase activity increase runs parallel to myoblast fusion rate. Experiments in which calcium was removed from cultures which had reached the final morphological state of mature myotubes 24 h after onset of fusion show that increases of enzyme activities are irreversible and that these increases proceed at unchanged rates. Experimental evidence suggest that although fusion and enzyme syntheses may be uncoupled, both are similarly triggered by being dependent on Ca2+ concentration.

Animals↗