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  • 1
    Electronic Resource
    Electronic Resource
    Effect of insulin on amino acid transport in isolated rat hepatocytes (1978)
    Springer
    Diabetologia 15 (1978), S. 117-123 
    Details
    ISSN: 1432-0428
    Keywords: Amino acid transport ; isolated hepatocytes ; liver ; insulin action ; insulin binding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The effects of insulin on amino acid transport were studied in freshly prepared suspensions of isolated hepatocytes from adult rats. Insulin stimulated the active transport of α-aminoisobutyric acid by increasing the influx. The onset of the insulin effect was delayed by thirty to sixty min. Insulin increased the Vmax of transport by about 60% without affecting the Km. Cycloheximide and actinomycin D inhibited hormonal action by 60 to 80%. Only the “A” system of transport was affected by insulin. Half-maximal stimulation of transport was observed with insulin at 2 to 3nmol/l, a concentration which also occupies about 50% of insulin-specific binding sites at steady state. Insulin did not antagonize the stimulatory effect of glucagon on amino acid transport.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00422256
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Relationship of binding to internalization of125I-insulin in isolated rat hepatocytes (1979)
    Springer
    Diabetologia 17 (1979), S. 379-384 
    Details
    ISSN: 1432-0428
    Keywords: Insulin receptor ; internalization ; endocytosis ; hepatocytes ; binding ; insulin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary By quantitative electron microscopic autoradiographic technique, we have previously shown that125I-insulin initially localizes to the plasma membrane of isolated rat hepatocytes and is subsequently internalized in a limited region of the peripheral cytoplasm. In the present study, we have shown that when cells are incubated at 20 °C, steady state binding is reached by 60 minutes and maintained up until 120 minutes of incubation while at 37 °C steady state binding is reached by 10 minutes and maintained for 30 minutes. Under both of these conditions, internalization of the labelled material occurs as a constant function of the binding. These data suggest that under normal conditions the binding of the ligand is an important rate limiting determinant of the internalization process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01236273
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Studies on the mechanism of insulin resistance after injury in the mouse (1978)
    Springer
    Diabetologia 14 (1978), S. 337-341 
    Details
    ISSN: 1432-0428
    Keywords: Injury ; insulin binding ; insulin resistance ; glucagon binding ; muscle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Acute insulin resistance developed after scald injury in the mouse. After 2h plasma glucose and insulin concentrations were each raised about two-fold. Glucose metabolism was studied in vitro in soleus muscles isolated at this time. Glycolysis and glycogen synthesis, and their stimulation by insulin, were unchanged in muscles from scalded mice, and insulin-stimulated transport of 2-deoxyglucose slightly increased, showing that the insulin resistance seen in vivo is not maintained in isolated tissues. Binding of insulin to liver cell membranes prepared from scalded mice was unaltered, whilst that of glucagon was slightly but significantly reduced, showing that changes in polypeptide-hormone receptors can occur within this short time. It was concluded that the acute loss of sensitivity to insulin after injury does not result from a change in insulin receptor sites and presumably reflects an impairment of glucose metabolism in vivo mediated by circulating hormones.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01223026
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Anti-insulin receptor antibodies inhibit insulin binding and stimulate glucose metabolism in skeletal muscle (1978)
    Springer
    Diabetologia 14 (1978), S. 311-317 
    Details
    ISSN: 1432-0428
    Keywords: Anti-insulin receptor antibodies ; insulin-like effects ; insulin resistance ; skeletal muscle ; insulin receptor ; insulin binding ; insulin action ; glucose transport ; glycolysis ; glycogen synthesis ; obese mice
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Autoantibodies against the insulin receptor are found in the serum of some patients with severe insulin resistance. The effects of one of these sera on insulin binding and on glucose transport and metabolism were investigated in the isolated mouse soleus muscle. Preincubation of muscles with the patient's serum resulted in an inhibition of subsequent125I-insulin binding (half-maximal effect at 1∶500 dilution) and in a two to three-fold stimulation of glucose transport and metabolism (half-maximal effect at 1∶2000 dilution). The insulin-like effects were blocked by anti-human IgG, but not by antiinsulin antibodies. The magnitude of the serum effects on 2-deoxyglucose uptake and glycolysis was similar to that of insulin, but the effect on glycogen synthesis was smaller than that of insulin. It is suggested that the patient's serum and insulin promote glucose transport and glycolysis through a common pathway, but act differently on glycogen synthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01223022
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  • 5
    Electronic Resource
    Electronic Resource
    Somatostatin in the pancreas and hypothalamus of obese mice (1979)
    Springer
    Diabetologia 17 (1979), S. 257-261 
    Details
    ISSN: 1432-0428
    Keywords: Somatostatin ; insulin ; glucagon ; endocrine pancreas ; hypothalamus ; obesity ; ob/ob mouse ; goldthioglucose-obese mouse
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The pancreatic content of somatostatin, insulin, and glucagon and the hypothalamic content of somatostatin were examined inob/ob mice at various ages and in goldthioglucose-obese mice. The total pancreatic content of somatostatin was increased inob/ob mice compared to controls: 92 ng vs 75 ng (a 22% increase) at 2 months of age; 208 ng vs 131 ng (a 60% increase) at 6 months of age; and 184 ng vs 118 ng (a 60% increase) at 8 months of age. The total pancreatic content of glucagon inob/ ob mice was already enhanced by 70% over controls at 2 months of age (301 ng vs 173 ng) and did not increase further at later stages, whereas that of insulin progressively rose with age. In goldthioglucoseobese mice the pancreatic content of insulin was also increased but to a lesser extent than inob/ob mice; the pancreatic levels of somatostatin and glucagon were unaltered. In bothob/ob mice (regardless of age) and goldthioglucose-obese mice, there was no significant change in the hypothalamic content of somatostatin compared with that of lean controls.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01235863
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Interactions of polypeptide hormones with cell membrane specific receptors: Studies with insulin and glucagon (1976)
    Springer
    Diabetologia 12 (1976), S. 83-100 
    Details
    ISSN: 1432-0428
    Keywords: Insulin ; glucagon ; polypeptide hormones ; receptors ; plasma membrane ; isolated liver cells ; isolated fat cells ; liver membranes ; fat cell membranes ; cardiac membranes ; adenylate cyclase ; monoiodoinsulin ; monoiodoglucagon ; 125I-insulin binding ; 125I-glucagon binding ; radioreceptorassay ; structure-function relationships ; modified insulins ; obese hyperglycémic (ob/ob) mouse ; obesity ; receptor defect ; insulin resistance ; insulin-dextran-ferritin ; visualization of binding sites
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00428972
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    Paper (German National Licenses)
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  • 7
    Electronic Resource
    Electronic Resource
    Glucagon and insulin from lean rats and genetically obese fatty rats: Studies by radioimmunoassay, radioreceptorassay and bioassay (1975)
    Springer
    Diabetologia 11 (1975), S. 517-526 
    Details
    ISSN: 1432-0428
    Keywords: Insulin ; glucagon ; receptors ; adenylate cyclase ; radioreceptorassay ; bioassay ; radioimmunoassay ; liver membranes ; fat cells ; genetically obese rat (fatty)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Insulin, proinsulin and glucagon extracted from lean rat pancreases were studied in radioimmunoassay, radioreceptorassay and bioassay systems. Extracted insulin behaved identically to a rat insulin used as a reference standard in radioimmunoassay. On the basis of its immunoreactivity, extracted insulin was slightly less potent (about 70%) than the rat standard insulin in competing with the binding of125I-insulin to rat liver membranes (radioreceptorassay) and in stimulating glucose oxidation by rat fat cells (bioassay). Extracted glucagon and a pork glucagon used as a reference standard were indistinguishable in two radioimmunoassay systems for glucagon, in competing with the binding of125I-glucagon to rat liver membranes (radioreceptorassay) and in stimulating adenylate cyclase in rat liver membranes (bioassay). Genetically obese rats (Zucker, “fatty”) were compared to their lean littermates with respect to insulin, proinsulin and glucagon extracted from their pancreases. Proinsulin represented the same proportion of total immunoreactive insulin in both types of rats. In the radioimmunoassays, the radioreceptorassays and the bioassays, insulin, proinsulin and glucagon from obese rats were indistinguishable from insulin, proinsulin and glucagon from lean rats. It is concluded that the pancreatic hormones of obese (“fatty”) rats possess the same immunoreactivity and biological potency as those of nonobese rats. This excludes the possibility that some alteration in the biological properties of pancreas insulin and/or glucagon of fatty rats could explain the metabolic abnormalities observed in this type of obesity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01222101
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  • 8
    Electronic Resource
    Electronic Resource
    A study of insulin binding sites in the chicken tissues (1977)
    Springer
    Diabetologia 13 (1977), S. 219-228 
    Details
    ISSN: 1432-0428
    Keywords: Insulin ; glucagon ; binding sites ; receptors ; liver plasma membrane ; hepatocyte ; erythrocyte ; chicken ; rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Specific binding of chicken and porcine insulin was demonstrated in isolated chicken hepatocytes, chicken liver plasma membranes and chicken erythrocytes. In the liver, the binding reaction was characterized by a sensitivity and an apparent affinity which were similar to those observed in rat liver and, in contrast, by a decreased number of binding sites. In chicken liver, there were about 5 times fewer binding sites per mg of membrane protein or per unit of cell surface area than in rat liver. In chicken erythrocytes, the number of insulin binding sites per cell was even lower than in chicken hepatocytes. This decreased insulin binding was not accounted for by a faster insulin degradation in chicken tissues. Glucagon binding sites also appeared to be less numerous in chicken than in rat liver, at least at low glucagon concentration; however, the decrease in maximal binding capacity in chicken liver involved insulin and not glucagon binding. That chicken cells are equipped with insulin receptors which are less numerous than in mammalian cells may explain, partly at least, the physiological state of insulin resistance observed in the chicken.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01219703
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  • 9
    Electronic Resource
    Electronic Resource
    125I-Insulin is preferentially internalized in regions of the hepatocytes rich in lysosomal and Golgi structures (1979)
    Springer
    Cellular and molecular life sciences 35 (1979), S. 904-906 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary 125I-Insulin initially localizes to the plasma membrane of isolated rat hepatocytes but is subsequently internalized and preferentially associates with lysosomal structures. In the present study, we show that this preferential association to lysosomes occurs in regions of the cell rich in lysosomal and Golgi structures.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01955140
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