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  • 1
    Electronic Resource
    Electronic Resource
    Internalization of polypeptide hormones (1980)
    Springer
    Diabetologia 18 (1980), S. 263-274 
    Details
    ISSN: 1432-0428
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00251003
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Binding and degradation of 125I-insulin by renal glomeruli and tubules isolated from rats (1982)
    Springer
    Diabetologia 22 (1982), S. 276-284 
    Details
    ISSN: 1432-0428
    Keywords: Insulin receptor ; insulin binding ; insulin degradation ; kidney ; renal glomeruli ; renal tubules ; insulin analogues
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Isolated rat renal glomeruli and tubules were shown to exhibit specific binding of 125I-insulin and enzymatic degradation of the hormone. Binding to both renal fractions reached a plateau by 1h at 22 °C and increased linearly with increasing protein concentrations. Binding was inhibited in both preparations by insulin and its analogues in the order of relative potency: insulin 〉 despentapeptide insulin 〉 proinsulin, but insulin was ten times more potent in inhibiting 125I-insulin binding to glomeruli than that to tubules, indicating a different affinity of receptors for the hormone in the two renal fractions (about 17 versus 210 μg unlabelled insulin/l inhibiting 50% of the 125I-insulin binding to glomeruli and tubules, respectively). Bound 125I-insulin dissociated at a faster rate from tubules than from glomeruli; this release was accelerated by unlabelled insulin in both renal fractions, but to a greater extent in glomeruli than in tubules. Two-thirds of the total bound material released from glomeruli was found to be intact insulin as measured by trichloroacetic acid precipitation, whereas only one-third of the material released from tubules was intact. No direct relationship between binding and degradation of 125I-insulin in these renal fractions could be demonstrated, however, because of the release of proteolytic enzymes into the incubation medium resulting in almost all degradation being extracellular. Although differing in their affinity for 125I-insulin the high affinity glomerular insulin receptor and the lower affinity tubular insulin receptor have characteristics similar to those of insulin receptors in insulin responsive tissues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00281306
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Glucose and glucagon do stimulate somatostatin release from isolated pancreatic islets (1981)
    Springer
    Diabetologia 21 (1981), S. 238-238 
    Details
    ISSN: 1432-0428
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00252662
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    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Photoaffinity labelling of the insulin receptor in intact rat hepatocytes, mouse soleus muscle, and cultured human lymphocytes (1982)
    Springer
    Diabetologia 23 (1982), S. 440-444 
    Details
    ISSN: 1432-0428
    Keywords: Insulin ; insulin receptors ; mouse skeletal muscle ; rat hepatocytes ; human lymphocytes ; photoaffinity labelling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Using the photoreactive, biologically active insulin analogue, B2-(2 nitro, 4-azidophenylacetyl)des-PheB1 insulin, which can be covalently bound to receptor molecules upon photolysis, the insulin receptor has been studied in three different types of cells or tissues: isolated rat hepatocytes, intact murine soleus muscle and cultured human lymphocytes. When compared with native insulin, this analogue displayed a slightly reduced binding affinity. Accordingly, the biological potency of the photoreactive analogue was decreased by approximately 30% compared with native insulin when tested for its ability to stimulate amino acid transport in hepatocytes, and deoxyglucose uptake in soleus muscles. It was as effective as insulin, however, at maximally stimulating concentrations and therefore is a full insulin agonist. This photoprobe was used to specifically label the insulin receptor in the three tissues: after ultra-violet irradiation, sodium dodecyl sulphatepolyacrylamide gel analysis of extracts under reducing conditions revealed that most of the radioactivity was associated with a 130,000 dalton band. In isolated hepatocytes, two bands at 125,000 and 23,000 daltons were also specifically labelled. In three different cell types from three different animal species, the 130,000 dalton band appeared to be the major subunit of the insulin receptor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00260959
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Sulphonylureas in vitro do not alter insulin binding or insulin effect on amino acid transport in rat hepatocytes (1983)
    Springer
    Diabetologia 24 (1983), S. 441-444 
    Details
    ISSN: 1432-0428
    Keywords: Insulin receptors ; aminoacid transport ; primary cultures of hepatocytes ; sulphonylureas
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The effects of four sulphonylureas (gliclazide, glibenclamide, chlorpropamide and glipizide) on insulin binding and insulin action were studied in vitro using primary cultured rat hepatocytes. Cells were cultured for 20 h in the absence or presence of the sulphonylurea. The binding of insulin to rat hepatocyte monolayers was not altered in cells previously exposed to gliclazide at 0.7, 7.0 or 70 μg/ml; and to glibenclamide, chlorpropamide, or glipizide at 0.1, 1.0 and 10 μg/ ml. Insulin-induced down regulation was not affected by a simultaneous exposure of hepatocyte monolayers to any of the four agents. The stimulatory effect of insulin on α-aminoisobutyric acid uptake by the cells was not modified following exposure to the drugs. These studies indicate that the sulphonylureas tested do not have a direct effect on insulin receptors in hepatocytes; and that, in vitro, they do not alter the post-receptor events involved in the insulin-induced stimulation of amino acid transport in these cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00257344
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    Paper (German National Licenses)
    Fulltext
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