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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Diabetologia 13 (1977), S. 251-255 
    ISSN: 1432-0428
    Keywords: Insulin receptor ; cultured lymphocytes ; insulin structure function relationship ; insulin chains
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The ability of insulin and the S-sulphonate A and B-chain derivatives to bind to a receptor on cultured human lymphocytes was evaluated. A receptor site for the S-sulphonate A-chain was identified and was strongly influenced by the intact insulin molecule. S-sulphonate A-chain weakly interfered with insulin binding. S-sulphonate B-chain showed no evidence of significant binding and did not interfere with insulin or S-sulphonate A chain binding.14CO2 production from14C-1-glucose was stimulated by insulin in cultured lymphocytes and this effect was blunted by S-sulphonate A-chain. The sulphhydryl blocking agent used in the production of insulin A-chain appears to be of critical importance.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0428
    Keywords: Insulin receptor ; mutation ; tyrosine kinase activity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We evaluated a 35-year-old diabetic male patient with type A insulin resistance, showing acanthosis nigricans. Insulin binding to the patient's Epstein-Barr-virus transformed lymphocytes was mildly reduced. The maximal insulin-stimulated autophosphorylation of the insulin receptor from the patient's transformed lymphocytes was decreased to 45% of that from the control subjects. On examination, the biological activities of insulin and insulin-like growth factor I in the patient's cultured fibroblasts, insulin sensitivity of amino isobutyric acid uptake and thymidine incorporation was decreased, but insulin-like growth factor I action was normal. The sequence analysis of amplified genomic DNA revealed that the patient was heterozygous for a mutation substituting Leu for Trp at codon 1193 in exon 20 of the insulin receptor gene. The patient's mother and sister were also heterozygous for a mutation in the insulin receptor gene that substituted Leu for Trp1193 in the Β subunit of the receptor. Therefore, the mutation causes insulin resistance in a dominant fashion. They were less hyperglycaemic and more hyperinsulinaemic than the proband after glucose loading. The mother had diabetes mellitus but did not show acanthosis nigricans, while the sister did not have diabetes and showed acanthosis nigricans. These results suggest that this mutation causes defective tyrosine kinase activity of the insulin receptor, which results in insulin resistance. Insulin action and phenotypic appearance may be mediated by different factors.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0428
    Keywords: Insulin receptor ; insulin proreceptor ; insulin resistance ; transformed lymphocytes ; point mutation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary An alteration of an amino acid sequence in the processing site of the insulin proreceptor by a point mutation of the insulin receptor gene produced extreme insulin resistance. We characterized functional properties of the unprocessed insulin receptor in transformed lymphocytes from a patient. Insulin binding to intact cells and to a partially purified insulin receptor preparation was radically decreased to 20% and 18% of the control values, respectively. In competitive insulin binding to intact cells, [LeuA3]-, [LeuB24]-, [SerB24-insulin, and mini-proinsulin ([B(1–29)-Ala-Ala-Lys-A(1–21)]-insulin) had the same relative binding activity in both the patient's and the control cells, but proinsulin and IGF-I were markedly less able to displace 125I-insulin in the patient's cells. In contrast to the study in intact cells, proinsulin and IGF-I as well as other insulin analogues had the same relative binding activity to bind to the partially lectin-purified insulin receptor preparations from both the patient's and the control cells. As regards the signal transduction after receptor binding, insulin-stimulated autophosphorylation of the unprocessed insulin proreceptor occurred proportionally to the amount of decreased insulin binding. With 0.025% trypsin treatment, the abnormal binding characteristics and autophosphorylation were normalized through conversion to functionally normal receptors. In spite of the abnormal processing, self-association of receptors into oligomeric structures was observed in the proreceptor. These results suggest that the unprocessed insulin proreceptor in the plasma membranes has an altered conformation which affects its binding characteristics but not its intramolecular signal transmission.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Gene Structure and Expression 1216 (1993), S. 425-430 
    ISSN: 0167-4781
    Keywords: (Human) ; COS 7 cell ; Co-transfection ; Insulin receptor ; Insulin resistance ; Tyrosine kinase
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Molecular Cell Research 1053 (1990), S. 185-188 
    ISSN: 0167-4889
    Keywords: Alpha-beta subunit interaction ; Insulin receptor ; Kinase defective insulin receptor ; Ligand binding affinity ; Tyrosine kinase
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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