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  • 1
    Electronic Resource
    Electronic Resource
    Kinetics of insulin binding and kinase activity of the partially purified insulin receptor from human skeletal muscle
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Molecular Cell Research 1052 (1990), S. 306-312 
    Details
    ISSN: 0167-4889
    Keywords: (Human skeletal muscle) ; Insulin receptor kinase ; Kinetic analysis ; Skeletal muscle
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0167-4889(90)90226-4
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  • 2
    Electronic Resource
    Electronic Resource
    Decreased tyrosine kinase activity in partially purified insulin receptors from muscle of young, non-obese first degree relatives of patients with Type 2 (non-insulin-dependent) diabetes mellitus (1993)
    Springer
    Diabetologia 36 (1993), S. 668-674 
    Details
    ISSN: 1432-0428
    Keywords: Insulin resistance ; insulin receptor ; tyrosine kinase ; skeletal muscle ; Type 2 (non-insulin-dependent) diabetes mellitus ; insulin binding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Recently, we demonstrated insulin resistance due to reduced glucose storage in young relatives of Type 2 diabetic patients. To investigate whether this was associated with a defective insulin receptor kinase, we studied ten of these young (27±1 years old) non-obese glucose tolerant first degree relatives of patients with Type 2 diabetes and eight matched control subjects with no family history of diabetes. Insulin sensitivity was assessed by a hyperinsulinaemic, euglycaemic clamp. Insulin receptors were partially purified from muscle biopsies obtained in the basal and the insulin-stimulated state during the clamp. Insulin binding capacity was decreased by 28% in the relatives (p〈0.05) in the basal biopsy. Tyrosine kinase activity in the receptor preparation was decreased by 50% in both basal and insulin-stimulated biopsies from the relatives. After stimulation with insulin “in vitro”, kinase activity was reduced in the relatives in basal (p〈0.005) and insulin-stimulated (p〈0.01) biopsies and also when expressed per insulin binding capacity (p≈0.05). Insulin stimulation of non-oxidative glucose metabolism correlated with “in vitro” insulin-stimulated tyrosine kinase activity (r=0.61, p〈0.01) and also when expressed per binding capacity (r=0.53, p〈0.025). We suggest that the marked defect in tyrosine kinase activity in partially purified insulin receptors from skeletal muscle is an early event in the development of insulin resistance and contributes to the pathophysiology of Type 2 diabetes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00404079
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  • 3
    Electronic Resource
    Electronic Resource
    Decreased skeletal muscle phosphotyrosine phosphatase (PTPase) activity towards insulin receptors in insulin-resistant Zucker rats measured by delayed Europium fluorescence (1996)
    Springer
    Diabetologia 39 (1996), S. 142-148 
    Details
    ISSN: 1432-0428
    Keywords: Insulin receptor ; phosphotyrosine phosphatases ; insulin resistance ; skeletal muscle ; Zucker rats ; metformin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary In order to measure the phosphotyrosine phosphatase (PTPase) activity in small muscle biopsies, a sandwich-immunofluorescence assay was developed using the phosphorylated human insulin receptor as a substrate, a C-terminal insulin receptor antibody as catching antibody and Europium-labelled anti-phosphotyrosine as detecting antibody. Soluble and particulate muscle fractions were prepared from soleus muscle of obese, diabetic (fa/fa) Zucker rats and their lean littermates (Fa/-). In the soluble muscle fractions of the obese (fa/fa) rats PTPase activity was significantly reduced compared to control (Fa/-) rats (45.2±2.6% vs 61.3±4.7%, p〈0.02). This reduction was completely prevented by 24 days of metformin treatment which decreased plasma glucose and plasma insulin levels. In particulate muscle fractions, however, no difference in PTPase activity was found among any groups of rats examined. These results show that the alterations in soluble PTPase activity in the insulin-resistant, diabetic Zucker rat vary with the abnormality in glucose homeostasis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00403956
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  • 4
    Electronic Resource
    Electronic Resource
    C-peptide stimulates glucose transport in isolated human skeletal muscle independent of insulin receptor and tyrosine kinase activation (1996)
    Springer
    Diabetologia 39 (1996), S. 306-313 
    Details
    ISSN: 1432-0428
    Keywords: Keywords Glucose transport ; insulin receptor ; insulin binding ; insulin receptor tyrosine kinase ; human skeletal muscle ; C-peptide ; insulin ; catecholamines ; insulin-dependent diabetes mellitus.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We have previously demonstrated that C-peptide stimulates glucose transport in skeletal muscle from non-diabetic subjects in a dose-dependent manner. To further elucidate the mechanism by which C-peptide activates glucose transport, we investigated the influence of human recombinant C-peptide on receptor and post-receptor events involved in the glucose transport process. Human skeletal muscle specimens were obtained from the vastus lateralis by means of an open biopsy procedure. Stimulation of isolated muscle strips from healthy control subjects with supra-physiological concentrations of insulin (6,000 pmol/l) and C-peptide (2,500 pmol/l), did not further augment the twofold increase in the rate of 3-o-methylglucose transport induced by either stimulus alone. C-peptide did not displace 125I-insulin binding from partially purified receptors, nor did it activate receptor tyrosine kinase activity. Tyrosine-labelled 125I-C-peptide did not bind specifically to crude membranes prepared from skeletal muscle, or to any serum protein other than albumin. The β-adrenergic receptor stimulation with isoproterenol inhibited insulin- but not C-peptide-mediated 3-o-methylglucose transport by 63 ± 18 % (p 〈 0.01), whereas the cyclic AMP analogue, Bt2cAMP, abolished the insulin- and C-peptide-stimulated 3-o-methylglucose transport. C-peptide (600 pmol/l) increased 3-o-methylglucose transport 1.8 ± 0.2-fold in skeletal muscle specimens from patients with insulin-dependent diabetes mellitus. In conclusion, C-peptide stimulates glucose transport by a mechanism independent of insulin receptor and tyrosine kinase activation. In contrast to the effect on insulin-stimulated glucose transport, catecholamines do not appear to have a counter regulatory action on C-peptide-mediated glucose transport. [Diabetologia (1996) 39: 306–313]
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00418346
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  • 5
    Electronic Resource
    Electronic Resource
    Expression of insulin regulatable glucose transporters in skeletal muscle from Type 2 (non-insulin-dependent) diabetic patients (1990)
    Springer
    Diabetologia 33 (1990), S. 625-627 
    Details
    ISSN: 1432-0428
    Keywords: Type 2 (non-insulin-dependent) diabetes mellitus ; skeletal muscle ; glucose transporters ; insulin regulatable glucose transporters
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary A prominent feature of Type 2 (non-insulin-dependent) diabetes mellitus is the inability of insulin to appropiately increase the transport of glucose into target tissue. In adipocytes from individuals with Type 2 diabetes, insulin resistance has been shown to be associated with a depletion of glucose transporters. Similarly, streptozotocin induced diabetes causes a diminished expression of the insulin regulatable glucose transporter in rat adipocytes. The expression of this glucose transporter isoform has not yet been investigated in muscle tissue from patients with Type 2 diabetes. We have measured the content of the insulin regulatable glucose transporter in a vesicular fraction isolated from muscle biopsies from fasting individuals with Type 2 diabetes and control subjects, and we found that the number of the insulin regulatable glucose transporters expressed in skeletal muscle was unaffected by Type 2 diabetes (0.208 vs 0.205, arbitrary units, p〉0.5, control subjects and diabetic patients). Thus, the decreased glucose disposal in Type 2 diabetes is not associated with a diminished number of insulin regulatable glucose transporters.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00400207
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  • 6
    Electronic Resource
    Electronic Resource
    Elevated GLUT 1 level in crude muscle membranes from diabetic Zucker rats despite a normal GLUT 1 level in perineurial sheaths (1994)
    Springer
    Diabetologia 37 (1994), S. 443-448 
    Details
    ISSN: 1432-0428
    Keywords: Key words GLUT 4, glucose transporter, insulin resistance, (fa/fa) rats, GLUT 1, Zucker rats, skeletal muscle, perineurial sheath, crude membranes, hyperglycaemia, metformin.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Recently, we demonstrated that approximately 60 % of GLUT 1 in a crude membrane fraction of rat skeletal muscle originates from perineurial sheaths. To study the in vivo regulation of GLUT 1 expression in different tissues in muscles, we measured the level of GLUT 1 in crude muscle membranes and in perineurial sheaths in diabetic (fa/fa) Zucker rats and lean controls, with and without metformin treatment. The GLUT 1 concentration in perineurial sheaths was identical in all four groups of rats, both when measured by quantitative immunofluorescence and by immunoblotting and densitometry. In a fraction of crude membranes of soleus muscles GLUT 1 expression was more than two-fold higher in (fa/fa) rats than in lean controls (p〈0.005). Metformin treatment significantly elevated GLUT 1 in control rats (p〈0.05) and tended to decrease GLUT 1 in diabetic rats (p〈0.075). The expressions of GLUT 1 and GLUT 4 in crude muscle membranes were inversely correlated (p〈0.01), and GLUT 1 expression correlated positively with fasting glucose (p〈0.05). In conclusion, GLUT 1 expression in perineurial sheaths is unaffected by alterations in glucose homeostasis and by the genes responsible for obesity and diabetes in the Zucker rat. GLUT 1 expression in a crude membrane fraction of soleus muscle is increased in the diabetic animals, likely due to an increased expression in muscle cells proper. [Diabetologia (1994) 37: 443–448]
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001250050130
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  • 7
    Electronic Resource
    Electronic Resource
    C-peptide stimulates glucose transport in isolated human skeletal muscle independent of insulin receptor and tyrosine kinase activation (1996)
    Springer
    Diabetologia 39 (1996), S. 306-313 
    Details
    ISSN: 1432-0428
    Keywords: Glucose transport ; insulin receptor ; insulin binding ; insulin receptor tyrosine kinase ; human skeletal muscle ; C-peptide ; insulin ; catecholamines ; insulin-dependent diabetes mellitus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We have previously demonstrated that C-peptide stimulates glucose transport in skeletal muscle from non-diabetic subjects in a dose-dependent manner. To further elucidate the mechanism by which C-peptide activates glucose transport, we investigated the influence of human recombinant C-peptide on receptor and post-receptor events involved in the glucose transport process. Human skeletal muscle specimens were obtained from the vastus lateralis by means of an open biopsy procedure. Stimulation of isolated muscle strips from healthy control subjects with supra-physiological concentrations of insulin (6,000 pmol/l) and C-peptide (2,500 pmol/l), did not further augment the twofold increase in the rate of 3-o-methylglucose transport induced by either stimulus alone. C-peptide did not displace 125I-insulin binding from partially purified receptors, nor did it activate receptor tyrosine kinase activity. Tyrosine-labelled 125I-C-peptide did not bind specifically to crude membranes prepared from skeletal muscle, or to any serum protein other than albumin. The Β-adrenergic receptor stimulation with isoproterenol inhibited insulin- but not C-peptide-mediated 3-o-methylglucose transport by 63±18% (p〈0.01), whereas the cyclic AMP analogue, Bt2cAMP, abolished the insulin- and C-peptide-stimulated 3-o-methylglucose transport. C-peptide (600 pmol/l) increased 3-o-methylglucose transport 1.8±0.2-fold in skeletal muscle specimens from patients with insulin-dependent diabetes mellitus. In conclusion, C-peptide stimulates glucose transport by a mechanism independent of insulin receptor and tyrosine kinase activation. In contrast to the effect on insulin-stimulated glucose transport, catecholamines do not appear to have a counter regulatory action on C-peptide-mediated glucose transport.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00418346
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    Paper (German National Licenses)
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