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  • 1
    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
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Effect of human C-peptide on glucose transport in in vitro incubated human skeletal muscle (1991)
    Springer
    Diabetologia 34 (1991), S. 899-901 
    Details
    ISSN: 1432-0428
    Keywords: C-peptide ; glucose transport ; human ; insulin ; skeletal muscle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Muscle specimens from the quadriceps femoris muscle were obtained from eight healthy subjects by means of an open muscle biopsy and prepared for in vitro incubation. C-peptide at 0.5, 1.0 and 2.5 nmol/l increased 3-0-methylglucose transport by 38% (NS), 64% (p〈0.05), and 64 % (p〈0.05) respectively. Glucose transport increased 1.8-fold in the presence of 0.3 nmol/l of insulin (p〈0.05). Glycogen content in muscle strips exposed to C-peptide at a concentration of 1 nmol/l increased significantly by 22% (p〈0.05). In conclusion, C-peptide stimulates the rate of 3-0-methylglucose transport in in vitro incubated human skeletal muscle strips in a dose-response manner. These observations suggest that C-peptide may contribute to the regulation of carbohydrate metabolism in human skeletal muscle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00400197
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 3
    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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Involvement of phosphoinositide 3-kinase in insulin stimulation of MAP-kinase and phosphorylation of protein kinase-B in human skeletal muscle: implications for glucose metabolism (1997)
    Springer
    Diabetologia 40 (1997), S. 1172-1177 
    Details
    ISSN: 1432-0428
    Keywords: Keywords Muscle ; human ; insulin ; phosphoinositide 3-kinase ; Map-kinase ; protein kinase B ; glycogen synthase ; glucose transport.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Isolated skeletal muscle from healthy individuals was used to evaluate the role of phosphoinositide 3-kinase (PI 3-kinase) in insulin signalling pathways regulating mitogen activated protein kinase (MAP-kinase) and protein kinase-B and to investigate whether MAP-kinase was involved in signalling pathways regulating glucose metabolism. Insulin stimulated glycogen synthase activity ( ≈ 1.7 fold), increased 3-o-methylglucose transport into human skeletal muscle strips ( ≈ 2 fold) and stimulated phosphorylation of the p42 ERK-2 isoform of MAP-kinase. This phosphorylation of p42 ERK2 was not blocked by the PI 3-kinase inhibitors LY294002 and wortmannin although it was blocked by the MAP-kinase kinase (MEK) inhibitor PD 98059. However, PD98059 (up to 20 μmol/l) did not block insulin activation of glycogen synthase or stimulation of 3-o-methylglucose transport. Wortmannin and LY294002 did block insulin stimulation of protein kinase-B (PKB) phosphorylation and stimulation of 3-o-methylglucose transport was inhibited by wortmannin (IC50≈ 100 nmol/l). These results indicate that MAP-kinase is activated by insulin in human skeletal muscle by a PI 3-kinase independent pathway. Furthermore this activation is not necessary for insulin stimulation of glucose transport or activation of glycogen synthase in this tissue. [Diabetologia (1997) 40: 1172–1177]
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001250050803
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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