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George Grunberger, X. Qiang, Z. Li, Suresh Mathews, D. Sbrissa, A. Shisheva, Anders Sima (2001)
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Proinsulin Cpeptide and its Cteminal pentapeptide : degradation in human serum and chiff base formation with subsequent CO 2 incorporation
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C - peptide stimulates ERK 1 / 2 phosphorylation via specific activation of PKC isoforms delta and epsilon in human renal tubular cells
Studies of C-peptide cellular effects show that not only the full-length native peptide but also specific C-terminal fragments are biologically active in in vitro systems. In the present study, the effect of five C-peptide fragments and the native peptide on whole-body glucose turnover was studied in streptozotocin diabetic rats using the insulin clamp technique. Insulin was infused intravenously at 18 pmol kg–1 min–1 for 90 min and blood glucose concentration was clamped at 8 and 4 mM in diabetic and non-diabetic animals. A steady state was reached during the last 30 min of the study period. Rat C-peptide II and fragments comprising residues 27–31 and 28–31 were effective in augmenting glucose turnover in diabetic rats (+100% to 150%), while no significant effects were seen for segments 1–26, 11–19 and 11–15. The metabolic clearance rate for glucose during infusion of C-peptide or fragments 27–31 and 28–31 in diabetic rats was similar to that seen in non-diabetic animals. We conclude that C-terminal tetra- and pentapeptides, but not fragments from the middle segment of C-peptide, are as effective as the full-length peptide in stimulating whole-body glucose turnover in diabetic rats.
Cellular and Molecular Life Sciences – Springer Journals
Published: Dec 18, 2003
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