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lüll Molecular and cellular effects of C-peptide--new perspectives on an old peptide Wahren J; Shafqat J; Johansson J; Chibalin A; Ekberg K; Jornvall HExp Diabesity Res 2004[Jan]; 5 (1): 15-23New results present C-peptide as a biologically active peptide hormone in its own right. Although C-peptide is formed from proinsulin and cosecreted with insulin, it is a separate entity with biochemical and physiological characteristics that differ from those of insulin. There is direct evidence of stereospecific binding of C-peptide to a cell surface receptor, which is different from those for insulin and other related hormones. The C-peptide binding site is most likely a G-protein-coupled receptor. The association constant for C-peptide binding is approximately 3 x 10(9) M(-1). Saturation of the binding occurs already at a concentration of about 1 nM, which explains why C-peptide effects are not observed in healthy subjects. Binding of C-peptide results in activation of Ca2+ and MAPK-dependent pathways and stimulation of Na+,K(+)-ATPase and eNOS activities. The latter 2 enzymes are both deficient in several tissues in type 1 diabetes. There is some evidence that C-peptide, and insulin may interact synergistically on the insulin signaling pathway. Clinical evidence suggests that replacement of C-peptide, together with regular insulin therapy, may be beneficial in patients with type 1 diabetes and serve to retard or prevent the development of long-term complications.|Amino Acid Sequence[MESH]|Animals[MESH]|C-Peptide/genetics/metabolism/*physiology[MESH]|Calcium/metabolism[MESH]|Cell Membrane/metabolism[MESH]|Humans[MESH]|Insulin/physiology[MESH]|Intracellular Membranes/metabolism[MESH]|Mitogen-Activated Protein Kinases/metabolism[MESH]|Molecular Sequence Data[MESH]|Molecular Structure[MESH]|Nitric Oxide Synthase Type III[MESH]|Nitric Oxide Synthase/metabolism[MESH]|Signal Transduction[MESH]|Sodium-Potassium-Exchanging ATPase/metabolism[MESH] |