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C-peptide is a 31-amino-acid polypeptide that connects the A-chain and B-chain of insulin in the proinsulin molecule. It is released from pancreatic beta cells in equimolar amounts with insulin during the cleavage of proinsulin. While originally considered biologically inactive and used primarily as a biomarker for endogenous insulin production (especially to distinguish between endogenous and exogenous insulin sources), research has shown that C-peptide binds to cell surfaces—likely via G-protein-coupled receptors—and activates intracellular signaling pathways such as MAPK, PLCγ, PKC, eNOS, and Na+K+ATPase. These actions are associated with improved nerve function and renal protection in animal models of type 1 diabetes. C-peptide also exhibits anti-inflammatory effects and may reduce endothelial dysfunction by modulating nitric oxide production and reactive oxygen species generation. It is under investigation for therapeutic use in diabetic complications such as peripheral neuropathy[3][5][8].
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