| Description |
The connecting peptide, or C-peptide, is a 31-aa long peptide that connects insulin A-chain to the B-chain in the proinsulin molecule. In the insulin synthesis pathway, preproinsulin is translocated into the endoplasmic reticulum of beta cells of the pancreas with an A-chain, a C-peptide, a B-chain, and a signal sequence. After signal sequence cleavage, the C-peptide is removed from the newly formed proinsulin in the Golgi apparatus leaving the A- and B-chains bound together by disulfide bonds, forming the insulin molecule. Besides a role in assembly, folding, and processing of insulin in the ER, the C-peptide is a bioactive peptide with effects on microvascular blood flow and tissue health. Because equimolar amounts of C-peptide are stored in secretory granules of the pancreatic beta cells and eventually released in the circulation, C-peptide is a marker of insulin secretion in understanding the pathophysiology of type 1 and type 2 diabetes.
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