CNP, a member of the natriuretic peptide family, was first identified in porcine brain and later found in other mammals as well as non-mammals. Processing of the CNP precursor gives rise to CNP-22 and its N-terminally elongated form, CNP-53. The CNPs shar
C-Type Natriuretic Peptide (CNP) (1-22), human (TFA), is a 22 amino acid fragment of CNP and functions as an agonist for the natriuretic peptide receptor B (NPR-B). It can inhibit cAMP synthesis, which is induced by histamine, 5-HT, or Forskolin. Additionally, CNP exhibits strong endothelial-derived relaxation properties and acts as a growth inhibitor.
Human proinsulin, the single-chain peptide precursor of insulin, consists of the insulin A and B chains connected by the 31 amino acid C-peptide. Cleavage of proinsulin by proteolytic enzymes produces insulin and free C-peptide.