“Corination” of the proANP converting enzyme Lincoln R. Potter  Cell Metabolism  Volume 1, Issue 2, Pages 88-90 (February 2005) DOI: 10.1016/j.cmet.2005.01.008 Copyright © 2005 Elsevier Inc. Terms and Conditions

Figure 1 A schematic model of corin processing of proANP to ANP Human ANP is synthesized as a preprohormone. Removal of the amino-terminal 26 amino acid signal sequence produces proANP. The membrane-associated serine protease, corin, cleaves proANP at arginine 124 to produce the mature 28 amino acid disulfide-linked receptor binding form of the peptide. Cell Metabolism 2005 1, 88-90DOI: (10.1016/j.cmet.2005.01.008) Copyright © 2005 Elsevier Inc. Terms and Conditions