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