CORIN

Human corin, a polypeptide of 1042 amino acids, consists of an N-terminal cytoplasmic domain, a transmembrane domain and an extracellular region with two frizzled-like domains, eight LDL receptor-like domains, a scavenger receptor-like domain and a C-terminal trypsin-like serine protease domain.[5][7] Corin is synthesized as a zymogen that is activated by PCSK6.[8]

Corin exhibits a trypsin-like catalytic activity favoring basic residues at the P1 position.[9]

Human corin contains 19 N-glycosylation sites.[5] N-glycans promote corin expression on the cell surface and protect corin from metalloproteinase-mediated shedding.[10][11][12]

Corin converts the atrial natriuretic peptide (ANP) precursor, pro-ANP, to mature ANP, a cardiac hormone that regulates salt-water balance and blood pressure.[13] In mice, corin deficiency prevents pro-ANP processing and causes salt-sensitive hypertension.[14][15]

Corin may also function as a pro-brain-type natriuretic peptide convertase.[13][16][17]

Corin-mediated ANP production in the pregnant uterus promotes spiral artery remodeling and trophoblast invasion.[18] CORIN mutations have been reported in patients with preeclampsia.[18][19]

In mice, corin functions in the dermal papilla to regulate coat color in an Agouti-dependent pathway.[20]

Variants encoded by alternative exons were reported in human and mouse corin.[21] A variant allele (T555I/Q568P) was found in African Americans with hypertension and cardiac hypertrophy.[22][23] The amino acid substitutions impaired corin activity.[24][25] An insertion variant in exon 1 alters the cytoplasmic tail.[26] This variant appeared more frequently in hypertensive patients. CORIN mutations were found in patients with hypertension.[18][19][27]

• Human CORIN genome location and CORIN gene details page in the UCSC Genome Browser.