Corin, also called atrial natriuretic peptide-converting enzyme, is a
protein that in humans is encoded by the CORINgene.[5][6]
Protein
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]
Function
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 and mutations
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.[27][18][19][28]
^Gladysheva IP, King SM, Houng AK (August 2008). "N-glycosylation modulates the cell-surface expression and catalytic activity of corin". Biochemical and Biophysical Research Communications. 373 (1): 130–135.
doi:
10.1016/j.bbrc.2008.05.181.
PMID18549807.
^Baris Feldman H, Chai Gadot C, Zahler D, Mory A, Aviram G, Elhanan E, et al. (November 2023). "Corin and Left Atrial Cardiomyopathy, Hypertension, Arrhythmia, and Fibrosis". The New England Journal of Medicine. 389 (18): 1685–1692.
doi:
10.1056/NEJMoa2301908.
PMID37913506.
S2CID264931773.
Peleg A, Jaffe AS, Hasin Y (November 2009). "Enzyme-linked immunoabsorbent assay for detection of human serine protease corin in blood". Clinica Chimica Acta; International Journal of Clinical Chemistry. 409 (1–2): 85–89.
doi:
10.1016/j.cca.2009.09.004.
PMID19751717.
Armaly Z, Assady S, Abassi Z (November 2013). "Corin: a new player in the regulation of salt-water balance and blood pressure". Current Opinion in Nephrology and Hypertension. 22 (6): 713–722.
doi:
10.1097/01.mnh.0000435609.35789.32.
PMID24100222.
S2CID34150725.
Corin, also called atrial natriuretic peptide-converting enzyme, is a
protein that in humans is encoded by the CORINgene.[5][6]
Protein
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]
Function
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 and mutations
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.[27][18][19][28]
^Gladysheva IP, King SM, Houng AK (August 2008). "N-glycosylation modulates the cell-surface expression and catalytic activity of corin". Biochemical and Biophysical Research Communications. 373 (1): 130–135.
doi:
10.1016/j.bbrc.2008.05.181.
PMID18549807.
^Baris Feldman H, Chai Gadot C, Zahler D, Mory A, Aviram G, Elhanan E, et al. (November 2023). "Corin and Left Atrial Cardiomyopathy, Hypertension, Arrhythmia, and Fibrosis". The New England Journal of Medicine. 389 (18): 1685–1692.
doi:
10.1056/NEJMoa2301908.
PMID37913506.
S2CID264931773.
Peleg A, Jaffe AS, Hasin Y (November 2009). "Enzyme-linked immunoabsorbent assay for detection of human serine protease corin in blood". Clinica Chimica Acta; International Journal of Clinical Chemistry. 409 (1–2): 85–89.
doi:
10.1016/j.cca.2009.09.004.
PMID19751717.
Armaly Z, Assady S, Abassi Z (November 2013). "Corin: a new player in the regulation of salt-water balance and blood pressure". Current Opinion in Nephrology and Hypertension. 22 (6): 713–722.
doi:
10.1097/01.mnh.0000435609.35789.32.
PMID24100222.
S2CID34150725.