Biology:CORIN

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A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Corin, also called atrial natriuretic peptide-converting enzyme, is a protein that in humans is encoded by the CORIN gene.[1][2]

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.[1][3] Corin is synthesized as a zymogen that is activated by PCSK6.[4]

Corin exhibits a trypsin-like catalytic activity favoring basic residues at the P1 position.[5]

Human corin contains 19 N-glycosylation sites.[1] N-glycans promote corin expression on the cell surface and protect corin from metalloproteinase-mediated shedding.[6][7][8]

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.[9] In mice, corin deficiency prevents pro-ANP processing and causes salt-sensitive hypertension.[10][11]

Corin may also function as a pro-brain-type natriuretic peptide convertase.[9][12][13]

Corin-mediated ANP production in the pregnant uterus promotes spiral artery remodeling and trophoblast invasion.[14] CORIN mutations have been reported in patients with preeclampsia.[14][15]

In mice, corin functions in the dermal papilla to regulate coat color in an Agouti-dependent pathway.[16]

Variants and mutations

Variants encoded by alternative exons were reported in human and mouse corin.[17] A variant allele (T555I/Q568P) was found in African Americans with hypertension and cardiac hypertrophy.[18][19] The amino acid substitutions impaired corin activity.[20][21] An insertion variant in exon 1 alters the cytoplasmic tail.[22] This variant appeared more frequently in hypertensive patients. CORIN mutations were found in patients with hypertension.[14][15][23]

References

  1. ↑ 1.0 1.1 1.2 "Corin, a mosaic transmembrane serine protease encoded by a novel cDNA from human heart". The Journal of Biological Chemistry 274 (21): 14926–35. May 1999. doi:10.1074/jbc.274.21.14926. PMID 10329693. 
  2. ↑ "Entrez Gene: CORIN corin, serine peptidase". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10699. 
  3. ↑ "Localization of the mosaic transmembrane serine protease corin to heart myocytes". European Journal of Biochemistry / FEBS 267 (23): 6931–7. Dec 2000. doi:10.1046/j.1432-1033.2000.01806.x. PMID 11082206. 
  4. ↑ "PCSK6-mediated corin activation is essential for normal blood pressure". Nature Medicine 21 (9): 1048–53. Sep 2015. doi:10.1038/nm.3920. PMID 26259032. 
  5. ↑ "Functional analysis of the transmembrane domain and activation cleavage of human corin: design and characterization of a soluble corin". The Journal of Biological Chemistry 278 (52): 52363–70. Dec 2003. doi:10.1074/jbc.M309991200. PMID 14559895. 
  6. ↑ "Role of glycosylation in corin zymogen activation". The Journal of Biological Chemistry 282 (38): 27728–35. Sep 2007. doi:10.1074/jbc.M703687200. PMID 17660514. 
  7. ↑ "N-glycosylation modulates the cell-surface expression and catalytic activity of corin". Biochemical and Biophysical Research Communications 373 (1): 130–5. Aug 2008. doi:10.1016/j.bbrc.2008.05.181. PMID 18549807. 
  8. ↑ "Distinct roles of N-glycosylation at different sites of corin in cell membrane targeting and ectodomain shedding". The Journal of Biological Chemistry 290 (3): 1654–63. Jan 2015. doi:10.1074/jbc.M114.606442. PMID 25451932. 
  9. ↑ 9.0 9.1 "Corin, a transmembrane cardiac serine protease, acts as a pro-atrial natriuretic peptide-converting enzyme". Proceedings of the National Academy of Sciences of the United States of America 97 (15): 8525–9. Jul 2000. doi:10.1073/pnas.150149097. PMID 10880574. 
  10. ↑ "Hypertension in mice lacking the proatrial natriuretic peptide convertase corin". Proceedings of the National Academy of Sciences of the United States of America 102 (3): 785–90. Jan 2005. doi:10.1073/pnas.0407234102. PMID 15637153. 
  11. ↑ "Impaired sodium excretion and salt-sensitive hypertension in corin-deficient mice". Kidney International 82 (1): 26–33. Jul 2012. doi:10.1038/ki.2012.41. PMID 22418978. 
  12. ↑ "Processing of pro-B-type natriuretic peptide: furin and corin as candidate convertases". Clinical Chemistry 56 (7): 1166–76. Jul 2010. doi:10.1373/clinchem.2010.143883. PMID 20489134. 
  13. ↑ "BNP molecular forms and processing by the cardiac serine protease corin". Advances in Clinical Chemistry 61: 1–31. 2013. doi:10.1016/b978-0-12-407680-8.00001-4. ISBN 9780124076808. PMID 24015598. 
  14. ↑ 14.0 14.1 14.2 "Role of corin in trophoblast invasion and uterine spiral artery remodelling in pregnancy". Nature 484 (7393): 246–50. Apr 2012. doi:10.1038/nature10897. PMID 22437503. 
  15. ↑ 15.0 15.1 "Corin mutations K317E and S472G from preeclamptic patients alter zymogen activation and cell surface targeting. [Corrected"]. The Journal of Biological Chemistry 289 (25): 17909–16. Jun 2014. doi:10.1074/jbc.M114.551424. PMID 24828501. 
  16. ↑ "The serine protease Corin is a novel modifier of the Agouti pathway". Development 135 (2): 217–25. Jan 2008. doi:10.1242/dev.011031. PMID 18057101. 
  17. ↑ "Human corin isoforms with different cytoplasmic tails that alter cell surface targeting". The Journal of Biological Chemistry 286 (23): 20963–9. Jun 2011. doi:10.1074/jbc.M110.217570. PMID 21518754. 
  18. ↑ "Corin gene minor allele defined by 2 missense mutations is common in blacks and associated with high blood pressure and hypertension". Circulation 112 (16): 2403–10. Oct 2005. doi:10.1161/CIRCULATIONAHA.105.568881. PMID 16216958. 
  19. ↑ "Corin I555(P568) allele is associated with enhanced cardiac hypertrophic response to increased systemic afterload". Hypertension 49 (4): 857–64. Apr 2007. doi:10.1161/01.HYP.0000258566.95867.9e. PMID 17296875. 
  20. ↑ "Corin variant associated with hypertension and cardiac hypertrophy exhibits impaired zymogen activation and natriuretic peptide processing activity". Circulation Research 103 (5): 502–8. Aug 2008. doi:10.1161/CIRCRESAHA.108.177352. PMID 18669922. 
  21. ↑ "Salt-sensitive hypertension and cardiac hypertrophy in transgenic mice expressing a corin variant identified in blacks". Hypertension 60 (5): 1352–8. Nov 2012. doi:10.1161/HYPERTENSIONAHA.112.201244. PMID 22987923. 
  22. ↑ "A corin variant identified in hypertensive patients that alters cytoplasmic tail and reduces cell surface expression and activity". Scientific Reports 4: 7378. 9 December 2014. doi:10.1038/srep07378. PMID 25488193. 
  23. ↑ "Corin mutation R539C from hypertensive patients impairs zymogen activation and generates an inactive alternative ectodomain fragment". The Journal of Biological Chemistry 288 (11): 7867–74. Mar 2013. doi:10.1074/jbc.M112.411512. PMID 23372161. 

External links

Further reading




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