Corin is co-expressed with pro-ANP and localized on the cardiomyocyte surface in both zymogen and catalytically active forms

Gladysheva, Inna P.; Robinson, Brian R.; Houng, Aiilyan K.; Kováts, Tímea; King, Samuel T.

doi:10.1016/j.yjmcc.2007.10.002

Cited by 50 publications

(54 citation statements)

References 32 publications

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“…The other candidate enzyme, corin, is located on the plasma membrane and has been shown to cleave the precursors upon secretion (18 ). The potential ability of corin to cleave proBNP has been described (19 ), whereas both the influence of proBNP glycosylation on corin-mediated processing and the specificity of cleavage have not been previously shown.…”

Section: Discussionmentioning

confidence: 99%

“…We evaluated cleavage efficiency using the following formula: [1 -(proBNP concentration in the furintreated sample/proBNP concentration in the control sample)] ϫ 100%. The concentration of proBNP in the samples was estimated by use of the in-house sandwich IFA 50E1 102-108 -16F3 [13][14][15][16][17][18][19][20] .…”

Section: Methodsmentioning

confidence: 99%

“…The other candidate enzyme, corin, is a recently discovered membrane-bound serine protease mainly produced in heart (16 ). In cell-based experiments, corin has been shown to be a specific enzyme responsible for processing of the A-type natriuretic peptide precursor (17,18 ). Corin has also been suggested to be responsible for proBNP processing (19 ), but its potential involvement in this process has not been supported by convincing experimental data.…”

Section: B-type Natriuretic Peptide (Bnp)mentioning

confidence: 99%

“…Assay 50E1 102-108 -16F3 [13][14][15][16][17][18][19][20] was chosen as a reference assay for measuring total proBNP, because it is not affected by proBNP glycosylation (25 ). We used assay 21E6 67-73 -24C5 87-93 for quantifying the proBNP nonglycosylated in the cleavage site region because it uses the mAb 21E6 67-73 , which is sensitive to the proBNP glycosylation in that region (10 ).…”

Section: Furin-mediated Cleavage Of Endogenous Probnp From the Plasmamentioning

confidence: 99%

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Processing of Pro–B-Type Natriuretic Peptide: Furin and Corin as Candidate Convertases2

et al. 2010

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BACKGROUND: B-type natriuretic peptide (BNP) and its N-terminal fragment (NT-proBNP) are the products of the enzyme-mediated cleavage of their precursor molecule, proBNP. The clinical significance of proBNP-derived peptides as biomarkers of heart failure has been explored thoroughly, whereas little is known about the mechanisms of proBNP processing. We investigated the role of 2 candidate convertases, furin and corin, in human proBNP processing.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: B-type Natriuretic Peptide (Bnp)mentioning

confidence: 99%

Section: Furin-mediated Cleavage Of Endogenous Probnp From the Plasmamentioning

confidence: 99%

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Processing of Pro–B-Type Natriuretic Peptide: Furin and Corin as Candidate Convertases2

et al. 2010

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“…Corin is a type II transmembrane serine protease that is highly expressed in cardiomyocytes (1)(2)(3)(4). The human corin gene is mapped to chromosome 4p12-13 (1) and encodes a polypeptide of 1,042 amino acids (5).…”

Section: Introductionmentioning

confidence: 99%

IL-1β increases urinary corin in patients with primary proteinuric kidney diseases and in 293 cells

et al. 2017

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Abstract. Corin is a serine protease that is important for the regulation of blood pressure and water balance. Corin was initially discovered in the heart, however, it has also been detected in kidney cells, though its function in the kidneys is unclear. To further investigate the function of corin in the kidney, the present study analyzed the levels of corin in urine and blood samples collected from normal individuals and patients with primary proteinuric diseases. The associations between the levels of corin, and the cytokines interleukin-1β (IL-1β) and tumor necrosis factor-α (TNF-α) were then assessed. The results demonstrated that corin was detectable in the urine and plasma following an enzyme-linked immunosorbent assay; the level of corin in the urine was associated with the level of urinary β 2 -microglobulin (P=0.01), which was indicative of renal tubular injury. When compared with normal individuals, the levels of urinary corin in proteinuric patients were markedly increased (P=0.02), and were also associated with IL-1β (P=0.03). This correlation between corin and IL-1β was confirmed in vitro using 293 cells. As the IL-1β concentrations increased (0, 0.1, 1, 10 ng/ml), an elevation in the level of corin was observed in the culture medium (P<0.01); however, the amount of corin was not markedly altered in the cell lysate (P>0.05). In addition, when TNF-α reached 10 ng/ml, the level of corin in the medium increased significantly when compared with the control group (0 ng/ml; P=0.02), however, no significant difference in corin levels was detected in the cell lysate. The results suggest that the cytokines IL-1β and TNF-α may increase urinary corin in patients with primary proteinuric kidney diseases. Cytokines may accelerate corin shedding from the cell membrane of renal tubule epithelial cells. These findings indicate that corin may be associated with kidney inflammation and injury.

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Corin in Natriuretic Peptide Processing and Hypertension

Zhou

2014

Curr Hypertens Rep

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Corin is a serine protease originally isolated from the heart. Functional studies show that corin is the long-sought enzyme responsible for activating cardiac natriuretic peptides. In mice, lack of corin prevents the natriuretic peptide processing, causing salt-sensitive hypertension. In humans, corin variants and mutations that reduce corin activity have been identified in patients with hypertension and heart failure. Decreased plasma levels of corin antigen and activity have been reported in patients with heart failure and coronary artery disease. Low levels of urinary corin also have been found in patients with chronic kidney disease. Most recent studies show that corin also acts in the uterus to promote spiral artery remodeling and prevent pregnancy-induced hypertension. Here we review the role of corin in natriuretic peptide processing and cardiovascular diseases such as hypertension, heart disease, pre-eclampsia, and chronic kidney disease.

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Corin is co-expressed with pro-ANP and localized on the cardiomyocyte surface in both zymogen and catalytically active forms

Cited by 50 publications

References 32 publications

Processing of Pro–B-Type Natriuretic Peptide: Furin and Corin as Candidate Convertases2

Processing of Pro–B-Type Natriuretic Peptide: Furin and Corin as Candidate Convertases2

IL-1β increases urinary corin in patients with primary proteinuric kidney diseases and in 293 cells

Corin in Natriuretic Peptide Processing and Hypertension

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