Corin Mutations K317E and S472G from Preeclamptic Patients Alert Zymogen Activation and Cell Surface Targeting

Dong, Ningzheng; Zhou, Tiantian; Zhang, Yue; Li, Meng; Li, Hui; Huang, Xin; Liu, Zhenzhen; Wu, Yi; Fukuda, Koichi; Qin, Jun; Wu, Qingyu

doi:10.1074/jbc.m114.551424

Cited by 46 publications

(34 citation statements)

References 52 publications

(61 reference statements)

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“…Hepsin and TMPRSS3 are important for normal hearing1617. Defects in these TTSPs may lead to major diseases such as skin disorders1819, congenital or inflammatory diarrheal diseases202122, iron-deficiency anaemia232425, hypertension26272829, and hearing loss16.…”

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confidence: 99%

The Transmembrane Serine Protease HAT-like 4 Is Important for Epidermal Barrier Function to Prevent Body Fluid Loss

Zhang

Yan

et al. 2017

Sci Rep

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Membrane-bound proteases are essential for epidermal integrity. Human airway trypsin-like protease 4 (HAT-L4) is a type II transmembrane serine protease. Currently, its biochemical property, cellular distribution and physiological function remain unknown. Here we examined HAT-L4 expression and function in vitro and in vivo. In Western analysis, HAT-L4 expressed in transfected CHO cells appeared as a 48-kDa protein. Flow cytometry confirmed HAT-L4 expression on the cell surface with the expected membrane topology. RT-PCR and immunostaining experiments indicated that HAT-L4 was expressed in epithelial cells and exocrine glands in tissues including skin, esophagus, trachea, tongue, eye, bladder, testis and uterus. In the skin, HAT-L4 expression was abundant in keratinocytes and sebaceous glands. We generated HAT-L4 knockout mice by disrupting the Tmprss11f gene encoding HAT-L4. HAT-L4 knockout mice were viable and fertile. No defects were found in HAT-L4 knockout mice in hair growth, wound healing, water repulsion and body temperature regulation. Compared with wild-type controls, HAT-L4-deficient newborn mice had greater body fluid loss and higher mortality in a trans-epidermal body fluid loss test. In metabolic studies, HAT-L4-deficient adult mice drank water more frequently than wild-type controls did. These results indicate that HAT-L4 is important in epidermal barrier function to prevent body fluid loss.

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The Transmembrane Serine Protease HAT-like 4 Is Important for Epidermal Barrier Function to Prevent Body Fluid Loss

Zhang

Yan

et al. 2017

Sci Rep

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“…Human corin protein was expressed with the plasmid pcDNACorin (Invitrogen) [36]. The protein encoded by this plasmid contained a C-terminal V5 tag for detection in Western blotting using an anti-V5 antibody (Invitrogen).…”

Section: Methodsmentioning

confidence: 99%

Localization of corin and atrial natriuretic peptide expression in human renal segments

et al. 2016

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Atrial natriuretic peptide (ANP)-mediated natriuretic response is a well-established cardiac endocrine function. Corin is a transmembrane protease that activates ANP in the heart. Corin expression has been detected in non-cardiac tissues including the kidney. Here we examined corin, pro-ANP/ANP and natriuretic peptide receptor-A (NPR-A) expression in human renal segments. By immunostaining and in situ hybridization, we found similar corin, pro-ANP/ANP and NPR-A protein and mRNA expression in human renal segments. The expression was most abundant in the proximal convoluted tubules and the medullary connecting ducts. In the proximal tubules, corin protein was present in the apical membrane region underneath the brush border where the ANP-degrading protease neprilysin was abundant. These results suggest that corin-mediated pro-ANP activation may occur in renal segments and that locally produced ANP may act in an autocrine manner to regulate sodium and water reabsorption in situ. Our results also point to the proximal convoluted tubules as a major site for local ANP action. Such a renal corin/ANP autocrine mechanism may differ from the cardiac corin/ANP endocrine mechanism in regulating sodium homeostasis under physiological and pathological conditions.

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“…In Corin and Nppa knockout mice, uterine spiral artery remodeling was impaired, causing gestational hypertension and proteinuria (Armstrong et al, 2013; Cui et al, 2012). In humans, CORIN variants associated with preeclampsia were reported in a Caucasian population (Stepanian et al, 2014) and CORIN mutations reducing corin activity were identified in preeclamptic patients (Cui et al, 2012; Dong et al, 2014). Consistent with these findings, low levels of plasma corin were associated with the risk of preeclampsia (Khalil et al, 2015).…”

Section: Biological Functions Of Anpmentioning

confidence: 99%

Atrial natriuretic peptide in cardiovascular biology and disease (NPPA)

Song

Wang

2015

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Atrial natriuretic peptide (ANP) is a cardiac hormone that regulates salt-water balance and blood pressure by promoting renal sodium and water excretion and stimulating vasodilation. ANP also has an anti-hypertrophic function in the heart, which is independent of its systemic blood pressure-lowering effect. In mice, ANP deficiency causes salt-sensitive hypertension and cardiac hypertrophy. Recent studies have shown that ANP plays an important role in regulating vascular remodeling and energy metabolism. Variants in the human NPPA gene, encoding the ANP precursor, are associated with hypertension, stroke, coronary artery disease, heart failure (HF) and obesity. ANP and related peptides are used as biomarkers for heart disease. Recombinant proteins and small molecules that enhance the ANP pathway have been developed to treat patients with HF. In this review, we discuss the role of ANP in cardiovascular biology and disease.

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Corin Mutations K317E and S472G from Preeclamptic Patients Alert Zymogen Activation and Cell Surface Targeting

Cited by 46 publications

References 52 publications

The Transmembrane Serine Protease HAT-like 4 Is Important for Epidermal Barrier Function to Prevent Body Fluid Loss

The Transmembrane Serine Protease HAT-like 4 Is Important for Epidermal Barrier Function to Prevent Body Fluid Loss

Localization of corin and atrial natriuretic peptide expression in human renal segments

Atrial natriuretic peptide in cardiovascular biology and disease (NPPA)

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