Results 171 to 180 of about 3,425 (209)
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Regulation of utero-placental prorenin

Regulatory Peptides, 1994
Prorenin (Pro) is synthesized in a number of human utero-placental tissues, including chorion, decidua, villous placenta and probably mesenchymal cells. The release of Pro from these extra-renal tissues follows new protein synthesis and appears to utilize the constitutive secretory pathway.
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Prorenin receptor in kidney development

Pediatric Nephrology, 2016
Prorenin receptor (PRR), a receptor for renin and prorenin and an accessory subunit of the vacuolar proton pump H+-ATPase, is expressed in the developing kidney. Global loss of PRR is lethal in mice, and PRR mutations are associated with a high blood pressure, left ventricular hypertrophy and X-linked mental retardation in humans.
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[The prorenin receptor].

Journal de la Societe de biologie, 2010
The renin-angiotensin system (RAS) is one of the most important systems in physiology and in pathology. The (pro)renin receptor [(P)RR] is a new component of the system that has attracted much attention, being potentially a new therapeutic target, because the binding of renin and of prorenin triggers the activation of the mitogen-activated protein ...
Diane, Bracquart   +3 more
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"Prorenin" in human plasma?

Circulation Research, 1975
An increase in plasma renin activity was demonstrated in plasma from normal subjects and most patients with essential hypertension after prolonged storage of the plasma at -20 degrees C. No change in renin substrate concentration was observed after storage for 12 months, and the rate of angiotensin generation during incubation with a fixed amount of ...
J E, Sealey, J H, Laragh
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Renin and prorenin as biomarkers in hypertension

Current Opinion in Nephrology & Hypertension, 2012
This review examines the evidence that plasma renin and/or prorenin level may be used to guide therapy in hypertension and as an independent risk factor for future cardiovascular events.A large number of retrospective analyses of patient populations in clinical trials, in whom 'baseline' renin measurements were available, supports that high renin, but ...
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Synthetic peptide inhibitors of prorenin activation

Journal of Hypertension, 1989
In studying potential inhibitors of prorenin activation, we synthesized stereoisomers of a nonapeptide which spans the putative prorenin cleavage site. Peptide 67 has a D-Leu substitution on the amino side of the sessile bond and peptide 68 has a D-Arg substitution on the carboxy side.
D, Dubin, K, Hui, R E, Pratt, V J, Dzau
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Immunological evidence that inactive renin is prorenin

Biochemical and Biophysical Research Communications, 1985
Antibody raised to a synthetic dodecapeptide, corresponding to the C-terminal portion of the human renin pro-segment, was tested for its ability to recognize highly purified human inactive or active (mature) renins; immune complexes were detected by precipitation with protein A-Sepharose.
S A, Atlas   +4 more
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Secretion of prorenin by a virilizing ovarian tumor

Gynecologic Oncology, 1992
A 53-year-old normotensive, normokalemic female presented with a 6-month history of virilization. Estradiol, LH, FSH, urinary-free cortisol, and DHEA-S levels were normal. Pelvic ultrasound and computerized tomography were also within normal limits. Her serum testosterone (551 ng/dl; nl, 20-70) and plasma prorenin (124 ng AI/ml/hr; nl, less than 50 ...
P W, Anderson   +4 more
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EXTRACTION OF PLASMA PRORENIN BY HUMAN HEART

The Lancet, 1986
Arterial plasma prorenin underwent 58% extraction during one passage through the coronary circulation in eleven patients undergoing myocardial metabolic studies. Active renin and renin substrate were unaffected. Changes in renin and renin substrate concentrations were not detected across the enterohepatic, femoral, or renal vascular beds.
S L, Skinner   +3 more
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Cathepsin B Is a Prorenin Processing Enzyme

Hypertension, 1996
Abstract Conversion of prorenin to renin results from proteolytic cleavage of a 43-amino-acid prorenin prosegment in renal juxtaglomerular cells. The enzyme that performs this processing is not known. Of several enzymes proposed, cathepsin B is a candidate because it colocalizes with renin in juxtaglomerular cell secretory ...
F A, Neves, K G, Duncan, J D, Baxter
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