Prorenin
Mostrando 1-12 de 36 artigos, teses e dissertações.
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1. Superimposing a high-fat diet on Schistosoma mansoni infection affects renin-angiotensin system components in the mouse kidney
Abstract INTRODUCTION: The levels of the full-length form of the (pro)renin receptor (PRR), a component of the renin-angiotensin system (RAS), may be reduced in the membranes of kidneys in renal diseases. This study aimed to investigate the RAS components in the kidneys of mice submitted to a combination of a high-fat diet and Schistosoma mansoni infection.
Rev. Soc. Bras. Med. Trop.. Publicado em: 07/03/2019
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2. Regulação do receptor de (pro)renina em células mesangiais sob estímulo de alta glicose. / Inglês: (Pro)renin receptor regulation in mesangial cell under high glucose stimulus.
O receptor de renina/prorenina (RRP) foi identificado em células mesangiais (CM) e sua ligação com a renina ou prorenina resulta no aumento da síntese de angiotensina II (AII) na superfície celular. A estimulação do RRP também induz fosforilação de proteínas quinases mitogênicas ERK1/2 levando a proliferação celular e supraregulação de moléc
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 25/03/2009
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3. Efeitos da pró-renina humana em cardiomiócitos de ratos neonatos e seu processamento pela catepsina B humana em céluklas GH4CI / Efeitos da pró-renina humana em cardiomiócitos de ratos neonatos e seu processamento pela catepsina B humana em céluklas GH4CI
A renina é uma aspartil protease sintetizada in vivo pela remoção proteolítica do prósegmento amino-terminal de seu precursor, a pró-renina. A catepsina B, uma tiol protease, tem sido sugerida como candidata à enzima conversora de pró-renina devido à sua colocalização com a renina nos grânulos secretórios e também pela sua capacidade de process
Publicado em: 2008
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4. Characterization of renin mRNA expression and enzyme activity in rat and mouse mesangial cells
Renin is an enzyme involved in the stepwise generation of angiotensin II. Juxtaglomerular cells are the main source of plasma renin, but renin activity has been detected in other cell types. In the present study we evaluated the presence of renin mRNA in adult male Wistar rat and mouse (C-57 Black/6) mesangial cells (MC) and their ability to process, store a
Brazilian Journal of Medical and Biological Research. Publicado em: 2002-01
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5. Cyclical secretion of prorenin during the menstrual cycle: synchronization with luteinizing hormone and progesterone.
Plasma prorenin, a high molecular weight precursor form of renin, (renin, EC 3.4.23.15; old number, EC 3.4.99.19), was measured three times weekly in normal young women during the menstrual cycle and was related to changes in luteinizing hormone, estradiol, and progesterone. In all subjects a stable baseline level of prorenin occurred during the follicular p
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6. Human ovarian theca cells are a source of renin.
Human ovarian follicular fluid contains renin-like activity. In normal women, circulating levels of prorenin, the biosynthetic precursor of renin (EC 3.4.23.15), change in parallel with changes in progesterone during the menstrual cycle. Therefore, the ovary has been implicated as a source of plasma prorenin. In the present studies, we report the finding of
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7. Response of plasma prorenin and active renin to chronic and acute alterations of renin secretion in normal humans. Studies using a direct immunoradiometric assay.
We employed a novel immunoradiometric assay to measure plasma levels of active renin and prorenin in physiologic and pharmacologic studies designed to characterize renin biosynthesis and processing in response to both chronic and acute stimuli of renin secretion in normal human subjects. Stimulation of renin secretion with prolonged dietary sodium restrictio
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8. Human renin biosynthesis and secretion in normal and ischemic kidneys.
The pathway of renin biosynthesis and secretion in normal and ischemic human kidneys has been investigated by pulse-labeling experiments. The results indicate that in normal human kidney, preprorenin is rapidly processed to 47-kDa prorenin. Microradiosequencing showed that this molecule was generated by cleavage between Gly-23 and Leu-24, yielding a 43-amino
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9. Initiation of plasma prorenin activation by Hageman factor-dependent conversion of plasma prekallikrein to kallikrein.
Plasma prorenin is an inactive form of renin (EC 3.4.99.19) that can be converted to active renin in acid-treated plasma by an endogenous serine protease that is active at alkaline pH (alkaline phase activation). To identify this enzyme we first tested the ability of Hageman factor fragments, plasma kallikrein (EC 3.4.21.8), and plasmin (EC 3.4.21.7) to acti
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10. Inhibition of diabetic nephropathy by a decoy peptide corresponding to the “handle” region for nonproteolytic activation of prorenin
We found that when a site-specific binding protein interacts with the “handle” region of the prorenin prosegment, the prorenin molecule undergoes a conformational change to its enzymatically active state. This nonproteolytic activation is completely blocked by a decoy peptide with the handle region structure, which competitively binds to such a binding p
American Society for Clinical Investigation.
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11. Raised plasma renin and prorenin in rheumatoid vasculitis.
The value of plasma renin and its inactive precursor, prorenin, were examined as a marker for vasculitis in rheumatoid arthritis (RA). Plasma renin and prorenin rise when the renin-angiotensin system is activated; an isolated increase of prorenin may be a marker for microvascular complications in diabetes mellitus. Renin concentrations in plasma obtained fro
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12. Regulation of prorenin secretion in cultured human transfected juxtaglomerular cells.
The regulation of renin secretion was studied in continuous culture of human juxtaglomerular cells (JGC), which provided a permanent source of human renin production (Pinet, F., M. T. Corvol, F. Dench, J. Bourguignon, J. Feunteun, J. Ménard, and P. Corvol, 1985, Proc. Natl. Acad. Sci. USA, 82:8503-8507). 95% of the renin species secreted was prorenin, and t