Prorenin and Other Large Molecular Weight Forms of Renin*

Sealey, Jean E.; Atlas, Steven A.; Laragh, John H.

doi:10.1210/edrv-1-4-365

Cited by 222 publications

(94 citation statements)

References 116 publications

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“…the lower the ARC, the lower the TRC or AR ratio. The same kind of results have been reported by other authors (Derkx et al 1978 ;Sealey et al 1980). The origin of inactive renin in plasma is still obscure.…”

Section: Discussionsupporting

confidence: 83%

Active, inactive and total renin concentrations in plasma of hypertensive patients.

Goto

Abe

Tsunoda

et al. 1985

Tohoku J. Exp. Med.

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Section: Discussionsupporting

confidence: 83%

Active, inactive and total renin concentrations in plasma of hypertensive patients.

Goto

Abe

Tsunoda

et al. 1985

Tohoku J. Exp. Med.

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“…Trypsin, plasmin, pepsin, kallikrein, and other proteases can also activate prorenin. 11,33,34 However, some of these enzymes are unlikely candidates to process active renin, because, for example, trypsin and pepsin also degrade renin. Recently, van Kesteren et al 10 reported that human renin and human prorenin were taken up into neonatal rat cardiac myocytes and fibroblasts by the mannose-6 phosphate receptor.…”

Section: Discussionmentioning

confidence: 99%

“…In humans, as much as 90% of circulating renin exists in its enzymatically inactive form. 11 However, prorenin is both the primary and final product of renin gene expression in most tissues. [12][13][14] Juxtaglomerular cells of rat and human kidneys constitute the main site of prorenin synthesis and the exclusive site of its intracellular processing to active renin.…”

mentioning

confidence: 99%

“…15,16 In vitro, prorenin can be activated to active renin by cryoactivation, acid activation, or proteolytic activation. 11,15,[17][18][19][20][21] Recently, van Kesteren et al 10 reported that prorenin is taken up in neonatal rat cardiac myocytes and fibroblasts by the mannose-6 phosphate receptor followed by intracellular activation. However, the role of prorenin in physiology and pathology is still unknown.…”

mentioning

confidence: 99%

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Effects of Human Prorenin in Rats Transgenic for Human Angiotensinogen

Müller

Hilgers²,

Mathews³

et al. 1999

Hypertension

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Abstract-The physiological role of prorenin is unknown; however, the possibility that prorenin inhibits renin locally has been suggested. We tested the hypothesis that prorenin may be an endogenous competitor for renin uptake in the tissue. We also investigated whether prorenin can be activated to active renin and affect mean arterial pressure (MAP). Isolated perfused hindquarters of rats transgenic for human angiotensinogen were infused with human renin and/or prorenin. The plateau phase of angiotensin (Ang) I release 15 minutes after cessation of infusions was used as a parameter for renin uptake. Renin (10 ng/mL for 15 minutes) caused sustained release of Ang I (153Ϯ16 fmol/mL). Coinfusion with a 15-fold excess of prorenin did not affect local Ang I formation (153Ϯ19 fmol/mL). Prorenin infusion alone showed no activation to active renin. In addition, we investigated MAP and plasma Ang II levels after injection of saline (⌬MAP, Ϫ1Ϯ2 mm Hg; 40Ϯ5 fmol/mL Ang II), 9 ng renin (⌬MAP, ϩ37Ϯ3 mm Hg; 378Ϯ39 fmol/mL), and 144 ng prorenin (⌬MAP, ϩ10Ϯ5 mm Hg; 61Ϯ5 fmol/mL) and the coinjection of renin and prorenin (⌬MAP, ϩ41Ϯ4 mm Hg; 305Ϯ23 fmol/mL) in anesthetized rats. The data show that prorenin was not activated to active renin and did not affect MAP in short-term experiments. Renin-induced Ang formation was not affected by prorenin. Renin may have been taken up specifically because of its physical and chemical properties or because of nonspecific sequestration in the extravascular space. We conclude that prorenin does not act as an endogenous antagonist for the long-lasting effects of renin in the vascular wall. Moreover, prorenin does not affect acute renin-related effects on blood pressure.

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“…1 Prorenin was initially detected in amniotic fluid and then in the plasma, where it can be processed into renin after cryoactivation, acid activation, or proteolytic activation (1)(2)(3). The cleavage site is located at the amino terminus of prorenin, and renin is released as a 43-amino acid species-specific peptide (4, 5).…”

Section: Introductionmentioning

confidence: 99%

Vascular damage without hypertension in transgenic rats expressing prorenin exclusively in the liver.

Véniant¹,

Ménard²,

Bruneval³

et al. 1996

J. Clin. Invest.

154

123

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We have developed a transgenic animal model to investigate the effects of overexpression of rat prorenin on the cardiovascular system. Two transgenic rat lines were generated in which rat prorenin expression was directed to the liver by a human ␣ 1-antitrypsin promoter. Liver-specific expression was confirmed by RNase protection assay. Plasma prorenin concentrations in transgenic rats were increased 400-fold in the males of both lines but were increased only two-to threefold in the females. Thus, transgene expression exhibited sexual dimorphism. Blood pressures were not significantly higher in transgenic rats than in nontransgenic controls. The ratio of heart weight to body weight was greater in male transgenic rats than in the nontransgenic controls.

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Prorenin and Other Large Molecular Weight Forms of Renin*

Cited by 222 publications

References 116 publications

Active, inactive and total renin concentrations in plasma of hypertensive patients.

Active, inactive and total renin concentrations in plasma of hypertensive patients.

Effects of Human Prorenin in Rats Transgenic for Human Angiotensinogen

Vascular damage without hypertension in transgenic rats expressing prorenin exclusively in the liver.

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