Human urinary kallikrein converts inactive to active renin and is a possible physiological activator of renin

Sealey, Jean E.; Atlas, Steven A.; Laragh, John H.; Oza, Narendra B.; Ryan, James W.

doi:10.1038/275144a0

Cited by 180 publications

(53 citation statements)

References 16 publications

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“…Figure 3 shows a representative experiment analyzing HPLC-injected cell homogenate samples preincubated with trypsin and then incubated with angiotensinogen to determine total renin activity. As can be seen, the angiotensinogen peak was reduced and the angiotensin I peak was increased over time (4,8,12 and 24 h). After 24 h of incubation, the angiotensinogen peak almost disappeared while the angiotensin I peak was substantially increased, indicating that a substantial quantity of angiotensinogen was hydrolyzed, releasing angiotensin I.…”

Section: Hplc Analysesmentioning

confidence: 70%

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Characterization of renin mRNA expression and enzyme activity in rat and mouse mesangial cells

Andrade

Casarini

Schor

et al. 2002

Braz J Med Biol Res

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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 and release both the active and inactive forms of the enzyme. Active renin and total renin content obtained after trypsin treatment were estimated by angiotensinogen consumption analyzed by SDS-PAGE electrophoresis and quantified by angiotensin I generation by HPLC. Renin mRNA, detected by RT-PCR, was present in both rat and mouse MC under basal conditions. Active renin was significantly higher (P<0.05) in the cell lysate (43.5 ± 5.7 ng h -1 10 6 cells) than in the culture medium (12.5 ± 2.5 ng h -1 10 6 cells). Inactive prorenin content was similar for the intra-and extracellular compartments (9.7 ± 3.1 and 3.9 ± 0.9 ng h -1 10 6 cells). Free active renin was the predominant form found in both cell compartments. These results indicate that MC in culture are able to synthesize and translate renin mRNA probably as inactive prorenin which is mostly processed to active renin inside the cell. MC secrete both forms of the enzyme but at a lower level compared with intracellular content, suggesting that the main role of renin synthesized by MC may be the intracellular generation of angiotensin II.

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Section: Hplc Analysesmentioning

confidence: 70%

“…About 80% of intracellular renin has little or no enzymatic activity and is called inactive renin or prorenin (2). Inactive renin can be converted into the active form through limited proteolysis at physiological pH by tissue proteases such as trypsin and kallikreins (3,4), but probably by cathepsin B in vivo (5).…”

Section: Introductionmentioning

confidence: 99%

Characterization of renin mRNA expression and enzyme activity in rat and mouse mesangial cells

Andrade

Casarini

Schor

et al. 2002

Braz J Med Biol Res

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show abstract

“…However, kallikrein has been reported to increase renin release (25) and to convert inactive renin to the active peptide (26), and has been proposed to play an important role in the normal regulation of renin. Since urinary kallikrein excretion is increased by administration ofCEI, it is possible that the increase in plasma renin activity observed in the nephrotic rats is the result ofrenin release and/or peripheral conversion ofinactive to active renin induced by kallikrein rather than by loss of negative feedback from angiotensin II.…”

Section: Discussionmentioning

confidence: 99%

Altered renal kallikrein and renin gene expression in nephrotic rats and modulation by converting enzyme inhibition.

Hutchison¹,

Webster²,

Jaffa³

1993

J. Clin. Invest.

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“…Renal kallikrein, however, may be relevant as there is evidence suggesting it may increase plasma renin activity directly by promoting the conversion of inactive renin to active renin 62 and it is well established that urinary kallikrein, an index of renal kallikrein, is substantially lower in blacks compared with whites, and this is independent of hypertension status. 63,64 Renal kallikrein could also be important as it generates the potent vasodilator and natriuretic peptide bradykinin which may in turn influence renin release indirectly through its effect on renal haemodynamics.…”

Section: Hormones and Pra In Whites And Blacksmentioning

confidence: 99%

Why is plasma renin activity lower in populations of African origin?

Sagnella

2000

J Hum Hypertens

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Plasma renin activity is significantly lower in black people compared with whites independent of age and blood pressure status. The lower PRA appears to be due to a reduction in the rate of secretion of renin but the exact mechanistic events underlying such differences in renin release between blacks and whites are still not fully understood. Nevertheless, given the paramount importance of the renin-angiotensin system in the control of sodium balance, a most likely explanation is that the lower renin is a consequence of differences in renal sodium handling between blacks and whites. The lower PRA does not reflect differences in dietary sodium intake but the evidence available suggests that the low PRA could be part of the corrective mechanisms designed to maintain sodium balance in the presence of an increased tendency for sodium retention in black people. While it is possible that several factors may contribute to the reduced PRA, more recent investigation at

show abstract

Human urinary kallikrein converts inactive to active renin and is a possible physiological activator of renin

Cited by 180 publications

References 16 publications

Characterization of renin mRNA expression and enzyme activity in rat and mouse mesangial cells

Characterization of renin mRNA expression and enzyme activity in rat and mouse mesangial cells

Altered renal kallikrein and renin gene expression in nephrotic rats and modulation by converting enzyme inhibition.

Why is plasma renin activity lower in populations of African origin?

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