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Cathepsin B is not the processing enzyme for mouse prorenin.

Chantal Mercure1, Marie-Josée Lacombe, Khashayarsha Khazaie

  • 1Laboratory of Molecular Biochemistry of Hypertension, Clinical Research Institute of Montreal, 110 Pine Avenue West, Montreal, Quebec, Canada.

American Journal of Physiology. Regulatory, Integrative and Comparative Physiology
|February 19, 2010
PubMed
Summary

Cathepsin B (CTSB) was investigated as the enzyme responsible for activating renin in mice. However, CTSB-deficient mice showed normal active renin levels, indicating CTSB is not the prorenin processing enzyme in vivo.

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Area of Science:

  • Biochemistry
  • Physiology
  • Molecular Biology

Background:

  • Renin initiates the renin-angiotensin system (RAS), regulating blood pressure.
  • Renin requires proteolytic activation by a prorenin processing enzyme (PPE) before secretion.
  • Cathepsin B (CTSB) was a candidate for PPE due to in vitro evidence.

Purpose of the Study:

  • To determine if CTSB is essential for prorenin processing in vivo.
  • To investigate the role of CTSB in generating active renin in mice.

Main Methods:

  • Utilized CTSB-deficient (CTSB-/-) mice.
  • Assessed active renin levels in circulation and kidney lysates.
  • Examined renin-producing cell morphology and distribution.
  • Evaluated renin activation response to RAS inhibition and chloroquine treatment.

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Main Results:

  • CTSB-/- mice exhibited normal development and no RAS deficiency symptoms.
  • Circulating active renin levels were comparable to controls and responded to RAS inhibition.
  • Renin molecular weight and processing were unaffected by CTSB deficiency or chloroquine.
  • Renin-producing cell characteristics remained normal in CTSB-/- mice.

Conclusions:

  • CTSB deficiency does not impair active renin generation in mice.
  • These findings do not support CTSB as the primary prorenin processing enzyme in vivo.
  • The identity of the in vivo PPE for renin remains undetermined.