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What’s new in the renin-angiotensin system?

Physiological roles of angiotensin-converting enzyme 2

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Abstract.

Angiotensin-converting enzyme 2 (ACE2) is a recently discovered homologue of the key enzyme of the renin-angiotensin system, the angiotensin-converting enzyme. The ACE2 enzyme is mainly expressed in cardiac blood vessels and tubular epithelia of the kidneys. Together with ACE2’s unique metallocarboxypeptidase activity, the restricted tissue distribution suggests a distinctive physiological function in blood pressure, blood flow and fluid regulation. The ace2 gene was mapped to quantitative trait loci affecting susceptibility to hypertension in rats. Furthermore, ACE2 appears to be a negative regulator of ACE in the heart. ACE2 messenger RNA and protein levels are substantially regulated in the kidney of diabetic and pregnant rats. The mechanism of ACE2 function and its physiologic significance are not yet fully understood; however, as ACE2 differs in its specificity and physiological role from ACE, this opens a new potential venue for drug discovery aimed at cardiovascular disease, hypertension and diabetic complications.

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Authors and Affiliations

  1. Departments of Medical Biophysics and Immunology, University of Toronto, 620 University Avenue, Toronto, M5G 2C1, Ontario, Canada

    U. Danilczyk & J. M. Penninger

  2. IMBA, Institute for Molecular Biotechnology of the Austrian Academy of Sciences, Dr. Bohr Gasse 7, 1030, Vienna, Austria

    U. Danilczyk & J. M. Penninger

  3. Departments of Research and Internal Medicine, Basel University Hospital, 4031, Basel, Switzerland

    U. Eriksson

  4. Faculty of Medicine, Heart and Stroke/Richard Lewar Centre of Excellence, Fitzgerald Building, University of Toronto, Rm 68, 150 College St., Toronto, M5S 2E3, Ontario, Canada

    G. Y. Oudit

Authors
  1. U. Danilczyk
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  2. U. Eriksson
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  3. G. Y. Oudit
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  4. J. M. Penninger
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Corresponding author

Correspondence to J. M. Penninger.

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Danilczyk, U., Eriksson, U., Oudit, G.Y. et al. What’s new in the renin-angiotensin system?. CMLS, Cell. Mol. Life Sci. 61, 2714–2719 (2004). https://doi.org/10.1007/s00018-004-4241-6

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  • DOI: https://doi.org/10.1007/s00018-004-4241-6

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