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Thomas, Douglas D.

Biological Chemistry

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Volume 387, Issue 2 (Feb 2006)


Genetically altered animal models in the kallikrein-kinin system

João B. Pesquero
  • Department of Biophysics, Universidade Federal de São Paulo, São Paulo, CEP 04023-062, Brazil
/ Michael Bader
  • Max-Delbrück Center for Molecular Medicine, D-13125 Berlin, Germany
Published Online: 2006-02-09 | DOI: https://doi.org/10.1515/BC.2006.017


Transgenic and gene-targeting technologies allowing the generation of genetically altered animal models have greatly advanced our understanding of the function of specific genes. This is also true for the kallikrein-kinin system (KKS), in which some, but not yet all, components have been functionally characterized using such techniques. The first genetically altered animal model for a KKS component was supplied by nature, the brown Norway rat carrying an inactivating mutation in the kininogen gene. Mice deficient in tissue kallikrein, B1 and B2 receptors, some kinin-degrading enzymes, and factor XII followed, together with transgenic rat and mouse strains overexpressing tissue kallikrein, B1 and B2 receptors, and degrading enzymes. There are still no animal models with genetic alterations in plasma kallikrein, kininases I and some other degrading enzymes. The models have confirmed an important role of the KKS in cardiovascular pathology, inflammation, and pain, and have partially elucidated the distinct function of the two receptors. This created the basis for rational decisions concerning the putative use of kinin receptor agonists and antagonists in therapeutic applications. However, a more thorough analysis of the existing models and the generation of new, more sophisticated transgenic models will be necessary to clarify the still elusive issue as to where and by which mechanisms the kinins exert their actions.

Keywords: bradykinin; kininase; kininogen; kinin receptor; knockout animals; transgenic animals


About the article

Corresponding author

Published Online: 2006-02-09

Published in Print: 2006-02-01

Citation Information: Biological Chemistry, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2006.017. Export Citation

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