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Tonin and kallikrein-kinin system
M H Feitosa1, J L Pesquero, M A Ferreira
1Department of Physiology and Biophysics, Federal University of Minas Gerais, Brazil.
Rat uterine contractions induced by tonin suggest two distinct kininogenase substrates. Desensitization experiments reveal specific interactions between tonin, kallikrein, and uterine muscle.
Area of Science:
- Biochemistry
- Pharmacology
- Physiology
Background:
- Tonin, an enzyme from the rat submandibular gland, possesses kininogenase activity.
- Previous studies have demonstrated the kininogenase activity of tonin.
Purpose of the Study:
- To investigate the mechanism of rat uterine contraction induced by tonin.
- To explore the potential presence of distinct substrates for tonin and kallikrein in the rat uterus.
- To elucidate the relationship between tonin, kallikrein, and kinin release.
Main Methods:
- Uterine contraction assays using isolated rat uteri.
- Enzyme desensitization experiments with tonin, kallikrein, and trypsin.
- Parallel uterus preparations to assess kinin release.
Main Results:
- Tonin induced rat uterine contractions, which were subject to desensitization upon repeated exposure.
- Desensitization to tonin significantly reduced subsequent contractions induced by kallikrein, but not vice versa.
- Desensitization to trypsin abolished tonin-induced contractions.
- Experiments suggested the release of kinin during tonin-mediated uterine contraction.
Conclusions:
- The rat uterus likely contains at least two distinct kininogenase substrates, with differential specificity for tonin and kallikrein.
- Tonin's action on the uterus involves kinin release, mediated by a trypsin-sensitive substrate.
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