Hagiwara Y, Kojima M, Hayashi I, Oh-ishi S
Department of Pharmacology, School of Pharmaceutical Sciences, Kitasato University, Tokyo, Japan.
Biochem Biophys Res Commun. 1994 Nov 15;204(3):1219-24. doi: 10.1006/bbrc.1994.2593.
The origin of urinary bradykinin was defined by use of plasma kininogen-deficient B/N-Katholiek rats, whose ureter urine contains very low amount of urinary kinin. The kinin level increased after the rats received an infusion of normal plasma. Furthermore, the bradykinin content in the ureter urine of these kininogen-deficient rats increased more by infusion of partially purified rat- low-molecular-weight kininogen than by that of high-molecular-weight kininogen. Urinary kallikrein activity of B/N-Katholiek rats was enzymatically identical with that of normal B/N-Kitasato rats. These results indicate that urinary bradykinin found in the ureter urine of normal rats is derived from plasma low-molecular-weight kininogen by cleavage by urinary kallikrein.
