Copyright © 1989 by the European Society of Cardiology.
© 1989 The European Society of Cardiology
Coronary vessels contain enzymes that liberate kinin-like vasodilator substances
Department of Physiology and Pharmacology, University of Strathclyde, Royal College Glasgow G1 1XW, Scotland, U.K.
Address for correspondence: Professor J. R. Parratt, Department of Physiology and Pharmacology, University of Strathclyde, Royal College, Glasgow G1 1XW, Scotland, U.K.
The presence of an acid optimum (pH6) enzyme capable of generating a spasmogenic, vasodilator polypeptide from human plasma kininogen has been demonstrated in dog coronary arteries, veins and in the wall of the left ventricle. This enzyme also cleaved the tripeptide kallikrein substrate Val-Leu-Arg-pNA. Highest amounts were present in the coronary arteries. Gel filtration (Sephacryl S-300) of coronary artery extracts gave a peak for this acid optimum enzyme of 38, 300±800 Daltons. Its activity was inhibited by pepstatin but not by aprotinin or soya bean trypsin inhibitor. This enzyme, which is similar to a cathepsin, may play a role in the processing of peptide hormones in the heart and coronary vessels.
Key Words: coronary vasomotor tone kallikrein-kinin system vascular proteinases