Plasma kallikrein localisation in human blood vessels

Abstract

Immunoreactive plasma kallikrein/prekallikrein was detected in the endothelial cells and the smooth muscle cells of the arteries examined. The most intense overall immunolabelling of plasma kallikrein/prekallikrein was visualized in the medium to small size arteries. The endothelial cells of the pulmonary artery and the smooth muscle cells of the supracallosal artery showed the highest intensity of plasma kallikrein/prekallikrein labelling. The least defined labelling occurred in the tunica adventitia. The renal vein was the only blood vessel that showed no trace of immunoreactive plasma kallikrein/prekallikrein The question arises as to the mechanisms that could be involved in the in vivo conversion of plasma kallikrein/prekallikrein into the active enzymatic molecule. The experiments indicate that a bacterial elastase cleaves the Arg371–Ile372 scissile bond within a disulphide bridge of the prekallikrein molecule. This is the bond that is cleaved also during activation of prekallikrein by trypsin-like proteinases. Functionally, the endogenous activation of plasma prekallikrein is of considerable importance, both in the regulation of blood flow and blood pressure and in the causation of septic shock. The incidental finding at histology, of patchy atheromatous disease in the coronary, vertebral and supracallosal arteries, assisted in elucidating the role of plasma kallikrein/prekallikrein in the commonest disease affecting human blood vessels. Intense labelling for plasma kallikrein was observed in the endothelial cells, foamy macrophages, inflammatory cells and fibroblasts within the thickened intima of the plaque as well as in smooth muscle cells of the underlying tunica media. The intense immunolabelling of plasma kallikrein/prekallikrein in these regions suggest that these may be induced by atheromatous disease.