90% of angiotensin converting enzyme (ACE) is found locally as tissue-bound ACE on vascular endothelial cells. Recently postulated classification of angiotensin converting enzyme inhibitors (ACE-I) on plasma and tissue ACE-I based on stronger and prolonged inhibition of tissue ACE, connected with their higher penetration to tissues. Tissue ACE-I, through their high affinity to endothelium, considerably stronger prevents the local synthesis of angiotensin II (Ang II) and by inhibition of kininase II causes the subsequent increase of bradykinin level and mediated by BK2 receptor release of nitric oxide (NO), prostacycline (PGI2) and tissue type plasminogen activator (t-PA). Therefore the beneficial consequences of tissue ACE inhibition may improve endothelial dysfunction by prevention of the unfavorable structural and functional changes and modulation the coagulation and fibrinolysis system. In this review authors discuss the hypothesis that tissue ACE-Is more effectively influence haemostasis and prevent thrombosis in comparison to plasma ACE-I.