By Professor Thomas Unger, Professor Bernward A. Schölkens (auth.)
Nearly thirty years in the past, in 1974, the amount on Angiotensin edited via Irvine H.Page and F. Merlin Bumpus extended the instruction manual of Experimental Pharmacology. Even after twenty years the multiplicity of its activities appears to be like to not were absolutely chanced on. to name consciousness to its many services is without doubt one of the reasons of this e-book. This new version of the amount on Angiotensin makes an attempt to supply an up-to-date account of the data and findings gathered because the complexity of angiotensin was once so effectively recognized.
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Extra resources for Angiotensin Vol. II
Circulation 100:1056-1064 Northermann W, Braciak TA, Hattori M, Lee F, Fey GH (1989) Structure of the rat IL-6 gene and its expression in macrophage-derived cells. J Biol Chem 264:16072-16082 Ohishi M, Ueda M, Rakugi H, Naruko T, Kolima A, Okamura A, Higaki J, Ogihara T (1999) Relative localization of angiotensin-converting enzyme, chymase and angiotensin II in human coronary atherosclerotic lesion. J Hypertens 17:547-553 Pagano PJ, Clark JK, Cifuentes-Pagano ME, Clark SM, Callis GM, Quinn MT (1997) Localization of a constitutively active, phagocyte-like NADPH oxidase in rabbit aortic adventitia: enhancement by angiotensin II.
1996). Potter and eo-workers further demonstrated that lipid-laden macrophages contain ANG II in a primate model of atherosclerosis (Potter et al. 1998). In humans, at least two major enzymes-ACE and chymase-are involved in the conversion of ANG-I to ANG-II, and may contribute to ANG II formation in coronary arteries. Further investigations, in normal and atheromatous coronary arterial tissue from patients dying of noncardiovascular diseases, demonstrated that only ACE but not chymase was colocalized with ANG-II in the intima of stable arthrosclerotic plaques (Ohishi et al.
Drexler . B. Schieffer metalloprotease expression and activity. , PAl-I, CRP, metalloproteases). Accumulation of these factors contribute to the subsequent pro-atherogenic potency of ANG II (see Fig. 4). Thus it is suggested that IL-6 induction by ANG II is redox-sensitive and involves the aforementioned signaling cascades. In-fact, recent observations reported that blockade of superoxide anion generation by ANG II abolished ANG Il-induced IL-6 release in vitro . In summary, generation of superoxide anions via the ATl receptor seems to be pivotal for the pro-inflammatory and proatherogenic properties of ANG II.