title: Extrarenal angiotensin-forming enzymes.
abstract: There are two types of enzymes in tissues leading to angiotensin formation: a) those resulting in the formation of angiotensin I, such as renin and cathepsin D, the presence of which is now well established for brain tissue and b) Those leading to the direct formation of angiotensin II without the angiotensin I step, such as cathepsin G and tonin. Recent findings concerning tonin, a serine protease, are described: a) 80% of its amino acid sequence, b) its different characteristics from other serine proteases, from renin, cathepsin D and the angiotensin I converting enzyme, c) the activation of inactive renin, d) its involvement in the 1K-1C hypertensive rats, e) the demonstration of its presence in the distal tubular cells of the rat kidney, and finally, f) its presence in urine and the influence of age and of sodium intake on its urinary excretion.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000803:Angiotensin I / Q000096:biosynthesis; D000804:Angiotensin II / Q000096:biosynthesis*; D055598:Chemical Phenomena; D002621:Chemistry; D010450:Endopeptidases / Q000378:metabolism; D004789:Enzyme Activation; D006801:Humans; D066298:In Vitro Techniques; D009504:Neutrophils / Q000201:enzymology; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism; D012697:Serine Endopeptidases
chemical_list: D000596:Amino Acids; D000804:Angiotensin II; D000803:Angiotensin I; D010450:Endopeptidases; D007703:Peptidyl-Dipeptidase A; D012697:Serine Endopeptidases