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J. Biol. Chem., Vol. 265, Issue 36, 22348-22357, Dec, 1990
H Urata, A Kinoshita, KS Misono, FM Bumpus and A Husain
Although angiotensin II (Ang II)-forming enzymatic activity in the human
left cardiac ventricle is minimally inhibited by angiotensin I (Ang I)
converting enzyme inhibitors, over 75% of this activity is inhibited by
serine proteinase inhibitors (Urata, H., Healy, B., Stewart, R. W., Bumpus,
F. M., and Husain, A. (1990) Circ. Res. 66, 883- 890). We now report the
identification and characterization of the major Ang II-forming, neutral
serine proteinase, from left ventricular tissues of the human heart. A
115,150-fold purification from human cardiac membranes yielded a purified
protein with an Mr of 30,000 by sodium dodecyl sulfate-polyacrylamide gel
electrophoresis. Based upon its amino-terminal sequence, the major human
cardiac Ang II-forming proteinase appears to be a novel member of the
chymase subfamily of chymotrypsin-like serine proteinases. Human heart
chymase was completely inhibited by the serine proteinase inhibitors,
soybean trypsin inhibitor, phenylmethylsulfonyl fluoride, and chymostatin.
It was partially inhibited by p-tosyl-L-phenylalanine chloromethyl ketone,
but was not inhibited by p-tosyl-L-lysine chloromethyl ketone, and
aprotinin. Also, human heart chymase was not inhibited by inhibitors of the
other three classes of proteinases. Human heart chymase has a high
specificity for the conversion of Ang I to Ang II and the Ang I-
carboxyl-terminal dipeptide His-Leu (Km = 60 microM; Kcat = 11,900 min- 1;
Kcat/Km = 198 min-1 microM-1). Human heart chymase did not degrade several
peptide hormones, including Ang II, bradykinin, and vasoactive intestinal
peptide, nor did it form Ang II from angiotensinogen. The high substrate
specificity of human heart chymase for Ang I distinguishes it from other
Ang II-forming enzymes including Ang I converting enzyme, tonin,
kallikrein, cathepsin G, and other known chymases.
Identification of a highly specific chymase as the major angiotensin II- forming enzyme in the human heart [published erratum appears in J Biol Chem 1991 Jun 25;266(18):12114]
Department of Heart and Hypertension Research, Cleveland Clinic Foundation, Ohio 44195-5069.
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