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J. Biol. Chem., Vol. 266, Issue 26, 17173-17179, 09, 1991
H Urata, A Kinoshita, DM Perez, KS Misono, FM Bumpus, RM Graham and A Husain
We have recently identified and characterized a chymotrypsin-like serine
proteinase in human heart (human heart chymase) that is the most
catalytically efficient enzyme described, thus far, for the cleavage of
angiotensin I to yield angiotensin II and the dipeptide His-Leu. Compared
to other chymases, this enzyme also has an unusually high degree of
specificity for the substrate angiotensin I. We report here the molecular
cloning and nucleotide sequence of the gene and cDNA encoding human heart
chymase, and determination of its entire deduced amino acid sequence. These
data indicate that human heart chymase is highly homologous to other
members of the chymase subfamily of chymotrypsin-like proteinases and, most
likely, all evolved from a common ancestral gene. Potential regulatory
elements found in the 5'- untranslated region of other chymases are also
found in the human heart chymase gene. However, this gene lacks mast
cell-specific sequences found in the 5'- and 3'-untranslated regions of the
rat chymase II gene. In addition, human heart chymase contains clusters of
unique amino acid sequences located at key positions likely involved in
substrate binding, which may contribute to its high substrate specificity.
These contrasting features of the human heart chymase gene and cDNA, and
the potential determinants of its primary structure that underlie its
unique functional characteristics are considered.
Cloning of the gene and cDNA for human heart chymase
Department of Heart and Hypertension Research, Cleveland Clinic Foundation, Ohio 44195-5069.
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