Rapid inactivation of endothelin-1 by a carboxypeptidase-like enzyme purified from rat kidney.
A survey of various rat tissues showed that the kidney had the highest endothelin degradation enzyme activity. An enzyme that effectively inactivated endothelin-1 was purified from soluble kidney extracts. This enzyme appeared to contain two subunits with molecular weights of 34 kDa and 21 kDa. It displayed carboxypeptidase-like properties and cleaved off the carboxyl terminal tryptophan of endothelin-1. These results agree with the findings that endothelin-1 is cleared efficiently by the kidney and suggest that this enzyme plays a role in the homeostasis of circulating endothelin-1.
Jeng
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AY
Research Department, Ciba-Geigy Corp., Summit, New Jersey 07901.
Deng
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D002268:Carboxypeptidases / Q000302:isolation & purification / Q000378:metabolism*; D016232:Endothelins / Q000378:metabolism* / Q000494:pharmacology; D066298:In Vitro Techniques; D007668:Kidney / Q000201:enzymology*; D008297:Male; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009119:Muscle Contraction / Q000187:drug effects; D009131:Muscle, Smooth, Vascular / Q000187:drug effects; D011817:Rabbits; D051381:Rats; D017207:Rats, Sprague-Dawley; D016339:Spectrometry, Mass, Fast Atom Bombardment
D016232:Endothelins; D002268:Carboxypeptidases