Inhibition of human chymase by suramin.
Chymase is a chymotrypsin-like protease localized in mast cells in complexes with heparin. In the present study, we demonstrated that suramin, a hexasulfonated naphthylurea used as an anti-cancer drug, inhibits the activity of purified human chymase in vitro. The inhibition was ionic-strength-dependent. It was observed that suramin competed with heparin-Sepharose gel for binding to chymase and the inhibition of chymase activity by suramin was partially impaired by heparin. Our results show that suramin may become a prototype of a new type of chymase inhibitor because of its unique character.
Takao
K
K
Department of Pharmacology, Osaka Medical College, Takatsuki, Japan.
Takai
S
S
Ishihara
T
T
Mita
S
S
Miyazaki
M
M
D000970:Antineoplastic Agents / Q000037:antagonists & inhibitors / Q000494:pharmacology*; D053818:Chymases; D006493:Heparin / Q000494:pharmacology; D006801:Humans; D011189:Potassium Chloride / Q000494:pharmacology; D011480:Protease Inhibitors / Q000494:pharmacology*; D012697:Serine Endopeptidases / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology*; D013498:Suramin / Q000037:antagonists & inhibitors / Q000494:pharmacology*
D000970:Antineoplastic Agents; D011480:Protease Inhibitors; D015842:Serine Proteinase Inhibitors; D013498:Suramin; D011189:Potassium Chloride; D006493:Heparin; D012697:Serine Endopeptidases; D053818:Chymases