title: Elucidation of crucial structures for a catechol-based inhibitor of plasma hyaluronan-binding protein (factor VII activating protease) autoactivation.
abstract: Plasma hyaluronan-binding protein (PHBP) is a serine protease the activation of which is implicated in inflammation. Previous investigations have suggested the presence of catechol-binding sites in its proenzyme form, pro-PHBP. Here we found that compounds with plural catechol groups conjugated with strong electron-withdrawing groups, such as tyrphostin AG 537 (IC(50)=18 nM), were potent inhibitors of pro-PHBP activation.
authors: Department of Applied Biological Science, Tokyo University of Agriculture and Technology, Fuchu, Tokyo, Japan.
authors: Eisaku
authors: E
authors: Yamamoto
authors: Yoshikazu
authors: Y
authors: Kitano
authors: Keiji
authors: K
authors: Hasumi
mesh_terms: D002396:Catechols / Q000737:chemistry* / Q000494:pharmacology*; D004789:Enzyme Activation / Q000187:drug effects; D006801:Humans; D011480:Protease Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D012697:Serine Endopeptidases / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D002396:Catechols; D011480:Protease Inhibitors; C433550:HABP2 protein, human; D012697:Serine Endopeptidases; C034221:catechol