Study on the Cupric Phenanthoroline-Induced β-Glucuronidase Release in Saponin-Permeabilized Polymorphonuclear Leukocytes

概要

論文の詳細を見る
Saponin-permeabilized polymorphonuclear leukocytes (PMNs) released β-glucuronidase, a lysosomal enzyme, dose-dependently in response to cupric phenanthroline (CuPh), a mild oxidant, which catalyzes the formation of disulfide bridges. The β-glucuronidase release induced by CuPh was inhibited by ehylene glycol bis(β-aminoehylether)-N, N, -N', N'-tetraacetic acid (EGTA). Both dithiothreitol (DTT) and N-(6-aminohexyl)-5-chloro-naphthlelne sulfonamide (W-7) also inhibited the β-glucuronidase release induced by CuPh. CuPh elicited a decrease in protein-bound free sulfhydryls simultaneously, and this decrease was not restored by EGTA treatment. CuPh inhibited Ca^<2+> uptake into Ca^<2+> store sites, and promoted a Ca^<2+> efflux from Ca^<2+> store sites. It also inhibited Ca^<2+>-adenosine triphosphatase (ATPase) activity in permeable PMNs. DTT, a sulfhydryl reducing agent, suppressed both the β-glucuronidase release and the Ca^<2+> uptake in CuPh-treated permeable PMNs. On the other hand, chloromercuriphenylsulfonic acid (CMPS), a sulfhydryl modifier, decreased the amount of free sulfhydryls in protein and released β-glucuronidase in permeable PMNs dose-dependently, but EGTA did not inhibit either reaction. Neither CuPh nor CMPS released β-glucuronidase from intact PMNs. These results indicate that both CuPh and CMPS act on intra-PMN target molecules to exert their influence, but the involved mechanisms are different in nature. Alteration in calcium movement is responsible for the β-glucuronidase release in the CuPh-treated permeable PMNs.
公益社団法人日本薬学会の論文
1991-09-25

Study on the Cupric Phenanthoroline-Induced β-Glucuronidase Release in Saponin-Permeabilized Polymorphonuclear Leukocytes

スポンサーリンク

概要

著者

関連論文

スポンサーリンク