[组织蛋白酶D的激肽原酶活性]

[Kininogenase activity of cathepsins D].

作者信息

Ogloblina O G, Ruanet V V, Kazakova O V, Paskhina T S, Orekhovich V N

出版信息

Biokhimiia. 1980 Dec;45(12):2217-24.

Abstract

The kininogenase activity of highly purified preparations of cathepsins D from human liver and spleen, leukemic infiltrate obtained from patients with myeloic leukemia, and from chicken liver was studied. It was found that pepstatin, a specific inhibitor of carboxylic proteinases, inhibits this activity of cathepsins D. Interaction of chicken liver cathepsin D with human plasma substrate, which is possibly a low molecular weight kininogen (Ks = 1.3.10(-7) M) results in a production of the bradikinin analog methionyl-lysyl-bradikinin. The role of cathepsins D as potent inflammatory agents responsible for the generation of biologically active peptides--mediators of inflammation from the protein substrates including kininogens under desintegration of lysosomes is discussed.

摘要

对来自人肝脏和脾脏的组织蛋白酶D的高纯度制剂、从髓性白血病患者获得的白血病浸润物以及鸡肝脏中的组织蛋白酶D的激肽原酶活性进行了研究。发现羧酸蛋白酶的特异性抑制剂胃酶抑素可抑制组织蛋白酶D的这种活性。鸡肝脏组织蛋白酶D与人血浆底物相互作用，该底物可能是低分子量激肽原（Ks = 1.3×10⁻⁷ M），结果产生了缓激肽类似物甲硫氨酰-赖氨酰-缓激肽。讨论了组织蛋白酶D作为强效炎症介质的作用，其负责在溶酶体解体时从包括激肽原在内的蛋白质底物产生生物活性肽——炎症介质。