Secretion and processing mechanisms of procathepsin L in bone resorption

FEBS Letters

Kakegawa, Hisao¹  Sumitani, Koji²  Kawata, Terushige²  Ohba, Yasuo²  Tagami, Kahori²  Katunumaa, Nobuhiko¹ 

[1]Institute for Health Sciences, Tokushima Bunri University, Yamashiro-cho, Tokushima 770, Japan

[2]Department of Orthodontics, School of Dentistry, The University of Tokushima, Kuramoto-cho, Tokushima 770, Japan

关键词: Procathepsin L;    Cysteine proteinase;    Bone resorption;    PTH;    1α25-(OH)2D3;    TNFα;    Z;    benzyloxycarbonyl;    MCA;    methylcoumaryl-amide;    E-64-a;    CA-074;    Enzyme;    cathepsin L;    EC 3.4.22.15;   

DOI  :  10.1016/0014-5793(95)00790-G

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Secretion of procathepsin L into the culture medium from a bone cell mixture was markedly enhanced by addition parathyroid hormone (PTH), 1α,25-(OH)₂D₃ or tumor necrosis factor α (TNF_α). These stimulators of secretion of procathepsin L enhanced bone pit formation, which was inhibited by E-64, but not by CA-074, a specific inhibitor of cathepsin B. Procathepsin L may thus participate in the process of bone collagenolysis during bone resorption. Procathepsin L partially purified from rat long bones under cold conditions was rapidly converted to the mature form under acidic conditions at room temperature. This conversion was inhibited by E-64, suggesting that the procathepsin L secreted into lacunae is catalytically converted to the mature enzyme by cysteine proteinase(s).

【 授权许可】

Unknown