Secretion and processing mechanisms of procathepsin L in bone resorption

Autor: Kakegawa, Hisao, Tagami, Kahori, Ohba, Yasuo, Sumitani, Koji, Kawata, Terushige, Katunumaa, Nobuhiko
Zdroj: FEBS Letters; August 1995, Vol. 370 Issue: 1-2 p78-82, 5p
Abstrakt: Secretion of procathepsin L into the culture medium from a bone cell mixture was markedly enhanced by addition parathyroid hormone (PTH), 1α,25‐(OH)2D3or tumor necrosis factor α (TNFα). 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).
Databáze: Supplemental Index