Abstract
The secretion mechanisms of cathepsin L from osteoclasts in the process of bone resorption were investigated. The increases in bone pit numbers formed take place by PTH addition in parallel with the increases of cathepsin L and/or L-like proteinase activities in the culture medium of bone cells, and these were suppressed by the addition ofcalcitonin. The Z-Phe-Arg-MCA hydrolysing activity increased in the medium through the effect of PTH is considered to be a kind of procathepsin L by Western blotting analysis, and was suppressed by calcitonin addition. Furthermore, monensin inhibited not only the PTH-induced pit formation, but also cysteine proteinase activity in osteoclasts. Therefore, the procathepsin L excreted might be transferred from endothelial reticulum via Golgi and/or via lysosomes.
Original language | English |
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Pages (from-to) | 308-312 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 342 |
Issue number | 3 |
DOIs | |
Publication status | Published - Apr 11 1994 |
Externally published | Yes |
Keywords
- Bone resorption
- Calcitonin
- Cysteine proteinase
- Monensin
- Parathyroid hormone
- Procathepsin L
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology