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The mechanisms and regulation of procathepsin L secretion from osteoclasts in bone resorption

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
342
Issue
3
Identifiers
DOI: 10.1016/0014-5793(94)80522-9
Keywords
  • Procathepsin L
  • Cysteine Proteinase
  • Parathyroid Hormone
  • Calcitonin
  • Monensin
  • Bone Resorption
Disciplines
  • Biology

Abstract

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.

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