Secretion and processing mechanisms of procathepsin L in bone resorption
| Autor: | Kahori Tagami, Yasuo Ohba, Koji Sumitani, Terushige Kawata, Hisao Kakegawa, Nobuhiko Katunumaa |
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| Rok vydání: | 1995 |
| Předmět: |
Male
Cathepsin L Parathyroid hormone Biochemistry Cysteine Proteinase Inhibitors Rats Sprague-Dawley Structural Biology Teriparatide Bone cell TNFα Cells Cultured Enzyme Precursors biology Chemistry Dipeptides Cysteine Endopeptidases Parathyroid Hormone Electrophoresis Polyacrylamide Gel PTH medicine.drug medicine.medical_specialty Calcitriol Blotting Western Biophysics Cysteine proteinase 1α25-(OH)2D3 Bone and Bones Bone resorption Leucine Internal medicine Endopeptidases Genetics medicine Animals Humans Secretion Bone Resorption Molecular Biology Cathepsin Tumor Necrosis Factor-alpha Cell Biology Cathepsins Molecular biology Peptide Fragments Rats Endocrinology biology.protein Calcium Protein Processing Post-Translational Procathepsin L |
| Zdroj: | FEBS Letters. 370:78-82 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(95)00790-g |
| Popis: | Secretion of procathepsin L into the culture medium from a bone cell mixture was markedly enhanced by addition of parathyroid hormone (PTH), 1 alpha,25-(OH)2D3 or tumor necrosis factor alpha (TNF alpha). 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: | OpenAIRE |
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