Inhibition ofUlmus davidiana Planch (Ulmaceae) on bone resorption mediated by processing of Cathepsin K in cultured mouse osteoclasts

2008 ◽  
Vol 22 (4) ◽  
pp. 511-517 ◽  
Author(s):  
Kyung-Woon Kim ◽  
Jun-Sung Park ◽  
Kap-Sung Kim ◽  
Un-Ho Jin ◽  
June-Ki Kim ◽  
...  
Keyword(s):  
Bone Resorption ◽  
Cathepsin K

A highly potent inhibitor of cathepsin K (relacatib) reduces biomarkers of bone resorption both in vitro and in an acute model of elevated bone turnover in vivo in monkeys

Bone ◽  
2007 ◽  
Vol 40 (1) ◽  
pp. 122-131 ◽  
Author(s):  
S. Kumar ◽  
L. Dare ◽  
J.A. Vasko-Moser ◽  
I.E. James ◽  
S.M. Blake ◽  
...  
Keyword(s):  
Bone Resorption ◽  
Bone Turnover ◽  
Potent Inhibitor ◽  
Cathepsin K

Impaired bone resorption in cathepsin K-deficient mice is partially compensated for by enhanced osteoclastogenesis and increased expression of other proteases via an increased RANKL/OPG ratio

Bone ◽  
2005 ◽  
Vol 36 (1) ◽  
pp. 159-172 ◽  
Author(s):  
Riku Kiviranta ◽  
Jukka Morko ◽  
Sari L. Alatalo ◽  
Roisin NicAmhlaoibh ◽  
Juha Risteli ◽  
...  
Keyword(s):  
Bone Resorption ◽  
Cathepsin K ◽  
Deficient Mice

scholarly journals Cathepsin K Antisense Oligodeoxynucleotide Inhibits Osteoclastic Bone Resorption

1997 ◽  
Vol 272 (13) ◽  
pp. 8109-8112 ◽  
Author(s):  
Takashi Inui ◽  
Osamu Ishibashi ◽  
Tetsuya Inaoka ◽  
Yumi Origane ◽  
Masayoshi Kumegawa ◽  
...  
Keyword(s):  
Bone Resorption ◽  
Cathepsin K ◽  
Osteoclastic Bone Resorption ◽  
Antisense Oligodeoxynucleotide

scholarly journals Peptide Aldehyde Inhibitors of Cathepsin K Inhibit Bone Resorption Both In Vitro and In Vivo

1997 ◽  
Vol 12 (9) ◽  
pp. 1396-1406 ◽  
Author(s):  
Bartholomew J. Votta ◽  
Mark A. Levy ◽  
Alison Badger ◽  
Jeremy Bradbeer ◽  
Robert A. Dodds ◽  
...  
Keyword(s):  
Bone Resorption ◽  
Cathepsin K ◽  
Inhibit Bone Resorption

scholarly journals Advances in the discovery of cathepsin K inhibitors on bone resorption

2018 ◽  
Vol 33 (1) ◽  
pp. 890-904 ◽  
Author(s):  
Jun Lu ◽  
Maolin Wang ◽  
Ziyue Wang ◽  
Zhongqi Fu ◽  
Aiping Lu ◽  
...  
Keyword(s):  
Bone Resorption ◽  
Cathepsin K ◽  
Cathepsin K Inhibitors

Bone Microenvironment Tissue Surrogates Engineered for Reporting of Metastasized Breast Cancer Osteolytic Activity

2014 ◽  
Vol 1625 ◽  
Author(s):  
Jerald E. Dumas ◽  
Akia N. Parks ◽  
Manu O. Platt
Keyword(s):  
Breast Cancer ◽  
Bone Resorption ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Cancer Metastasis ◽  
Osteolytic Lesion ◽  
Cathepsin K ◽  
Mineral Dissolution ◽  
Bone Microenvironment ◽  
Metastatic Niche

ABSTRACTBreast cancer metastasis to bone continues to be a major clinical problem, and patient-to-patient variability in rates of disease progression and metastasis complicate treatment even further. This may be due to differences in the cancer cells, the osteoclasts, or the pre-metastatic niche, but all of these contribute to proteolytic remodeling necessary for osteolytic lesion establishment, primarily through secretion of cathepsin K, the most powerful human collagenase. There is debate about the relative contributions of breast cancer cells and osteoclasts and synergism between the two in altering the biochemical and biomechanical properties of the colonized bone, as these are difficult to parse with animal models. To quantify the relative contributions of breast cancer cells and osteoclasts in bone resorption, we have been developing engineered bone microenvironment tissue surrogates by adapting a poly(ester urethane) urea system embedded with microbone particles. Here, we report their use with MDA-MB-231 breast cancer cells and RAW264.7 derived osteoclasts, to provide temporal, multiscale reporters of bone resorption that can be measured non-destructively: 1) collagen degradation measured by C-terminal collagen fragment release, 2) mineral dissolution by measuring calcium released with the calcium arsenazo assay, and also show their beneficial effects in upregulating cathepsin K expression compared to tissue culture polystyrene controls. These more natural derived bone surrogates may be useful tools in mimicking bone metastatic niche and determining differences between proteolytic activity of different patients’ tumor and bone resident cells in a controlled manner.

scholarly journals Roles of Mitogen-Activated Protein Kinases in Osteoclast Biology

2018 ◽  
Vol 19 (10) ◽  
pp. 3004 ◽  
Author(s):  
Kyunghee Lee ◽  
Incheol Seo ◽  
Mun Choi ◽  
Daewon Jeong
Keyword(s):  
Bone Resorption ◽  
Protein Kinases ◽  
Current Knowledge ◽  
Osteoclast Differentiation ◽  
Cathepsin K ◽  
Proton Pumping ◽  
Mitogen Activated Protein Kinases ◽  
Extracellular Signal ◽  
Mitogen Activated Protein ◽  
Inorganic Mineral

Bone undergoes continuous remodeling, which is homeostatically regulated by concerted communication between bone-forming osteoblasts and bone-degrading osteoclasts. Multinucleated giant osteoclasts are the only specialized cells that degrade or resorb the organic and inorganic bone components. They secrete proteases (e.g., cathepsin K) that degrade the organic collagenous matrix and establish localized acidosis at the bone-resorbing site through proton-pumping to facilitate the dissolution of inorganic mineral. Osteoporosis, the most common bone disease, is caused by excessive bone resorption, highlighting the crucial role of osteoclasts in intact bone remodeling. Signaling mediated by mitogen-activated protein kinases (MAPKs), including extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38, has been recognized to be critical for normal osteoclast differentiation and activation. Various exogenous (e.g., toll-like receptor agonists) and endogenous (e.g., growth factors and inflammatory cytokines) stimuli contribute to determining whether MAPKs positively or negatively regulate osteoclast adhesion, migration, fusion and survival, and osteoclastic bone resorption. In this review, we delineate the unique roles of MAPKs in osteoclast metabolism and provide an overview of the upstream regulators that activate or inhibit MAPKs and their downstream targets. Furthermore, we discuss the current knowledge about the differential kinetics of ERK, JNK, and p38, and the crosstalk between MAPKs in osteoclast metabolism.

scholarly journals Expression of the Proteinase Specialized in Bone Resorption, Cathepsin K, in Granulomatous Inflammation

2000 ◽  
Vol 6 (8) ◽  
pp. 648-659 ◽  
Author(s):  
Alvaro Díaz ◽  
Antony C. Willis ◽  
Robert B. Sim
Keyword(s):  
Bone Resorption ◽  
Granulomatous Inflammation ◽  
Cathepsin K
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