Relevant bibliographies by topics / Inhibiteur de cathepsine K

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Academic literature on the topic 'Inhibiteur de cathepsine K'

Author: Grafiati
Published: 4 June 2021
Last updated: 18 February 2022

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Journal articles on the topic "Inhibiteur de cathepsine K"

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Chapurlat, Roland. "Les inhibiteurs de la cathepsine K et les anticorps anti-sclérostine. Les prochains traitements de l’ostéoporose ?" Revue du Rhumatisme 83, no. 5 (October 2016): 321–23. http://dx.doi.org/10.1016/j.rhum.2016.07.015.

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Keegan, Philip M., Suhaas Anbazhakan, Baolin Kang, Betty S. Pace, and Manu O. Platt. "Biomechanical and biochemical regulation of cathepsin K expression in endothelial cells converge at AP-1 and NF-κB." Biological Chemistry 397, no. 5 (May 1, 2016): 459–68. http://dx.doi.org/10.1515/hsz-2015-0244.

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Abstract Cathepsins K and V are powerful elastases elevated in endothelial cells by tumor necrosis factor-α (TNFα) stimulation and disturbed blood flow both of which contribute to inflammation-mediated arterial remodeling. However, mechanisms behind endothelial cell integration of biochemical and biomechanical cues to regulate cathepsin production are not known. To distinguish these mechanisms, human aortic endothelial cells (HAECs) were stimulated with TNFα and exposed to pro-remodeling or vasoprotective shear stress profiles. TNFα upregulated cathepsin K via JNK/c-jun activation, but vasoprotective shear stress inhibited TNFα-stimulated cathepsin K expression. JNK/c-jun were still phosphorylated, but cathepsin K mRNA levels were significantly reduced to almost null indicating separate biomechanical regulation of cathepsin K by shear stress separate from biochemical stimulation. Treatment with Bay 11-7082, an inhibitor of IκBα phosphorylation, was sufficient to block induction of cathepsin K by both pro-remodeling shear stress and TNFα, implicating NF-κB as the biomechanical regulator, and its protein levels were reduced in HAECs by vasoprotective shear stress. In conclusion, NF-κB and AP-1 activation were necessary to activate cathepsin K expression in endothelial cells, highlighting integration of biochemical and biomechanical stimuli to control cathepsins K and V, powerful elastases implicated for arterial remodeling due to chronic inflammation and disturbed blood flow.
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James, Ian E., Robert W. Marquis, Simon M. Blake, Shing Mei Hwang, Catherine J. Gress, Yu Ru, Denise Zembryki, et al. "Potent and Selective Cathepsin L Inhibitors Do Not Inhibit Human Osteoclast Resorptionin Vitro." Journal of Biological Chemistry 276, no. 15 (January 8, 2001): 11507–11. http://dx.doi.org/10.1074/jbc.m010684200.

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Cathepsins K and L are related cysteine proteases that have been proposed to play important roles in osteoclast-mediated bone resorption. To further examine the putative role of cathepsin L in bone resorption, we have evaluated selective and potent inhibitors of human cathepsin L and cathepsin K in anin vitroassay of human osteoclastic resorption and anin situassay of osteoclast cathepsin activity. The potent selective cathepsin L inhibitors (Ki= 0.0099, 0.034, and 0.27 nm) were inactive in both thein situcytochemical assay (IC50> 1 μm) and the osteoclast-mediated bone resorption assay (IC50> 300 nm). Conversely, the cathepsin K selective inhibitor was potently active in both the cytochemical (IC50= 63 nm) and resorption (IC50= 71 nm) assays. A recently reported dipeptide aldehyde with activity against cathepsins L (Ki= 0.052 nm) and K (Ki= 1.57 nm) was also active in both assays (IC50= 110 and 115 nm, respectively) These data confirm that cathepsin K and not cathepsin L is the major protease responsible for human osteoclastic bone resorption.
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Coppini, Larissa P., Nilana M. T. Barros, Marcela Oliveira, Izaura Y. Hirata, Marcio F. M. Alves, Thaysa Paschoalin, Diego M. Assis, et al. "Plasminogen hydrolysis by cathepsin S and identification of derived peptides as selective substrate for cathepsin V and cathepsin L inhibitor." Biological Chemistry 391, no. 5 (May 1, 2010): 561–70. http://dx.doi.org/10.1515/bc.2010.049.

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Abstract Plasminogen is a glycoprotein implicated in angiogenesis and fibrin clot degradation associated with the release of angiostatin and plasmin activation, respectively. We have recently reported that cathepsin V, but not cathepsins L, B, and K, can release angiostatin-like fragments from plasminogen. Here, we extended the investigation to cathepsin S which has been implicated in angiogenesis and tumor cell proliferation. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of plasminogen hydrolysis by cathepsin S revealed generation of two fragments (60 and 38 kDa). Amino-terminal sequencing indicated that cleavage occurs at the Leu469-Leu470 peptide bond. In contrast to cathepsin V, which possesses antiangiogenic activity, cathepsin S plasminogen cleavage products were not capable of inhibiting angiogenesis on endothelial cells. Moreover, we explored the different selectivities presented by cathepsins V and S towards plasminogen and synthesized fluorescence resonance energy transfer peptides encompassing the hydrolyzed peptide bonds by both enzymes. The peptide Abz-VLFEKKQ-EDDnp (Abz=ortho-aminobenzoic acid; EDDnp= N-[2,4-dinitrophenyl]ethylenediamine), hydrolyzed by cath-epsin V at the Phe-Glu bond, is a selective substrate for the enzyme when compared with cathepsins B, L, and S, whereas Abz-VLFEKKVYLQ-EDDnp is an efficient cathepsin L inhibitor. The demonstrated importance of the S3′-P3′ interaction indicates the significance of the extended subsites for enzyme specificity and affinity.
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LECAILLE, Fabien, Enrico WEIDAUER, Maria A. JULIANO, Dieter BRÖMME, and Gilles LALMANACH. "Probing cathepsin K activity with a selective substrate spanning its active site." Biochemical Journal 375, no. 2 (October 15, 2003): 307–12. http://dx.doi.org/10.1042/bj20030468.

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The limited availability of highly selective cathepsin substrates seriously impairs studies designed to monitor individual cathepsin activities in biological samples. Among mammalian cysteine proteases, cathepsin K has a unique preference for a proline residue at P2, the primary determinant of its substrate specificity. Interestingly, congopain from Trypanosoma congolense also accommodates a proline residue in its S2 subsite. Analysis of a congopain model showed that amino acids forming its S2 subsite are identical with those of cathepsin K, except Leu67 which is replaced by a tyrosine residue in cathepsin K. Furthermore, amino acid residues of the congopain S2′ binding pocket, which accepts a proline residue, are strictly identical with those of cathepsin K. Abz-HPGGPQ-EDN2ph [where Abz represents o-aminobenzoic acid and EDN2ph (=EDDnp) represents N-(2,4-dinitrophenyl)-ethylenediamine], a substrate initially developed for trypanosomal enzymes, was efficiently cleaved at the Gly–Gly bond by cathepsin K (kcat/Km=426000 M−1·s−1). On the other hand, Abz-HPGGPQ-EDN2ph was resistant to hydrolysis by cathepsins B, F, H, L, S and V (20 nM enzyme concentration) and the Y67L (Tyr67→Leu)/L205A cathepsin K mutant (20 nM), but still acted as a competitive inhibitor. Taken together, the selectivity of Abz-HPGGPQ-EDN2ph to cathepsin K primarily depends on the S2 and S2′ subsite specificities of cathepsin K and the ionization state of histidine at P3. Whereas Abz-HPGGPQ-EDN2ph was hydrolysed by wild-type mouse fibroblast lysates, its hydrolysis was completely abolished in the cathepsin K-deficient samples, indicating that Abz-HPGGPQ-EDN2ph can be used to monitor selectively cathepsin K activity in physiological fluids and cell lysates.
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Scaffa, P. M. C., C. M. P. Vidal, N. Barros, T. F. Gesteira, A. K. Carmona, L. Breschi, D. H. Pashley, et al. "Chlorhexidine Inhibits the Activity of Dental Cysteine Cathepsins." Journal of Dental Research 91, no. 4 (January 19, 2012): 420–25. http://dx.doi.org/10.1177/0022034511435329.

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The co-expression of MMPs and cysteine cathepsins in the human dentin-pulp complex indicates that both classes of enzymes can contribute to the endogenous proteolytic activity of dentin. Chlorhexidine (CHX) is an efficient inhibitor of MMP activity. This study investigated whether CHX could also inhibit cysteine cathepsins present in dentin. The inhibitory profile of CHX on the activity of dentin-extracted and recombinant cysteine cathepsins (B, K, and L) was monitored in fluorogenic substrates. The rate of substrate hydrolysis was spectrofluorimetrically measured, and inhibitory constants were calculated. Molecular docking was performed to predict the binding affinity between CHX and cysteine cathepsins. The results showed that CHX inhibited the proteolytic activity of dentin-extracted cysteine cathepsins in a dose-dependent manner. The proteolytic activity of human recombinant cathepsins was also inhibited by CHX. Molecular docking analysis suggested that CHX strongly interacts with the subsites S2 to S2′ of cysteine cathepsins B, K, and L in a very similar manner. Taken together, these results clearly showed that CHX is a potent inhibitor of the cysteine cathepsins-proteolytic enzymes present in the dentin-pulp complex.
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Prunk, Mateja, Milica Perišić Nanut, Tanja Jakoš, Jerica Sabotič, Urban Švajger, and Janko Kos. "Extracellular Cystatin F Is Internalised by Cytotoxic T Lymphocytes and Decreases Their Cytotoxicity." Cancers 12, no. 12 (December 6, 2020): 3660. http://dx.doi.org/10.3390/cancers12123660.

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Cystatin F is a protein inhibitor of cysteine cathepsins, peptidases involved in the activation of the effector molecules of the perforin/granzyme pathway. Cystatin F was previously shown to regulate natural killer cell cytotoxicity. Here, we show that extracellular cystatin F has a role in regulating the killing efficiency of cytotoxic T lymphocytes (CTLs). Extracellular cystatin F was internalised into TALL-104 cells, a cytotoxic T cell line, and decreased their cathepsin C and H activity. Correspondingly, granzyme A and B activity was also decreased and, most importantly, the killing efficiency of TALL-104 cells as well as primary human CTLs was reduced. The N-terminally truncated form of cystatin F, which can directly inhibit cathepsin C (unlike the full-length form), was more effective than the full-length inhibitor. Furthermore, cystatin F decreased cathepsin L activity, which, however, did not affect perforin processing. Cystatin F derived from K-562 target cells could also decrease the cytotoxicity of TALL-104 cells. These results clearly show that, by inhibiting cysteine cathepsin proteolytic activity, extracellular cystatin F can decrease the cytotoxicity of CTLs and thus compromise their function.
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Altinci, Pinar, Roda Seseogullari-Dirihan, Gulsen Can, David Pashley, and Arzu Tezvergil-Mutluay. "Zinc Inhibits Collagenolysis by Cathepsin K and Matrix Metalloproteinases in Demineralized Dentin Matrix." Caries Research 51, no. 6 (2017): 576–81. http://dx.doi.org/10.1159/000479896.

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The enzymatic degradation of dentin organic matrix occurs via both the action of matrix metalloproteinases (MMPs) and cysteine cathepsins (CCs). Zinc can prevent collagen hydrolysis by MMPs. However, its effect on the activity of dentin-bound CCs is not known. The aim of this study was to investigate the effect of zinc on matrix-bound cathepsin K and MMP activity in dentin. Completely demineralized dentin beams were divided into test groups (n = 9) and incubated at 37°C in an incubation media (1 mL) containing ZnCl2 of 0.02 (physiological level, control), 0.2, 0.5, 1, 5, 10, 20, 30, or 40 mM. The dry mass changes of the beams were determined, and incubation media were analyzed for cathepsin K- and MMP-specific collagen degradation end products - CTX (C-terminal cross-linked telopeptide of type I collagen) and ICTP (cross-linked carboxy-terminal telopeptide of type I collagen) - at 1, 3, and 7 days of incubation. The mass loss of the beams decreased when the zinc level in the incubation media was ≥5 mM (p < 0.05). The release of liberated collagen degradation telopeptides decreased in accordance with the decrease in the mass loss rates of the beams. Cathepsin K-induced dentin collagen degradation can be strongly inhibited by zinc. Zinc levels of ≥5 mM can be considered as a reliable threshold for the stabilization of dentin matrices.
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Herroon, Mackenzie K., Rajgopal Sharma, Erandi Rajagurubandara, Claudia Turro, Jeremy J. Kodanko, and Izabela Podgorski. "Photoactivated inhibition of cathepsin K in a 3D tumor model." Biological Chemistry 397, no. 6 (June 1, 2016): 571–82. http://dx.doi.org/10.1515/hsz-2015-0274.

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Abstract Collagenolytic activity of cathepsin K is important for many physiological and pathological processes including osteoclast-mediated bone degradation, macrophage function and fibroblast-mediated matrix remodeling. Here, we report application of a light-activated inhibitor for controlling activity of cathepsin K in a 3D functional imaging assay. Using prostate carcinoma cell line engineered to overexpress cathepsin K, we demonstrate the utility of the proteolytic assay in living tumor spheroids for the evaluation and quantification of the inhibitor effects on cathepsin K-mediated collagen I degradation. Importantly, we also show that utilizing the ruthenium-caged version of a potent nitrile cathepsin K inhibitor (4), cis-[Ru(bpy)2(4)2](BF4)2 (5), offers significant advantage in terms of effective concentration of the inhibitor and especially its light-activated control in the 3D assay. Our results suggest that light activation provides a suitable, attractive approach for spatial and temporal control of proteolytic activity, which remains a critical, unmet need in treatment of human diseases, especially cancer.
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Roy, A., F. Gosselin, P. O’Shea, and C.-y. Chen. "Synthesis of a Cathepsin K Inhibitor." Synfacts 2006, no. 11 (November 2006): 1095. http://dx.doi.org/10.1055/s-2006-949394.

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Dissertations / Theses on the topic "Inhibiteur de cathepsine K"

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Ren, Zhongyuan. "Small molecules regulated bone resorption and enzyme activity in osseous cells." Thesis, Lyon 1, 2014. http://www.theses.fr/2014LYO10291/document.

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La Cathepsine K est parmi la plus efficace des collagénases de mammifère pour cliver la triple hélice de collagène de type-1. Nous avons développé une série d'azanitriles, (CKI-8 and CKI-13) inhibiteurs de cathepsine K. CKI-8 (un isomère de CKI-13) et CKI-13 ne sont pas toxiques sur les osteoblastes Saos-2 et les cellules RAW 264.7 jusqu' à une concentration de 1000 nM, tandis qu'ils ne le sont pas jusqu'à une concentration de 100 nM sur les osteoclastes. CKI-8 n'affecte pas l'activité de la phosphatase alkaline ainsi que la minéralisation induite par les Saos-2 et par les osteoblastes primaires. CKI-13 diminue de 35 % la minéralisation induite par les Saos-2 tandis qu'il n'affecte pas la minéralisation induite par les osteoblastes primaires. L'addition de CKI-13 diminue l'activité de la phosphatase alkaline d'environ 20% (Saos-2) et de 40 % (osteoblastes primaires). La résorption osseuse sur des tranches d'os d'origine bovine est diminuée avec 10 nM de CKI-13, 100 nM de CKI- 8 et 100 nM d'inhibiteur commercial E64. CKI-8 et CKI-13 diminuent la mobilité des osteoclastes. Nous avons développé un dosage d'hydrolyse de PPi par la phosphatase alkaline au moyen de l'IR, ayant l'avantage de fonctionner sur des vésicules matricielles et des cellules avec des substrats naturels à un pH physiologique. La bande de PPi localisée à 1107 cm-1 (∑= 2158 ± 211 M-1.cm-1) et celles de Pi localisées à 1076 cm-1 (∑= 1346 ± 116 M-1.cm- 1) et à 991 cm-1 (∑= 493 ± 49 M-1.cm-1) ont servis à mesurer les concentrations du substrat et du produit
Cathepsin K is among the most potent mammalian collagenase, capable of cleaving the triple helix in type-I collagen. We developed a series of azanitriles (CKI-8 and CKI-13) which are inhibitors of cathepsin K. CKI-8 (an isomer of CKI-13) and CKI-13 did not induce significant toxicity on osteoblasts Saos-2 and RAW 264.7 cells up to 1000 nM, while they were not toxic on mature osteoclasts up to 100 nM. Commercial E64 inhibitor was not toxic in primary osteoclast cells up to 1000 nM. CKI-8 did not affect alkaline phosphatase activity as well the mineralization induced by Saos-2 cells and by primary osteoblasts. CKI-13 decreased by 35% the mineralization induced by Saos-2 cells while it did not on mineralization induced by primary osteoblasts. Addition of CKI-13 decreased alkaline phosphatase activity by around 20% (Saos-2 cells) and 45% (primary osteoblasts). Bone resorption on bovine slices decreased significantly with 10 nM of CKI-13, with 100 nM of CKI-8 and commercial inhibitor E64. Our findings indicated that CKI-8 and CKI-13 inhibited bone resorption and affected the mobility of osteoclast. To monitor directly the PPi hydrolytic activity by alkaline phosphatase, we developed an infrared (IR) assay taking the advantage to use natural substrate under physiological pH in matrix vesicles and in living cells. PPi band located at 1107 cm-1 (∑= 2158 ± 211 M-1.cm-1) and Pi bands located at 1076 cm-1 (∑= 1346 ± 116 M-1.cm-1) and at 991 cm-1 (∑= 493 ± 49 M-1.cm-1) served to measure the substrate and the product concentrations
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Wartenberg, Mylène. "Régulation de l'activité protéolytique des cathepsines à cystéine S et K par des inactivateurs/inhibiteurs chimiques et pseudopeptidiques." Thesis, Tours, 2018. http://www.theses.fr/2018TOUR3318.

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La cathepsine (Cat) S est une protéase ciblée pour le développement de médicaments utilisés dans les maladies auto-immunes ou la douleur neuropathique. Elle joue également un rôle clé durant l’emphysème compte tenu de ses propriétés élastinolytiques. La Cat K, qui est une collagénase impliquée dans la résorption osseuse, représente une cible pertinente dans le traitement de l’ostéoporose et des métastases osseuses. De plus ces deux protéases sont des protagonistes majeurs du remodelage matriciel et l’homéostasie pulmonaire. Lors de la BPCO, la dégradation tissulaire bronchique est associée à une réaction inflammatoire qui s’accompagne d’un stress oxydatif et d’un déséquilibre de la balance protéases/antiprotéases. L'exposition à la fumée de cigarette constitue le principal facteur de risque dans la BPCO. Malgré la présence d'une cystéine nucléophile (Cys25) dans son site actif, nous avons constaté que la Cat S conserve partiellement son activité enzymatique après exposition à la fumée de cigarette. Ainsi, nous avons exploré les mécanismes soutenant la stabilité de la Cat S, en présence d’oxydants majeurs de la fumée de cigarette : peroxyde d’hydrogène, formaldéhyde, acroléine et peroxynitrite. Par ailleurs, dans le but de réguler l'activité des cathepsines à cystéine K et S, nous avons développé des inhibiteurs pseudopeptidiques de nouvelle génération dérivés de séquences substrats des cathepsines S et K ainsi que des dérivés triazines
Cathepsin (Cat) S is an attractive target for drugs in autoimmune diseases or neuropathic pain. Moreover Cat S plays a key role during emphysema according to its potent elastinolytic activity. Cat K is a critical bone-resorbing collagenase and is a relevant target for the treatment of osteoporosis and bone metastasis. Both enzymes play a key role in matrix remodeling and pulmonary homeostasis. During COPD, the degradation of pulmonary parenchyma depends on inflammatory reactions associated with oxidative stress and proteases/antiproteases imbalance. Exposure to cigarette smoke, a major source of oxidants, is the main risk factor for COPD. Despite the presence of a nucleophilic cysteine (Cys25) within its active site, we found that CatS preserved partially its proteolytic activity after exposure to cigarette smoke extract (CSE). Thus, we have explored molecular mechanisms supporting this stability in the presence of selected major CSE oxidants: hydrogen peroxide, formaldehyde, acrolein and peroxynitrite. In the other hand, we have designed innovative pseudopeptidic inhibitors derived from selective substrates of cathepsin S and K as well triazine derivatives in order to regulate the activity of cathepsins K and S
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Le, Gall Céline. "Évaluation préclinique de nouvelles therapies ciblant les ostéoclastes dans le traitement des métastases osseuses du cancer du sein." Lyon 1, 2007. http://tel.archives-ouvertes.fr/docs/00/26/21/24/PDF/manuscrit_de_these.pdf.pdf.

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Les bisphosphonates (BPs) sont des outils thérapeutiques de choix pour le traitement de l'ostéolyse maligne. Toutefois, ils n'ont pas d'effet anti-tumoral et n'améliorent pas la survie des patients. C'est pourquoi nous avons testé leur efficacité en association avec de nouveaux agents pharmacologiques ciblant les cellules responsables de la résorption osseuse, les ostéoclastes. Nous avons ainsi démontré qu'un inhibiteur de cathepsine K (CKI) réduit l'activité des ostéoclastes in vitro, et de ce fait, le développement des métastases osseuses in vivo en agissant indirectemnet sur les cellules tumorales. De plus, un inhibiteur de tyrosine kinase (Imatinib) ralentit la formation et la progression des métastases osseuses in vivo, en ayant une activité anti-ostéoclastique et anti-tumorale. Toutefois, bien qu'une polythérapie puisse favoriser une synergie d'action entre les médicaments, nos résultats montrent que dans nos conditions d'utilisation, aucune synergie significative entre le CKI, l'Imatinib et le BP zolédronate n'a lieu
Bisphosphonates (BPs) are therapeutics tools of choice to treat malignant osteolysis. However, they don't have antitumor effects and do not provide a life prolonging benefit to patients. That's why we have tested their efficacy in association with new pharmacological agents targeting osteoclasts, the cells responsible of bone resorption. We demonstrated that a cathepsin K inhibitor (CKI) decreases osteoclasts activity in vitreo,and so, bone metastases development in vivo by acting indirectly on tumor cells. Furthermore, a tyrosine kinase inhibitor (Imatinib) decreases bone metastases formation and progression in vivo, by antiosteoclastic and antitumor activities. Howerver, although polytherapy can promote an action synergy between drugs, our results demonstrated that in our conditions of use, no significative synergy was seen between CKI, Imatinib, and the BP zoledronate
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Le, Gall Céline. "ÉVALUATION PRECLINIQUE DE NOUVELLES THERAPIES CIBLANT LES OSTEOCLASTES DANS LE TRAITEMENT DES METASTASES OSSEUSES DU CANCER DU SEIN." Phd thesis, Université Claude Bernard - Lyon I, 2007. http://tel.archives-ouvertes.fr/tel-00262124.

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Les bisphosphonates (BPs) sont des outils thérapeutiques de choix pour le traitement de l'ostéolyse maligne. Toutefois, ils n'ont pas d'effet anti-tumoral et n'améliorent pas la survie des patients. C'est pourquoi nous avons testé leur efficacité en association avec de nouveaux agents pharmacologiques ciblant les cellules responsables de la résorption osseuse, les ostéoclastes.
Nous avons ainsi démontré qu'un inhibiteur de cathepsine K (CKI) réduit l'activité des ostéoclastes in vitro, et de ce fait, le développement des métastases osseuses in vivo en agissant indirectement sur les cellules tumorales. De plus, un inhibiteur de tyrosine kinase (Imatinib) ralentit la formation et la progression des métastases osseuses in vivo, en ayant une activité anti-ostéoclastique et anti-tumorale. Toutefois, bien qu'une polythérapie puisse favoriser une synergie d'action entre les médicaments, nos résultats montrent que dans nos conditions d'utilisation, aucune synergie significative entre le CKI, l'Imatinib et le BP zolédronate n'a lieu.
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Naour, Nadia. "Implication physiopathologique des cathepsines S, K, L et de leur inhibiteur endogène, la cystatine C, dans l'obésité et ses complications." Paris 6, 2009. http://www.theses.fr/2009PA066525.

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Parmi les adipokines sécrétées par le tissu adipeux figurent des protéases à cystéine de la famille des cathepsines. L’enjeu de mon travail de thèse a été d’analyser l’importance relative de trois cathepsines S, L et K et de leur inhibiteur endogène, la cystatine C, dans la physiopathologie de l’obésité. Nos résultats montrent que le tissu adipeux humain est une source de cystatine C, produite en quantité plus élevée chez l’obèse. Ainsi, la cystatine C peut être considérée comme une adipokine dont la production est dérégulée dans l’obésité. Nous avons comparé l’expression des cathepsines S, L et K dans le tissu adipeux d’un même sujet. Nous montrons que seule la cathepsine S est surexprimée dans le tissu adipeux du sujet obèse et diminuée après perte de poids, avec des modifications parallèles des concentrations circulantes. Enfin, nous montrons que l’absence de cathepsine S chez la souris provoque une amélioration de l’homéostasie glucidique. En conclusion, ces travaux suggèrent que la cathepsine S est plus modulable que les cathepsines K et L par les variations de la balance énergétique chez l’homme. L’augmentation concomitante de la cystatine C représente potentiellement un mécanisme compensatoire visant à réduire l’impact de la cathepsine S chez le sujet obèse. Cette protéase reste néanmoins une cible potentielle dont l’inhibition pourrait améliorer l’homéostasie glucidique chez la personne obèse.
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Keppler, Daniel. "Etude chez l'homme d'une cathepsine b particuliere aux cancers." Paris 6, 1988. http://www.theses.fr/1988PA066327.

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Purification et caracterisation de la cathepsine b tumorale et de ses precurseurs a partir d'une ascite cancereuse. Etude des interactions de la cathepsine avec les inhibiteurs endogenes specifiques des cysteine-proteases. Detection et localisation des cathepsines dans divers adenocarcinomes du colon chez l'homme
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TOURNU, CECILE. "Controle nutritionnel de l'expression des cathepsines dans des fibroblastes transformes par l'oncogene k-ras : role du glucose." Clermont-Ferrand 1, 1998. http://www.theses.fr/1998CLF1MM04.

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Lutgens, Suzanne Paulina Maria. "Functional genomics in atherosclerosis: focus on cathepsin K." Maastricht : Maastricht : Universitaire Pers Maastricht ; University Library, Universiteit Maastricht [host], 2007. http://arno.unimaas.nl/show.cgi?fid=9378.

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Nolibe, Anne-Laure. "Etude du pouvoir inhibiteur du sérum d'insuffisants rénaux sur la pompe Na-K-ATPase." Bordeaux 2, 1996. http://www.theses.fr/1996BOR2P097.

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Duplat, Denis. "Identification et caractérisation des molécules de la matrice organique de la nacre de l'huître Pinctada margaritifera, actives sur les cellules de la lignée ostéoclastique." Paris, Muséum national d'histoire naturelle, 2007. http://www.theses.fr/2007MNHN0018.

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La nacre comme l'os est une structure squelettique biominéralisée, composée d'une matrice organique et de minéral. Il a été démontré que la nacre de la coquille de l'huître Pinctada margaritifera contient dans sa fraction organique des molécules hydrosolubles qui stimulent l'activité du tissu osseux en agissant sur la différenciation des ostéoblastes (cellules formatrices d'os) et la minéralisation. Nous avons démontré dans cette étude que la matrice organique de la nacre contient également des molécules signal actives sur les cellules de la lignée ostéoclastique ce qui explique l'activité de la nacre sur le remodelage osseux. Les résultats font apparaître trois groupes de molécules d'intérêt: des molécules de faibles masses moléculaires apparentes qui stimulent la différenciation des ostéoclastes; des molécules associées à une fraction de haute masse moléculaire apparente qui inhibent la différenciation des ostéoclastes et des molécules inhibitrices de protéases à cystéine et particulièrement de la cathepsine K humaine, protéase essentielle de la résorption ostéoclastique. Au total, 15 protéines spécifiquement exprimées par les cellules responsables de la biominéralisation de la nacre sont caractérisées : 13 protéines de structure de la matrice organique de la nacre et 2!protéines intracellulaires impliquées dans la régulation de la biominéralisation, l'une au niveau de la mobilisation du calcium et l'autre par une activité inhibitrice de protéases. Les séquences des protéines de structure caractérisées suggèrent qu'elles possèderaient d'intéressantes propriétés d'agrégation et participeraient de ce fait à la réticulation de la trame organique de la nacre et à l'adsorption de molécules de faible masse moléculaire, mobilisables et porteuses de l'activité biologique. Le potentiel d'application de ces recherches dans les domaines industriels liés à la santé a conduit à la protection des molécules valorisables par le dépôt de 3 brevets
Mother-of-pearl, from the shellfish Pinctada margaritifera, like bone in vertebrates is made-up of an organic matrix and mineral. Nacre water-soluble organic matrix was previously shown, by in vitro and in vivo experiments, to contain signal molecules that stimulate bone tissue, especially osteoblastic differentiation and mineralization. These studies demonstrate the presence of signal molecules, in the nacre organic matrix, active on osteoclasts, the bone resorbing cells, explaining the outcome of bone remodeling. Nacre water-soluble matrix contains 3 groups of significant molecules: low-molecular weight molecules stimulating osteoclastic differentiation, molecules within the high-molecular weight fraction of nacre organic matrix inhibiting osteoclastic differentiation and molecules inhibiting cysteine proteases and particularly cathepsin K, the main hydrolytic protease in bone resorbing cells. Fifteen proteins specifically expressed by the nacre-forming cells have been characterized : 13!proteins scaffolding the nacre organic matrix and 2 proteins involved in the control of biomineralization, calcium transport and protease inhibition. The matrix proteins characterized in these studies can form aggregates and thus contribute in threading the cross-linked network of the nacre organic matrix and in maintaining inside, the diffusible low-molecular weight molecules bearing the biological activity. The high rate of valuation of this research for health industry leads to the deposit of 3 patents
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Book chapters on the topic "Inhibiteur de cathepsine K"

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Veber, Daniel F. "Factors that influence oral bioavailability; A cathepsin K inhibitor for human studies." In Advances in Experimental Medicine and Biology, 607–10. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-0-387-73657-0_263.

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Truppo, Matthew D. "An Efficient, Asymmetric Synthesis of Odanacatib, a Selective Inhibitor of Cathepsin K for the Treatment of Osteoporosis, Using an Enzyme-Mediated Dynamic Kinetic Resolution." In Asymmetric Catalysis on Industrial Scale, 397–414. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2010. http://dx.doi.org/10.1002/9783527630639.ch22.

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Conference papers on the topic "Inhibiteur de cathepsine K"

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Fasanya, Henrietta, and Dietmar Siemann. "Abstract 4899: The small molecule cathepsin L and K inhibitor KGP-94 impairs the metastatic phenotype of osteosarcoma cells." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-4899.

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Jensen, AB, C. Wynne, G. Ramirez, L. Antje, O. Nina, A. Mehta, H. Wang, et al. "Suppression of bone resorption from odanacatib, a cathepsin K inhibitor, in women with bone metastases from breast cancer, and the effect of concomitant anti-neoplastic treatment on efficacy: a 4-week, double-blind, randomized controlled trial." In CTRC-AACR San Antonio Breast Cancer Symposium: 2008 Abstracts. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/0008-5472.sabcs-1157.

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