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1. Bone degradation machinery of osteoclasts : An HIV-1 target that contributes to bone loss

Author

Raynaud-Messina, Brigitte, Bracq, Lucie, Dupont, Maeva, Souriant, Shanti, Usmani, Shariq M., Proag, Amsha, Pingris, Karine, Soldan, Vanessa, Thibault, Christophe, Capilla, Florence, Saati, Talal Al, Gennero, Isabelle, Jurdic, Pierre, Jolicoeur, Paul, Davignon, Jean-Luc, Mempel, Thorsten R., Benichou, Serge, Maridonneau-Parini, Isabelle, and Vérollet, Christel

Published
2018

2. Parathyroid hormone mediates hematopoietic cell expansion through interleukin-6.

Author

Pirih, Flavia Q, Michalski, Megan N, Cho, Sun W, Koh, Amy J, Berry, Janice E, Ghaname, Eduardo, Kamarajan, Pachiyappan, Bonnelye, Edith, Ross, Charles W, Kapila, Yvonne L, Jurdic, Pierre, and McCauley, Laurie K

Subjects
Bone Marrow Cells, Osteoblasts, Animals, Mice, Inbred C57BL, Mice, Parathyroid Hormone, Interleukin-6, Blotting, Western, Flow Cytometry, Reverse Transcriptase Polymerase Chain Reaction, Cell Adhesion, Cell Division, Cell Differentiation, Cell Lineage, Blotting, Western, Inbred C57BL, General Science & Technology
Abstract

Parathyroid hormone (PTH) stimulates hematopoietic cells through mechanisms of action that remain elusive. Interleukin-6 (IL-6) is upregulated by PTH and stimulates hematopoiesis. The purpose of this investigation was to identify actions of PTH and IL-6 in hematopoietic cell expansion. Bone marrow cultures from C57B6 mice were treated with fms-like tyrosine kinase-3 ligand (Flt-3L), PTH, Flt-3L plus PTH, or vehicle control. Flt-3L alone increased adherent and non-adherent cells. PTH did not directly impact hematopoietic or osteoclastic cells but acted in concert with Flt-3L to further increase cell numbers. Flt-3L alone stimulated proliferation, while PTH combined with Flt-3L decreased apoptosis. Flt-3L increased blasts early in culture, and later increased CD45(+) and CD11b(+) cells. In parallel experiments, IL-6 acted additively with Flt-3L to increase cell numbers and IL-6-deficient bone marrow cultures (compared to wildtype controls) but failed to amplify in response to Flt-3L and PTH, suggesting that IL-6 mediated the PTH effect. In vivo, PTH increased Lin(-) Sca-1(+)c-Kit(+) (LSK) hematopoietic progenitor cells after PTH treatment in wildtype mice, but failed to increase LSKs in IL-6-deficient mice. In conclusion, PTH acts with Flt-3L to maintain hematopoietic cells by limiting apoptosis. IL-6 is a critical mediator of bone marrow cell expansion and is responsible for PTH actions in hematopoietic cell expansion.

Published
2010

6. Induction of osteoclastogenesis and bone loss by human autoantibodies against citrullinated vimentin

Author

Harre, Ulrike, Georgess, Dan, Bang, Holger, Bozec, Aline, Axmann, Roland, Ossipova, Elena, Jakobsson, Per-Johan, Baum, Wolfgang, Nimmerjahn, Falk, Szarka, Eszter, Sarmay, Gabriella, Krumbholz, Grit, Neumann, Elena, Toes, Rene, Scherer, Hans-Ulrich, Catrina, Anca Irinel, Klareskog, Lars, Jurdic, Pierre, and Schett, Georg

Subjects
Bone resorption -- Research, Autoantibodies -- Research, Citrulline -- Research, Osteoclasts (Biology) -- Research, Rheumatoid arthritis -- Research, Health care industry
Abstract

Autoimmunity is complicated by bone loss. In human rheumatoid arthritis (RA), the most severe inflamma-tory joint disease, autoantibodies against citrullinated proteins are among the strongest risk factors for bone destruction. We therefore hypothesized that these autoantibodies directly influence bone metabolism. Here, we found a strong and specific association between autoantibodies against citrullinated proteins and serum markers for osteoclast-mediated bone resorption in RA patients. Moreover, human osteoclasts expressed enzymes eliciting protein citrullination, and specific N-terminal citrullination of vimentin was induced during osteoclast differentiation. Affinity-purified human autoantibodies against mutated citrullinated vimentin (MCV) not only bound to osteoclast surfaces, but also led to robust induction of osteoclastogenesis and bone-resorptive activity. Adoptive transfer of purified human MCV autoantibodies into mice induced osteopenia and increased osteoclastogenesis. This effect was based on the inducible release of TNF-[alpha] from osteoclast precursors and the subsequent increase of osteoclast precursor cell numbers with enhanced expression of activation and growth factor receptors. Our data thus suggest that autoantibody formation in response to citrul-linated vimentin directly induces bone loss, providing a link between the adaptive immune system and bone., Introduction RA affects about 1% of the population worldwide and is one of the most destructive diseases in humans (1, 2). Current concepts suggest that RA emerges by complex gene-environment [...]

Published
2012
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12. I[kappa]B kinase [beta] phosphorylates Dok1 serines in response to TNF, IL-1, or [gamma]/radiation

Author

Lee, Sanghoon, Andrieu, Charlotte, Saltel, Frederic, Destaing, Olivier, Auclair, Jessie, Pouchkine, Veronique, Michelon, Jocelyne, Salaun, Bruno, Kobayashi, Ryuji, Jurdic, Pierre, Kieff, Elliott D., and Sylla, Bakary S.

Subjects
Tyrosine -- Research, Cells -- Research, Science and technology
Abstract

Dok1 is an abundant Ras-GTPase-activating protein-associated tyrosine kinase substrate that negatively regulates cell growth and promotes migration. We now find that I[kappa]B kinase [beta] (IKK[beta]) associated with and phosphorylated Dok1 in human epithelial cells and B lymphocytes. IKK[beta] phosphorylation of Dok1 depended on Dok1 [S.sub.439], [S.sub.443], [S.sub.446], and [S.sub.450]. Recombinant IKK[beta] also phosphorylated Dok1 or Dok1 amino acids 430-481 in vitro. TNF-[alpha], IL-1, [gamma] radiation, or IKK[beta] overexpression phosphorylated Dok1 [S.sub.443], [S.sub.446], and [S.sub.450] in vivo, as detected with Dok1 phospho-S site-specific antisera. Moreover, Dok1 with [S.sub.439], [S.sub.443], [S.sub.446], and [S.sub.450] mutated to A was not phosphorylated by IKK[beta] in vivo. Surprisingly, mutant Dok1 [A.sub.439] [A.sub.443], [A.sub.446], and [A.sub.450] differed from wild-type Dok1 in not inhibiting platelet-derived growth factor-induced extracellular signal-regulated kinase 1/2 phosphorylation or cell growth. Mutant Dok1 [A.sub.439], [A.sub.443], [A.sub.446], and [A.sub.450] also did not promote cell motility, whereas wild-type Dok1 promoted cell motility, and Dok1 [E.sub.439], [E.sub.443], [E.sub.446], and [E.sub.450] further enhanced cell motility. These data indicate that IKK[beta] phosphorylates Dok1 [S.sub.439][S.sub.443] and [S.sub.446][S.sub.450] after TNF-[alpha], IL-1, or [gamma]-radiation and implicate the critical Dok1 serines in Dok1 effects after tyrosine kinase activation. NF-[kappa]B | serine phosphorylation | cell migration

Published
2004

20. Comparative transcriptomics reveals RhoE as a novel regulator of actin dynamics in bone-resorbing osteoclasts

Author

Georgess, Dan, Mazzorana, Marlene, Terrado, Jose, Delpart, Chrisitne, Chamot, Christophe, Guasch, Rosa M., Perez-Roger, Ignocia, Jurdic, Pierre, Machuca-Gayet, Irma, Georgess, Dan, Mazzorana, Marlene, Terrado, Jose, Delpart, Chrisitne, Chamot, Christophe, Guasch, Rosa M., Perez-Roger, Ignocia, Jurdic, Pierre, and Machuca-Gayet, Irma

Abstract

The function of osteoclasts (OCs), multinucleated giant cells (MGCs) of the monocytic lineage, is bone resorption. To resorb bone, OCs form podosomes. These are actin-rich adhesive structures that pattern into rings that drive OC migration and into “sealing-zones” (SZs) that confine the resorption lacuna. Although changes in actin dynamics during podosome patterning have been documented, the mechanisms that regulate these changes are largely unknown. From human monocytic precursors, we differentiated MGCs that express OC degradation enzymes but are unable to resorb the mineral matrix. We demonstrated that, despite exhibiting bona fide podosomes, these cells presented dysfunctional SZs. We then performed two-step differential transcriptomic profiling of bone-resorbing OCs versus nonresorbing MGCs to generate a list of genes implicated in bone resorption. From this list of candidate genes, we investigated the role of Rho/Rnd3. Using primary RhoE-deficient OCs, we demonstrated that RhoE is indispensable for OC migration and bone resorption by maintaining fast actin turnover in podosomes. We further showed that RhoE activates podosome component cofilin by inhibiting its Rock-mediated phosphorylation. We conclude that the RhoE-Rock-cofilin pathway, by promoting podosome dynamics and patterning, is central for OC migration, SZ formation, and, ultimately, bone resorption.

Published
2019

21. Podosome organization drives osteoclast-mediated bone resorption

Author

Georgess, Dan, Machuca-Gayet, Irma, Blangy, Anne, Jurdic, Pierre, Georgess, Dan, Machuca-Gayet, Irma, Blangy, Anne, and Jurdic, Pierre

Abstract

Osteoclasts are the cells responsible for physiological bone resorption. A specific organization of their most prominent cytoskeletal structures, podosomes, is crucial for the degradation of mineralized bone matrix. Each podosome is constituted of an F-actin-enriched central core surrounded by a loose F-actin network, called the podosome cloud. In addition to intrinsic actin dynamics, podosomes are defined by their adhesion to the extracellular matrix, mainly via core-linking CD44 and cloud-linking integrins. These properties allow podosomes to collectively evolve into different patterns implicated in migration and bone resorption. Indeed, to resorb bone, osteoclasts polarize, actively secrete protons, and proteases into the resorption pit where these molecules are confined by a podosome-containing sealing zone. Here, we review recent advancements on podosome structure and regulatory pathways in osteoclasts. We also discuss the distinct functions of different podosome patterns during the lifespan of a single osteoclast.

Published
2019

22. Biphasic effects of vitamin D and FGF23 on human osteoclast biology

Author

Georgess, Dan, Machuca-Gayet, Irma, Demoncheaux, Nathalie, Allard, Lise, Coury-Lucas, Fabienne, Jurdic, Pierre, Bacchetta, Justine, Georgess, Dan, Machuca-Gayet, Irma, Demoncheaux, Nathalie, Allard, Lise, Coury-Lucas, Fabienne, Jurdic, Pierre, and Bacchetta, Justine

Abstract

Vitamin D and FGF23 play a major role in calcium/phosphate balance. Vitamin D may control bone resorption but the potential role of FGF23 has never been evaluated. The objective of this study was therefore to compare the effects of vitamin D and FGF23 on osteoclast differentiation and activity in human monocyte-derived osteoclasts. Human monocytes, purified from blood of healthy donors, were incubated with M-CSF and RANKL to obtain mature multinucleated osteoclasts (MNC). Experiments were carried out to assess the effects of FGF23 as compared to native vitamin D (25-D) and active vitamin D (1,25-D) on osteoclast differentiation and on bone-resorbing osteoclast activity. Additional experiments with the pan fibroblast growth factor receptor inhibitor (FGFR-i) were performed. Phosphorylation Akt and Erk pathways were analyzed by Western blot analyses. Both 1,25-D and FGF23, to a lesser extent, significantly inhibited osteoclastogenesis at early stages; when adding FGFR-i, osteoclast formation was restored. Biochemical experiments showed an activation of the Akt and Erk pathways under FGF23 treatment. In contrast, in terms of activity, 1,25-D had no effect on resorption, whereas FGF23 slightly but significantly increased bone resorption; 25-D had no effects on either differentiation or on activity. These data show that 1,25-D inhibits osteoclastogenesis without regulating osteoclast-mediated bone resorption activity; FGF23 has biphasic effects on osteoclast physiology, inhibiting osteoclast formation while stimulating slightly osteoclast activity. These results may be of importance and taken into account in chronic kidney disease when therapies modulating FGF23 are available.

Published
2019

23. Podosome rings generate forces that drive saltatory osteoclast migration

Author

Dan, Georgess, Hu, Shiqiong, Planus, Emmanuelle, Place, Christophe, Wang, Xianghui, Alibiges-Rizo, Corinne, Jurdic, Pierre, Geminard, Jean-Christophe, Mogliner, Alexander, Dan, Georgess, Hu, Shiqiong, Planus, Emmanuelle, Place, Christophe, Wang, Xianghui, Alibiges-Rizo, Corinne, Jurdic, Pierre, Geminard, Jean-Christophe, and Mogliner, Alexander

Abstract

Podosomes are dynamic, actin-containing adhesion structures that collectively self-organize as rings. In this study, we first show by observing osteoclasts plated on bead-seeded soft substrates that podosome assemblies, such as rings, are involved in tension forces. During the expansion of a podosome ring, substrate displacement is oriented outward, suggesting that podosomal structures push the substrate away. To further elucidate the function of forces generated by podosomes, we analyze osteoclast migration. Determining the centers of mass of the whole cell (G) and of actin (P), we demonstrate that osteoclasts migrate by “jumps” and that the trajectories of G and P are strongly correlated. The velocity of the center of mass as a function of time reveals that osteoclasts rapidly catch up with podosomal structures in a periodic pattern. We conclude that actin dynamics inside the cell are not only correlated with cell migration, but drive it.

Published
2019

25. Flt3+ macrophage precursors commit sequentially to osteoclasts, dendritic cells and microglia

Author

Hanau Daniel, Dumontel Christiane, Perret Magali, Rivollier Aymeric, Destaing Olivier, Domenget Chantal, Soulas Caroline, Grasset Marie-France, Nataf Serge, Jurdic Pierre, Arnaud Sylvie, Servet-Delprat Christine, Gilmore Gary L, Belin Marie-Françoise, Rabourdin-Combe Chantal, and Mouchiroud Guy

Subjects
Immunologic diseases. Allergy, RC581-607
Abstract

Abstract Background Macrophages, osteoclasts, dendritic cells, and microglia are highly specialized cells that belong to the mononuclear phagocyte system. Functional and phenotypic heterogeneity within the mononuclear phagocyte system may reveal differentiation plasticity of a common progenitor, but developmental pathways leading to such diversity are still unclear. Results Mouse bone marrow cells were expanded in vitro in the presence of Flt3-ligand (FL), yielding high numbers of non-adherent cells exhibiting immature monocyte characteristics. Cells expanded for 6 days, 8 days, or 11 days (day 6-FL, day 8-FL, and day 11-FL cells, respectively) exhibited constitutive potential towards macrophage differentiation. In contrast, they showed time-dependent potential towards osteoclast, dendritic, and microglia differentiation that was detected in day 6-, day 8-, and day 11-FL cells, in response to M-CSF and receptor activator of NFκB ligand (RANKL), granulocyte-macrophage colony stimulating-factor (GM-CSF) and tumor necrosis factor-α (TNFα), and glial cell-conditioned medium (GCCM), respectively. Analysis of cell proliferation using the vital dye CFSE revealed homogenous growth in FL-stimulated cultures of bone marrow cells, demonstrating that changes in differential potential did not result from sequential outgrowth of specific precursors. Conclusions We propose that macrophages, osteoclasts, dendritic cells, and microglia may arise from expansion of common progenitors undergoing sequential differentiation commitment. This study also emphasizes differentiation plasticity within the mononuclear phagocyte system. Furthermore, selective massive cell production, as shown here, would greatly facilitate investigation of the clinical potential of dendritic cells and microglia.

Published
2002
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28. Inhibitors : effects on cell toxicity ; osteoblast-induced mineralization and osteoclast-mediated bone resorption

Author

Ren, Zhong-Yuan, Machuca-Gayet, Irma, Domenget, Chantal, Buchet, Rene, Wu, Yuqing, Jurdic, Pierre, Mebarek, Saida, State Key Laboratory of Supramolecular Structure and Materials, Jilin University, Institut de Chimie et Biochimie Moléculaires et Supramoléculaires (ICBMS), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-École Supérieure Chimie Physique Électronique de Lyon-Centre National de la Recherche Scientifique (CNRS), Institut de Génomique Fonctionnelle de Lyon (IGFL), École normale supérieure - Lyon (ENS Lyon)-Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Métabolisme, Enzymes et Mécanismes Moléculaires (MEM²), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-École Supérieure Chimie Physique Électronique de Lyon-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Depierre, Frédérique, Université de Lyon-Université de Lyon-École Supérieure de Chimie Physique Électronique de Lyon (CPE)-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), École normale supérieure de Lyon (ENS de Lyon)-Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-École Supérieure Chimie Physique Électronique de Lyon-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), and Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-École Supérieure Chimie Physique Électronique de Lyon-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL)

Subjects
musculoskeletal diseases, [CHIM.ORGA]Chemical Sciences/Organic chemistry, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], [CHIM.ORGA] Chemical Sciences/Organic chemistry, [SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM]
Abstract

International audience; AimThe cysteine protease cathepsin K (CatK), abundantly expressed in osteoclasts, is responsible for the degradation of bone matrix proteins, including collagen type 1. Thus, CatK is an attractive target for new anti-resorptive osteoporosis therapies, but the wider effects of CatK inhibitors on bone cells also need to be evaluated to assess their effects on bone. Therefore, we selected, among a series of synthetized isothiosemicarbazides, two molecules which are highly selective CatK inhibitors (CKIs) to test their effects on osteoblasts and osteoclasts.Research Design and MethodsCell viability upon treatment of CKIs were was assayed on human osteoblast-like Saos-2, mouse monocyte cell line RAW 264.7 and mature mouse osteoclasts differentiated from bone marrow. Osteoblast-induced mineralization in Saos-2 cells and in mouse primary osteoblasts from calvaria, with or without CKIs,; were was monitored by Alizarin Red staining and alkaline phosphatase activity, while osteoclast-induced bone resorption was performed on bovine slices.ResultsTreatments with two CKIs, CKI-8 and CKI-13 in human osteoblast-like Saos-2, murine RAW 264.7 macrophages stimulated with RANKL and mouse osteoclasts differentiated from bone marrow stimulated with RANKL and MCSF were found not to be toxic at doses of up to 100 nM. As probed by Alizarin Red staining, CKI-8 did not inhibit osteoblast-induced mineralization in mouse primary osteoblasts as well as in osteoblast-like Saos-2 cells. However, CKI-13 led to a reduction in mineralization of around 40% at 10–100 nM concentrations in osteoblast-like Saos-2 cells while it did not in primary cells. After a 48-hour incubation, both CKI-8 and CKI-13 decreased bone resorption on bovine bone slices. CKI-13 was more efficient than the commercial inhibitor E-64 in inhibiting bone resorption induced by osteoclasts on bovine bone slices. Both CKI-8 and CKI-13 created smaller bone resorption pits on bovine bone slices, suggesting that the mobility of osteoclasts was slowed down by the addition of CKI-8 and CKI-13.ConclusionCKI-8 and CKI-13 screened here show promise as antiresorptive osteoporosis therapeutics but some off target effects on osteoblasts were found with CKI-13.

Published
2015

29. Autophagy in osteoblasts is involved in mineralization and bone homeostasis

Author

Nollet, Marie, Santucci-Darmanin, Sabine, Breuil, Véronique, Al-Sahlanee, Rasha, Cros, Chantal, Topi, Majlinda, Momier, David, Samson, Michel, Pagnotta, Sophie, Cailleteau, Laurence, Battaglia, Séverine, Farlay, Delphine, Dacquin, Romain, Barois, Nicolas, Jurdic, Pierre, Boivin, Georges, Heymann, Dominique, Lafont, Frank, Lu, Shi Shou, Dempster, David, Carle, Georges, Pierrefite-Carle, Valérie, Carle, Pierre, Transporteurs et Imagerie, Radiothérapie en Oncologie et Mécanismes biologiques des Altérations du Tissu Osseux (TIRO-MATOs - UMR E4320), Service Hospitalier Frédéric Joliot (SHFJ), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-UMR E4320 (TIRO-MATOs), Université Nice Sophia Antipolis (1965 - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Côte d'Azur (UCA)-Université Nice Sophia Antipolis (1965 - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Côte d'Azur (UCA), Centre Commun de Microscopie Appliquée (CCMA), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA), UMR E4320 (TIRO-MATOs), Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Côte d'Azur (UCA)-Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Côte d'Azur (UCA)-Service Hospitalier Frédéric Joliot (SHFJ), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay

Subjects
collagen, HRTEM, high resolution transmission electron microscopy, [SDV]Life Sciences [q-bio], Osteoporosis, bone volume, Osteoclasts, TNFSF11/RANKL, runt-related transcription factor 2, TV, Bone remodeling, Mice, Homeostasis, tumor necrosis factor (ligand) superfamily, mineralization, PBS, ComputingMilieux_MISCELLANEOUS, total volume, Microscopy, Confocal, biology, Osteoblast, BECN1, Beclin 1, tartrate resistant, autophagy-related, Cell biology, ACP5/TRAP, medicine.anatomical_structure, RANKL, osteoclast, osteoblast, Female, ribonucleic acid, secreted phosphoprotein 1, medicine.medical_specialty, autophagy, Basic Research Papers, RUNX2, Green Fluorescent Proteins, acid phosphatase 5, Mice, Transgenic, type I, phosphate-buffered saline, Bone and Bones, Bone resorption, SAED, member 11, Osteoclast, Cell Line, Tumor, Internal medicine, bafilomycin A1, medicine, Animals, BV, OC, selected area electron diffraction, OB, Baf, Bone Resorption, Molecular Biology, bone remodeling, microtubule-associated protein 1 light chain 3, Osteoblasts, RANK Ligand, Autophagy, NF-kappa B p50 Subunit, α 1, X-Ray Microtomography, Cell Biology, MAP1LC3 (LC3), medicine.disease, Rats, Oxidative Stress, Endocrinology, TUBB, tubulin, SPP1/OPN, Col1A, biology.protein, RNA, beta
Abstract

International audience; Bone remodeling is a tightly controlled mechanism in which osteoblasts (OB), the cells responsible for bone formation, osteoclasts (OC), the cells specialized for bone resorption, and osteocytes, the multifunctional mechanosensing cells embedded in the bone matrix, are the main actors. Increased oxidative stress in OB, the cells producing and mineralizing bone matrix, has been associated with osteoporosis development but the role of autophagy in OB has not yet been addressed. This is the goal of the present study. We first show that the autophagic process is induced in OB during mineralization. Then, using knockdown of autophagy-essential genes and OB-specific autophagy-deficient mice, we demonstrate that autophagy deficiency reduces mineralization capacity. Moreover, our data suggest that autophagic vacuoles could be used as vehicles in OB to secrete apatite crystals. In addition, autophagy-deficient OB exhibit increased oxidative stress and secretion of the receptor activator of NFKB1 (TNFSF11/RANKL), favoring generation of OC, the cells specialized in bone resorption. In vivo, we observed a 50% reduction in trabecular bone mass in OB-specific autophagy-deficient mice. Taken together, our results show for the first time that autophagy in OB is involved both in the mineralization process and in bone homeostasis. These findings are of importance for mineralized tissues which extend from corals to vertebrates and uncover new therapeutic targets for calcified tissue-related metabolic pathologies.

Published
2014
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30. Novel models of osteoporosis in transgenic mice overexpressing human rankl

Author

Douni, Eleni, Dacquin, Romain, Bonnet, Nicolas, Jurdic, Pierre, Ferrari, Serge, Rinotas, Vagelis, Agricultural University of Athens, Institut de Génomique Fonctionnelle de Lyon (IGFL), École normale supérieure de Lyon (ENS de Lyon)-Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Hôpitaux Universitaires de Genève (HUG), Université de Genève = University of Geneva (UNIGE), ProdInra, Migration, École normale supérieure - Lyon (ENS Lyon)-Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Université de Genève (UNIGE), Université Claude Bernard Lyon 1 (UCBL), and Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-École normale supérieure - Lyon (ENS Lyon)

Subjects
[SDV.MHEP.EM] Life Sciences [q-bio]/Human health and pathology/Endocrinology and metabolism, [SDV.MHEP.EM]Life Sciences [q-bio]/Human health and pathology/Endocrinology and metabolism, ComputingMilieux_MISCELLANEOUS
Abstract

Osteoporosis International, 25, Supplement 2; International audience

Published
2014

31. Novel genetic models of osteoporosis by overexpression of human RANKL in transgenic mice

Author

Rinotas, Vagelis, Niti, Alexandra, Dacquin, Romain, Bonnet, Nicolas, Stolina, Marina, Han, Chun-Ya, Kostenuik, Paul, Jurdic, Pierre, Ferrari, Serge Livio, and Douni, Eleni

Subjects
ddc:616, Models, Genetic, RANK Ligand, Calcinosis, Osteoclasts, Mice, Transgenic, Disease Models, Animal, Mice, Gene Expression Regulation, Osteopetrosis, Animals, Humans, Osteoporosis, Female, Growth Plate
Abstract

Receptor activator of NF-κB ligand (RANKL) plays a key role in osteoclast-induced bone resorption across a range of degenerative bone diseases, and its specific inhibition has been recently approved as a treatment for women with postmenopausal osteoporosis at high or increased risk of fracture in the United States and globally. In the present study, we generated transgenic mice (TghuRANKL) carrying the human RANKL (huRANKL) genomic region and achieved a physiologically relevant pattern of RANKL overexpression in order to establish novel genetic models for assessing skeletal and extraskeletal pathologies associated with excessive RANKL and for testing clinical therapeutic candidates that inhibit human RANKL. TghuRANKL mice of both sexes developed early-onset bone loss, and the levels of huRANKL expression were correlated with bone resorption and disease severity. Low copy Tg5516 mice expressing huRANKL at low levels displayed a mild osteoporotic phenotype as shown by trabecular bone loss and reduced biomechanical properties. Notably, overexpression of huRANKL, in the medium copy Tg5519 line, resulted in severe early-onset osteoporosis characterized by lack of trabecular bone, destruction of the growth plate, increased osteoclastogenesis, bone marrow adiposity, increased bone remodeling, and severe cortical bone porosity accompanied by decreased bone strength. An even more severe skeletal phenotype developed in the high copy Tg5520 founder with extensive soft tissue calcification. Model validation was further established by evidence that denosumab, an antibody that inhibits human but not murine RANKL, fully corrected the hyper-resorptive and osteoporotic phenotypes of Tg5519 mice. Furthermore, overexpression of huRANKL rescued osteopetrotic phenotypes of RANKL-defective mice. These novel huRANKL transgenic models of osteoporosis represent an important advance for understanding the pathogenesis and treatment of high-turnover bone diseases and other disease states caused by excessive RANKL.

Published
2013

32. Control of bone resorption by semaphorin 4D is dependant on ovarian function

Author

Machuca-Gayet, Irma, Dacquin, Romain, Domenget, Chantal, Jurdic, Pierre, ProdInra, Migration, Institut de Génomique Fonctionnelle de Lyon (IGFL), École normale supérieure - Lyon (ENS Lyon)-Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), École normale supérieure de Lyon (ENS de Lyon)-Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Université Claude Bernard Lyon 1 (UCBL), and Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-École normale supérieure - Lyon (ENS Lyon)

Subjects
[SDV] Life Sciences [q-bio], semaphorin 4d, [SDV]Life Sciences [q-bio], [INFO]Computer Science [cs], [INFO] Computer Science [cs], ComputingMilieux_MISCELLANEOUS, bone resorption
Abstract

International audience

Published
2011

34. Paxillin Phosphorylation Controls Invadopodia/Podosomes Spatiotemporal Organization

Author

Badowski, Cédric, Pawlak, Géraldine, Grichine, Alexei, Chabadel, Anne, Oddou, Christiane, Jurdic, Pierre, Pfaff, Martin, Albiges-Rizo, Corinne, Block, Marc, Institut d'oncologie/développement Albert Bonniot de Grenoble (INSERM U823), Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM), Dynamique des systèmes d'adhérence et différenciation (DySAD), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), École normale supérieure de Lyon (ENS de Lyon), CNRS ERL 3148, and École normale supérieure - Lyon (ENS Lyon)

Subjects
adhesion, podosomes, paxilline, macromolecular substances, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, cell invasion, invadopodia
Abstract

International audience; In Rous sarcoma virus (RSV)-transformed baby hamster kidney (BHK) cells, invadopodia can self-organize into rings and belts, similarly to podosome distribution during osteoclast differentiation. The composition of individual invadopodia is spatiotemporally regulated and depends on invadopodia localization along the ring section: the actin core assembly precedes the recruitment of surrounding integrins and integrin-linked proteins, whereas the loss of the actin core was a prerequisite to invadopodia disassembly. We have shown that invadopodia ring expansion is controlled by paxillin phosphorylations on tyrosine 31 and 118, which allows invadopodia disassembly. In BHK-RSV cells, ectopic expression of the paxillin mutant Y31F-Y118F induces a delay in invadopodia disassembly and impairs their self-organization. A similar mechanism is unraveled in osteoclasts by using paxillin knockdown. Lack of paxillin phosphorylation, calpain or extracellular signal-regulated kinase inhibition, resulted in similar phenotype, suggesting that these proteins belong to the same regulatory pathways. Indeed, we have shown that paxillin phosphorylation promotes Erk activation that in turn activates calpain. Finally, we observed that invadopodia/podosomes ring expansion is required for efficient extracellular matrix degradation both in BHK-RSV cells and primary osteoclasts, and for transmigration through a cell monolayer.

Published
2008
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35. Thyroid hormone T3 acting through the thyroid hormone ALPHA receptor is necessary for implementation of erythropoiesis in the neonatal spleen environment in the mouse

Author

Angelin-Duclos, C., Domenget, Chantal, Kolbus, A., Beug, H., Jurdic, Pierre, Samarut, Jacques, Unité mixte de recherche biologie moléculaire de la cellule, École normale supérieure - Lyon (ENS Lyon)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Institut de Génomique Fonctionnelle de Lyon (IGFL), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-École normale supérieure - Lyon (ENS Lyon), École normale supérieure de Lyon (ENS de Lyon)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), École normale supérieure de Lyon (ENS de Lyon)-Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), and Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-École normale supérieure - Lyon (ENS Lyon)

Subjects
SOURIS KO, [SDV]Life Sciences [q-bio], [INFO]Computer Science [cs], SOURIS TRANSGENIQUE, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2005

36. SH3P2 in complex with Cbl and Src

Author

Szymkiewicz, I., Destaing, O., Jurdic, Pierre, Dikic, Ivan, Unité mixte de recherche biologie moléculaire de la cellule, and Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-École normale supérieure - Lyon (ENS Lyon)

Subjects
[SDV]Life Sciences [q-bio], TYROSINE KYNASE, [INFO]Computer Science [cs], ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2004

37. Cell surface delivery of the Measles virus nucleoprotein: a viral strategy to induce immunosuppression

Author

Marie, J.C., Saltel, F., Escola, J.M., Jurdic, Pierre, Wild, T.F., Horvat, Branka, Unité mixte de recherche biologie moléculaire de la cellule, Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-École normale supérieure - Lyon (ENS Lyon), ProdInra, Migration, and École normale supérieure de Lyon (ENS de Lyon)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
[SDV] Life Sciences [q-bio], [SDV]Life Sciences [q-bio], [INFO]Computer Science [cs], [INFO] Computer Science [cs], ComputingMilieux_MISCELLANEOUS, VIROLOGIE
Abstract

International audience

Published
2004

38. I KAPPA B BETA phosphorylates Dok1 serines in response to TNF, IL-1, or GAMMA radiation

Author

Lee, Sue Han, Andrieu, C., Saltel, F., Destaing, O., Auclair, Julie, Pouchkine, V., Michelon, J., Salaun, B., Kobayashi, R., Jurdic, Pierre, Kieff, E.D., Sylla, B.S., Unité mixte de recherche biologie moléculaire de la cellule, École normale supérieure de Lyon (ENS de Lyon)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), and Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-École normale supérieure - Lyon (ENS Lyon)

Subjects
[SDV]Life Sciences [q-bio], BIOLOGIE CELLULAIRE, [INFO]Computer Science [cs], ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2004

40. Dual Impact of Live Staphylococcus aureus on the Osteoclast Lineage, Leading to Increased Bone Resorption

Author

Trouillet-Assant, Sophie, primary, Gallet, Marlène, additional, Nauroy, Pauline, additional, Rasigade, Jean-Philippe, additional, Flammier, Sacha, additional, Parroche, Peggy, additional, Marvel, Jacqueline, additional, Ferry, Tristan, additional, Vandenesch, Francois, additional, Jurdic, Pierre, additional, and Laurent, Frederic, additional

Published
2014
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42. Lysophosphatidic Acid Receptor Type 1 (LPA1) Plays a Functional Role in Osteoclast Differentiation and Bone Resorption Activity

Author

David, Marion, primary, Machuca-Gayet, Irma, additional, Kikuta, Junichi, additional, Ottewell, Penelope, additional, Mima, Fuka, additional, Leblanc, Raphael, additional, Bonnelye, Edith, additional, Ribeiro, Johnny, additional, Holen, Ingunn, additional, Vales, Rùben Lopez, additional, Jurdic, Pierre, additional, Chun, Jerold, additional, Clézardin, Philippe, additional, Ishii, Masaru, additional, and Peyruchaud, Olivier, additional

Published
2014
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45. Podosomes Display Actin Turnover and Dynamic Self-Organization in Osteoclasts Expressing Actin-Green Fluorescent Protein □ V

Author

Destaing, Olivier, Saltel, Frédéric, Géminard, Jean-Christophe, Jurdic, Pierre, Bard, Frédéric, Laboratoire de Biologie Moléculaire de la Cellule (LBMC), École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Physique de l'ENS Lyon (Phys-ENS), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon, and École normale supérieure - Lyon (ENS Lyon)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL)

Subjects
[PHYS.PHYS.PHYS-GEN-PH]Physics [physics]/Physics [physics]/General Physics [physics.gen-ph]
Abstract

International audience; Podosomes, small actin-based adhesion structures, differ from focal adhesions in two aspects: their core structure and their ability to organize into large patterns in osteoclasts. To address the mechanisms underlying these features, we imaged live preosteoclasts expressing green fluorescent protein-actin during their differentiation. We observe that podosomes always form inside or close to podosome groups, which are surrounded by an actin cloud. Fluorescence recovery after photobleaching shows that actin turns over in individual podosomes in contrast to cortactin, suggesting a continuous actin polymerization in the podosome core. The observation of podo-some assemblies during osteoclast differentiation reveals that they evolve from simple clusters into rings that expand by the continuous formation of new podosomes at their outer ridge and inhibition of podosome formation inside the rings. This self-organization of podosomes into dynamic rings is the mechanism that drives podosomes at the periphery of the cell in large circular patterns. We also show that an additional step of differentiation, requiring microtubule integrity, stabilizes the podosome circles at the cell periphery to form the characteristic podosome belt pattern of mature osteoclasts. These results therefore provide a mechanism for the patterning of podosomes in osteoclasts and reveal a turnover of actin inside the podosome.

Published
2003
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46. Microtubule dynamics regulates Rho and Rac activities antagonistically and triggers stress fiber-like formation independently of Rho in macrophage polykaryons

Author

Ory, S., Destaing, O., Jurdic, Pierre, Laboratoire de Biologie Moléculaire de la Cellule (LBMC), École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), and Bigouraux, Sylvie

Subjects
[SDV] Life Sciences [q-bio], [SDV]Life Sciences [q-bio], ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2002

47. Molecular complexes that contain both c-Cbl and c-Src associate with Golgi membranes

Author

Bard, F., Patel, U., Levy, J.B., Jurdic, Pierre, Horne, W.C., Baron, R., Bigouraux, Sylvie, Laboratoire de Biologie Moléculaire de la Cellule (LBMC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon, École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), and Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)

Subjects
[SDV] Life Sciences [q-bio], [SDV]Life Sciences [q-bio], ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2002

48. RANKL induces formation of avian osteoclasts but not from macrophage polykaryons

Author

Boissy, P., Destaing, O., Jurdic, Pierre, Bigouraux, Sylvie, Laboratoire de Biologie Moléculaire de la Cellule (LBMC), École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), and Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)

Subjects
[SDV] Life Sciences [q-bio], [SDV]Life Sciences [q-bio], ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2001

49. CD46/CD3 co-stimulation induces morphological changes of human T cells and activation of vav, Rac and Extracellular signal-related kinase mitogen-activated protein kinase

Author

Zafran, Y., Destaing, O., Roux, A., Ory, S., Nheu, T., Jurdic, Pierre, Rabourdin-Combe, C., Astier, A., Laboratoire de Biologie Moléculaire de la Cellule (LBMC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon, École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), and Bigouraux, Sylvie

Subjects
[SDV] Life Sciences [q-bio], [SDV]Life Sciences [q-bio], ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2001

50. Podosomes in osteoclast-like cells : structural analysis and cooperative role of paxillin, proline-rich tyrosine kinase2 (Pyk2) and integrin avb3

Author

Pfaff, M., Jurdic, Pierre, Bigouraux, Sylvie, Laboratoire de Biologie Moléculaire de la Cellule (LBMC), École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), and Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)

Subjects
[SDV] Life Sciences [q-bio], [SDV]Life Sciences [q-bio], ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2001

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