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The Effects of Particulate Wear Debris, Cytokines, and Growth Factors on the Functions of MG-63 Osteoblasts
Csaba Vermes, MD; Raman Chandrasekaran, PhD; Joshua J. Jacobs, MD; Jorge O. Galante, MD, DMSc; Kenneth A. Roebuck, PhD; Tibor T. Glant, MD, PhD
View Disclosures and Other Information
Investigation performed at Rush-Presbyterian-St. Luke's Medical Center, Chicago, Illinois
Csaba Vermes, MD Raman Chandrasekaran, PhD Joshua J. Jacobs, MD Jorge O. Galante, MD, DMSc Tibor T. Glant, MD, PhD Department of Orthopedic Surgery, Rush University, Rush-Presbyterian-St. Luke's Medical Center, 1653 West Congress Parkway, Chicago, IL 60612. E-mail address for T.T. Glant: tglant@rush.edu
Kenneth A. Roebuck, PhD Department of Immunology/Microbiology, Rush University, Rush-Presbyterian-St. Luke's Medical Center, 1653 West Congress Parkway, Chicago, IL 60612
Although none of the authors has received or will receive benefits for personal or professional use from a commercial party related directly or indirectly to the subject of this article, benefits have been or will be received but are directed solely to a research fund, foundation, educational institution, or other nonprofit organization with which one or more of the authors is associated. Funds were received in total or partial support of the research or clinical study presented in this article. The funding sources were the National Institutes of Health, Zimmer, and the Musculoskeletal Research Foundation.

The Journal of Bone & Joint Surgery.  2001; 83:201-201 
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Abstract

Background: Particle-challenged cells release cytokines, chemokines, and eicosanoids, which contribute to periprosthetic osteolysis. The particle-induced activation of macrophages and monocytes has been extensively studied, but only limited information is available on the response of osteoblasts to particulate wear debris. This study examines the effects of particulate wear debris, proinflammatory cytokines, and growth factors on osteoblast functions.

Methods: MG-63 osteoblasts were treated with metal particles (titanium, titanium alloy, and chromium orthophosphate) or polymeric particles (polyethylene and polystyrene) of phagocytosable sizes or were treated with exogenous cytokines and growth factors. The kinetics of particle phagocytosis and the number of engulfed particles were assessed with use of fluoresceinated particles. Cell proliferation was determined according to [3H]-thymidine incorporation, and cell viability was determined by either fluorescein diacetate uptake or trypan blue exclusion. Expressions of osteoblast-specific genes were quantified with Northern blot hybridization, and the secretions of osteoblast-specific proteins and cytokines were analyzed by enzyme-linked immunosorbent assays.

Results: MG-63 osteoblasts phagocytosed particles and became saturated after twenty-four hours. A maximum of forty to sixty particles per cell were phagocytosed. Each type of particle significantly suppressed procollagen a1[I] gene expression (p < 0.05), whereas other osteoblast-specific genes (osteonectin, osteocalcin, and alkaline phosphatase) did not show significant changes. Particle-stimulated osteoblasts released interleukin-6 (p < 0.05) and a smaller amount of transforming growth factor-b1. Particles reduced cell proliferation in a dose-dependent manner without affecting cell viability (p < 0.05). Exogenous tumor necrosis factor-a also enhanced the release of interleukin-6 (p < 0.01) and transforming growth factor-b1 (p < 0.05), whereas the secretion of transforming growth factor-b1 was increased by insulin-like growth factor-I and prostaglandin E2 as well. Insulin-like growth factor-I and transforming growth factor-b1 significantly increased procollagen a1[I] gene expression in osteoblasts (p < 0.05), while tumor necrosis factor-a and prostaglandin E2 significantly suppressed procollagen a1[I] gene expression (p < 0.01). In contrast, neither exogenous nor endogenous interleukin-6 had any effect on other cytokine secretion, on proliferation, or on procollagen a1[I] gene expression. The transcription inhibitor actinomycin D reduced both procollagen a1[I] transcription and interleukin-6 production. Inhibitors of protein synthesis (cyclohexamide) and intracellular protein transport (brefeldin A and monensin) blocked the release of interleukin-6, but none of these compounds influenced the suppressive effect of titanium on procollagen a1[I] gene expression.

Conclusions: MG-63 osteoblasts phagocytose particulate wear debris, and this process induces interleukin-6 production and suppresses type-I collagen synthesis. Osteoblast-derived interleukin-6 may induce osteoclast differentiation and/or activation, but the resorbed bone cannot be replaced by new bone because of diminished osteoblast function (reduced type-I collagen synthesis). Exogenous cytokines (tumor necrosis factor-a and interleukin-1b), growth factors (insulin-like growth factor-I and transforming growth factor-b1), and prostaglandin E2 can modify particulate-induced alterations of osteoblast functions.

Clinical Relevance: Altered osteoblast functions probably contribute to the progression of periprosthetic osteolysis. Suppressed osteoblast functions, however, could be compensated for by certain growth factors, such as insulin-like growth factor-I or transforming growth factor-b1. These growth factors, if delivered locally, may have therapeutic potential to prevent or reverse periprosthetic osteolysis.

Figures in this Article
    Periprosthetic osteolysis is a major clinical problem that may jeopardize the long-term success of total joint arthroplasty1-4. In periprosthetic osteolysis, a granulomatous tissue of fibroblasts, macrophages, and foreign-body giant cells develops at the interface of the bone and prosthesis or of the bone and bone cement5-8. All cell types of this interfacial tissue contain wear debris from prosthetic components9-14, and particle phagocytosis is a central event in the pathogenesis of periprosthetic osteolysis15-18.
    Phagocytosis is a nonspecific defense mechanism for the elimination of tissue debris, bacteria, and foreign particles. The phagocytic process requires the opsonization of particles and a protein coat on the surface of particles that bind to phagocytosis receptors (such as Fcg receptors, complement or mannose receptors, and b1 integrins). This interaction activates intracellular signaling pathways that lead to cytoskeletal reorganization, pseudopod formation, and the ingestion of the particles19-21. This phagocytosis-induced signaling process may simultaneously result in the upregulation or downregulation of a number of genes through the action of various nuclear transcription factors19,22-25. However, the normal phagocytic process may be altered when tissue macrophages or other cells are continuously exposed to nondegradable wear debris.
    The phagocytosis of particulate wear debris stimulates macrophages/monocytes to secrete mediators of bone resorption such as eicosanoids, interleukin-1 (IL-1), tumor necrosis factor-alpha (TNF-a), and interleukin-6 (IL-6) in vitro11,15,22,24,26-29. These compounds have also been shown to be present in periprosthetic soft tissue in vivo6,11,30.
    Osteoblasts also phagocytose particles. This process upregulates the release of cytokines25 and prostaglandin E231, inducing bone loss through osteoclast activation. In addition, particle-stimulated osteoblasts exhibit suppressed procollagen a1[I] gene expression followed by reduced type-I collagen synthesis17,25, which may result in decreased formation of bone. Thus, particle-induced altered osteoblast functions may play a critical role in pathological bone resorption through both osteoclast activation and reduced osteoblastic bone formation.
    In previous studies, we identified the upstream signaling events in particle-stimulated osteoblasts25 that ultimately led to the suppression of procollagen a1[I] gene expression17,25. Activation of protein tyrosine kinases seems to be the earliest cellular event resulting in the activation of nuclear transcription factor-kappaB (NF-kB)25 in osteoblasts, and this transcription factor was shown to be activated in particle-challenged human macrophages as well24. However, NF-kB is a general transcription factor that may suppress procollagen a1[I] mRNA25,32 while simultaneously upregulating many other genes, including the genes of proinflammatory cytokines such as IL-1, IL-6, and TNF-a24 in particle-challenged cells. Since these mediators are continuously secreted by particle-challenged cells, their effects may be crucial in the development of periprosthetic osteolysis by altering osteoblast and osteoclast functions.
    We hypothesized that, besides the direct effects of particulate wear debris on osteoblasts (increased IL-6 release and suppressed type-I collagen synthesis)25, there is a paracrine regulation of cytokines, prostaglandins, and growth factors, which contribute to bone resorption by alteration of osteoblast functions. We investigated this hypothesis by monitoring the kinetics of particle phagocytosis in osteoblasts and by determining the effects of proinflammatory cytokines and growth factors on osteoblast-specific gene expression, cell proliferation, and cytokine release.
     
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    +Fig. 1-A:The number of phagocytosed Fluoresbrite particles in a single cell is shown at different time-points.
     
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    +Fig. 1-B:The number of phagocytosed Fluoresbrite particles in a single cell is shown at different time-points.
     
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    +Fig. 1-C:The number of phagocytosed Fluoresbrite particles in a single cell is shown at different time-points.
     
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    +Fig. 2:Effect of titanium particles and exogenous mediators on MG-63 cell proliferation. Cells were not treated or were treated either with different concentrations of titanium particles (panel A) or with exogenous cytokines and growth factors (panel B). The level of proliferation was measured with [3H]-thymidine incorporation and was normalized to untreated samples (100%) at each time-point. Error bars are omitted for clarity, but the broken line indicates significance at a minimum level of p < 0.05 in panel A. In panel B, * indicates a level of significance (relative to untreated cells) of p < 0.05 and ** indicates a level of p < 0.01.
     
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    +Fig. 3:Effect of titanium particles on production of IL-6 and TGF-b1 by MG-63 cells. Confluent osteoblast cultures were not treated or were treated with 0.1% (volume/volume) titanium particles. Levels of IL-6, TNF-a, IL-1b, and TGF-b1 were measured with enzyme-linked immunosorbent assays at various time-points. Only IL-6 (panel A) and TGF-b1 (panel B) reached detectable and significantly elevated levels, with * indicating a p value of less than 0.05 and ** indicating a p value of less than 0.01.
     
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    +Fig. 4:Effect of exogenous cytokines on the release of cytokines by MG-63 cells. Confluent osteoblast cultures were not treated or were treated with exogenous IL-6, TNF-a, IL-1b, TGF-b1, IGF-I, or prostaglandin E2 as described in Materials and Methods. Conditioned media were collected at various time-points, and cytokine levels were measured with enzyme-linked immunosorbent assays. Only IL-6 (panel A) and TGF-b1 (panel B) reached detectable and significantly elevated levels, with * indicating a p value of less than 0.05 and ** indicating a p value of less than 0.01.
     
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    +Fig. 5:The effect of various particles on procollagen a1[I] and osteocalcin gene expressions in MG-63 cells. Confluent cell cultures were deprived of serum for twenty-four hours and were left untreated (lanes 1 and 10) or were treated with different particles for forty-eight hours at the various concentrations indicated. The level of gene expression was compared with that in untreated samples. Columns represent means of duplicates of at least five independent experiments (and the standard deviation) of procollagen a1[I] gene expression. * indicates a p value of less than 0.05, and ** indicates a p value of less than 0.01. The osteocalcin gene expression in particle-treated MG-63 cells showed no significant differences, and a representative hybridization panel (OC) is shown. All types of particles significantly reduced the procollagen a1[I] mRNA expression.
     
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    +Fig. 6:Northern blot analysis of procollagen a1[I] rnRNA expression in MG-63 cells treated with different cytokines (panel A) or growth factors (panel B) in the presence or absence of phagocytosable-size titanium particles. Confluent osteoblast cultures were deprived of serum for twenty-four hours and were pretreated with cytokine/growth factor for three hours, and then titanium particles (0.1%, volume/volume) were added where indicated. Bottom panels show the amounts of total (ribosomal) RNA on an ethidium bromide-stained membrane prior to hybridization. Columns represent means of duplicates of at least five independent experiments and the standard deviation. Data are normalized to the mRNA level measured in nonstimulated MG-63 cells (lane 1 in both panels). * indicates a p value of less than 0.05, and ** indicates a p value of less than 0.01. Neither IL-6 nor IL-1b had an effect on procollagen a1[I] gene expression in the particle-free condition, although IL-1b could partially compensate for the suppressive effect of titanium on procollagen a1[I] gene expression.
     
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    +Fig. 7:Effect of protein synthesis and transport inhibitors on procollagen a1[I] gene expression. Confluent MG-63 osteoblast cultures were deprived of serum for twenty-four hours and were left untreated or were pretreated with the indicated compound for three hours, and then titanium particles (0.1% volume/volume) were added where shown. The level of gene expression was analyzed by Northern blots to determine procollagen a1[I] mRNA and was compared with that in untreated samples (lane 1). Columns represent means of duplicates of at least five independent experiments and the standard deviation. * indicates a p value of less than 0.05, and ** indicates a p value of less than 0.01. None of the compounds were able to reverse the particle-treatment-induced gene suppression.

    Particles

    All metal and polymeric particles used in this study were described previously17,18,26,28. Particles of commercially pure titanium with a 1 to 3-mm nominal diameter and chromium orthophosphate (CrPO4 4H2O) (mean diameter and standard deviation, 1.42 ± 0.83 m)28 were purchased from Johnson Matthey (Danvers, Massachusetts). Titanium-alloy particles (6% aluminum and 4% vanadium) (Sulzer Metco, Troy, Michigan) were ground from 150 to 300-mm-sized grinding particles29. Conventional medical-grade ultra-high molecular weight polyethylene (GUR 415; Hoecht-Celanese, Houston, Texas) was pulverized in liquid nitrogen29. Particles were sedimented and then subjected to filtration. The particles had a comparable size distribution, with at least 90% of the particles less than 3 m in diameter. Polystyrene particles (mean diameter and standard deviation, 1.14 ± 0.01 mm) and polystyrene-based fluorescent particles (Fluoresbrite) (mean diameter and standard deviation, 0.926 ± 0.027 mm) were purchased from Polysciences (Warrington, Pennsylvania). A 0.1% (volume/volume) particle suspension contained approximately 2.2 to 6.7 108 particles per milliliter. The particles were sterilized by irradiation with 2.2 megarad (22,000 gray) from a Cs-137 source (model 143; J.L. Shepherd Irradiator, San Fernando, California) opsonized in 10% human type-AB serum29 and stored in sterile phosphate-buffered saline solution, pH 7.2. Endotoxin contamination of particles was excluded by limulus assay (E-Toxate; Sigma Chemical, St. Louis, Missouri).

    Cells and Cell Cultures

    The MG-63 osteoblast cell line was purchased from the American Type Culture Collection (ATCC, Rockville, Maryland). Cells were cultured in monolayer in Dulbecco modified Eagle medium (GIBCO, Grand Island, New York) containing 10% fetal bovine serum (HyClone Laboratories, Logan, Utah) in a humidified atmosphere of 5% carbon dioxide in air at 37C17,18,26.

    Treatment of Cells with Particles, Cytokines, and Growth Factors

    Confluent cultures of cells were subjected to serum starvation (0.3% fetal bovine serum) for twenty-four hours prior to treatment. Culture media were then replaced with fresh media consisting of 0.3% fetal bovine serum containing particles, cytokines, or growth factors. Proliferation and viability assays, phagocytosis analysis, and total RNA extraction were performed on the cultured cells. Tissue culture media were collected at various time-points, centrifuged, filtered through a 0.22-mm polycarbonate filter (Spin-x; CoStar, Cambridge, Massachusetts), and stored at -80C. All of the experiments were performed in duplicate or triplicate in at least five independent experiments.
    Reagents were purchased from Calbiochem (La Jolla, California) or R and D Systems (Minneapolis, Minnesota). Insulin-like growth factor-I (IGF-I, 30 ng/ml) and transforming growth factor-beta1 (TGF-b1, 20 pg/ml) were used to stimulate collagen production33,34. Tumor necrosis factor-a, IL-6, and IL-1b were added to the cultures at concentrations of 10 ng/ml, 500 pg/ml, and 30 pg/ml. Prostaglandin E2 (100 ng/ml) is an eicosanoid that has been shown to regulate collagen synthesis35. Actinomycin D (1 mg/ml) was used to block transcriptional events, cyclohexamide (35.5 M) was used to inhibit protein translation and synthesis, brefeldin A (0.1 M) was used to inhibit the transport of freshly synthesized proteins from the endoplasmatic reticulum to the Golgi apparatus, monensin (1.5 M) was used to block the release of newly synthesized proteins from the Golgi apparatus, and cytochalasin D (1 M) was used to destabilize the cytoskeleton, thus inhibiting phagocytosis. All of the concentrations listed above were selected after serial dilutions of each compound were tested in MG-63 cell culture.

    Viability Tests and [3H]-Thymidine Incorporation

    The trypan blue exclusion test was used to determine the viability of cells. Since the presence of phagocytosed titanium particles, especially at higher concentrations, precluded a precise evaluation of dye exclusion, cell viability was also determined with fluorescein diacetate (Molecular Probes, Eugene, Oregon)28. Viability tests were performed in duplicate, and at least 200 cells were counted with transmission or fluorescent microscopy in a Microphot-FXA microscope (Nikon, Tokyo, Japan).
    Proliferation of cells was measured by the incorporation of [3H]-thymidine (Amersham International, Arlington Heights, Illinois) into DNA in a ninety-six-well microplate system. Trypsinized cells were harvested (Cell Harvester; Tomtec, Orange, Connecticut) at different time-points after a twelve-hour [3H]-thymidine (1 C [37 Bcq] of [3H]-thymidine per well) incubation.

    RNA Extraction and Northern Blot Hybridization

    Total RNA samples were isolated from monolayer cultures as described previously17,18. Approximately 10 mg of total RNA was denatured in 50% formamide and 17.5% formaldehyde, dissolved in MOPS buffer (20 mM 3-[N-morpholino]propane-sulfonic acid, 5 mM sodium acetate, and 1 mM EDTA at pH 7.0), separated by electrophoresis in 1% agarose gel, and then transferred to GeneScreen Plus membranes (New England Nuclear, Boston, Massachusetts). Blots were hybridized with 32P-deoxycytidine-triphosphate-labeled specific cDNA probes at a concentration of 3 106 cpm/ml (specific activities: 2 to 6 108 cpm/g of cDNA)18. Human-specific cDNA probes (plasmids) were purchased from the American Type Culture Collection. The following recombinant plasmid DNAs were used as probes: a 1.8-kb cDNA probe for procollagen a1[I] (Hf677; ATCC 61322), a 2.0-kb probe for osteocalcin (ATCC 86269), a 1.8-kb probe for osteonectin (ATCC 78193), and a 1.5-kb probe for alkaline phosphatase (ATCC 59633). Following hybridization, the blots were washed and exposed to Kodak XAR-5 film (Eastman Kodak, Rochester, New York) at -70C for photographic documentation or the original Northern blot was analyzed by STORM PhosphorImiger with ImigeQuant software (both from Molecular Dynamics, Sunnyvale, California).

    Measurement of Particle Phagocytosis

    To further understand particle-induced changes in osteoblast function, we characterized the kinetics of particle uptake by MG-63 cells. In initial experiments, cells grown in monolayers were treated with 0.1% (volume/volume) titanium particles for various time-periods, harvested by trypsinization, washed, and allowed to attach to coverslips. Trypsinization and repeated washing of the cells removed nonphagocytosed and/or surface-attached particles, and cell-free areas of the coverslip had essentially no particles. Two hundred particle-treated cells from different areas on the coverslip were examined with light microscopy (Nikon). Although we could easily identify cells containing particles, it was difficult to determine the exact number of particles in a single cell because of the intracellular aggregation of titanium particles.
    To circumvent this problem and to be able to quantify the number of phagocytosed particles within a single cell, we used fluorescent particles (Fluoresbrite) as an alternative source of particles. Two different methods were applied to determine the number of engulfed particles in osteoblasts. First, the number of Fluoresbrite particles in cells was counted directly in epifluorescence mode with use of a Microphot-FXA microscope. However, this method could only be applied to cells treated for short time-periods (less than twelve hours), as the large number of phagocytosed particles in cells treated for longer periods formed intracellular aggregates, precluding accurate particle counts. The second method involved preparing serial dilutions of Fluoresbrite particles. The particles were counted in a hemocytometer, and the fluorescence intensity of each concentration was determined with a fluorescent plate reader (Victor 1420 multilabel counter; Wallac, Gaithersburg, Maryland). The particle numbers and the corresponding fluorescence intensities were plotted to generate a standard curve, which then was used to determine the number of fluorescent particles (on the basis of the fluorescence intensities) in cell lysates from osteoblasts treated with Fluoresbrite. Cells containing phagocytosed Fluoresbrite were trypsinized, washed, counted, and lysed by ultrasonication (VirTis, Gardina, New York) at 20 kHz for two minutes on ice.

    Measurement of Cytokines and Osteoblast-Specific Proteins in Culture Media

    Cytokine concentrations in supernatants of osteoblast cultures were measured by sandwich enzyme-linked immunosorbent assays (ELISAs) in ninety-six-well plates. High-sensitivity assay kits for TNF-a (range, 0.5 to 32 pg/ml), IL-1b (range, 0.12 to 8.0 pg/ml), IL-6 (range, 0.12 to 8.0 pg/ml), and TGF-b1 (range, 31 to 2000 pg/ml) were purchased from R and D Systems. Secreted osteocalcin was measured by NovoCalcin and type-I collagen was measured by Procollagen-C ELISAs purchased from Metra Biosystems (Mountain View, California).

    Statistical Analysis

    Descriptive statistics were used to determine group means and standard deviations. The Pillai trace (similar to Wilks lambda or the Hotelling-Lawley trace) criterion was used to detect multivariate significance. Subsequently, paired Student t tests were performed between groups of interest. The level of significance was set at p < 0.05. All statistical analyses were performed with use of computer-based statistical software (SPSS/PC+, version 4.0.1; SPSS, Chicago, Illinois).

    Particle Phagocytosis by Osteoblasts

    Osteoblasts phagocytosed particles in a time-dependent fashion (Fig. 1-CFig. 1-C). Determining the number of phagocytosed particles, however, is difficult because of the indiscernible location of phagocytosed, partially engulfed, or surface-attached particles and the intracellular aggregation of phagocytosed particles. The use of fluorescent particles (Fluoresbrite) is a method for determining the number of engulfed particles. The mean number of particles per cell (and standard deviation), measured with fluorescence intensity in MG-63 cell lysates, was 0.4 ± 0.6 (range, zero to two) after one hour, 5 ± 2 (range, three to twelve) after two hours, 13 ± 3 (range, seven to nineteen) after six hours, 23 ± 2 (range, sixteen to twenty-eight) after twelve hours, 53 ± 5 after twenty-four hours, 60 ± 6 after forty-eight hours, and 58 ± 5 after seventy-two hours (Fig. 1-CFig. 1-C). A maximum of forty to sixty Fluoresbrite particles phagocytosed within twenty-four hours seems to be the saturation level for MG-63 cells. The number of engulfed particles could be precisely determined only when fluorescent-labeled particles were used. Cytochalasin D, which destabilizes the cytoskeleton and inhibits phagocytosis, significantly reduced (p < 0.01) the phagocytosis of particles (4 ± 3 particles per cell after forty-eight hours) but did not completely abolish it (Figs. 1-AFigs. 1-A, panel A2, and 1-B1-B, panel B2).

    Effect of Particulate Wear Debris on Cell Viability and Proliferation

    Next, we addressed how the phagocytosed particles influenced cell functions and whether different compositions of particles could initiate different cell responses. Particulate wear debris had no effect on the viability of MG-63 cells, which remained higher than 95% even in long-term experiments (seventy-two to ninety-six hours) over a wide range of particle compositions (titanium, titanium alloy, chromium orthophosphate, polyethylene, polystyrene, and Fluoresbrite) and concentrations (0.0125% to 0.2% volume/volume). In contrast to viability, cell proliferation was reduced when compared with that in untreated cultures, and the effect was dose-dependent (Fig. 2Fig. 2, A). Interestingly, suppressed proliferation returned to normal by forty-eight hours at low particle concentrations (0.0125% to 0.05%) (Fig. 2Fig. 2, A).

    Effect of Exogenous Cytokines on Cell Viability and Proliferation

    Exogenous cytokines (IL-1b and IL-6), prostaglandin E2, and growth factors TGF-b1 and IGF-I had no effect on cell viability over a wide range of concentrations. Only TNF-a significantly reduced cell viability when higher concentrations (more than 100 ng/ml) were used (p < 0.01), especially in long-term experiments (more than seventy-two hours). As shown in Figure 2Figure 2, B, TNF-a (at a nontoxic concentration of 10 ng/ml) and prostaglandin E2 decreased cell proliferation, while TGF-b1 and IGF-I increased it. Neither IL-b1 nor IL-6 affected cell proliferation.

    Cytokine Release in Osteoblasts Induced by Either Titanium Particles or Exogenous Cytokines

    The earliest cytokine release in culture media of titanium-stimulated MG-63 cells was detected after twelve hours, and it was restricted to IL-6 (Fig. 3Fig. 3, A). There were undetectable amounts of IL-1 and TNF-a in culture media of either untreated or particle-challenged MG-63 cells. A basal TGF-b1 secretion was enhanced in particle-treated cultures after seventy-two hours (Fig. 3Fig. 3, B).
    As found in titanium-stimulated MG-63 cultures, only IL-6 and TGF-b1 secretion was modified by exogenous mediators. Only TNF-a at a nontoxic concentration (10 ng/ml) had a significant effect on IL-6 release (p < 0.01) (Fig. 4Fig. 4, A), whereas the basal TGF-b1 secretion was increased (p < 0.05) by exogenous TNF-a, IGF-I, or prostaglandin E2 (Fig. 4Fig. 4, B).

    Suppression of Osteoblast-Specific Gene Expression

    We reported a 40% to 60% suppression of procollagen a1[I] mRNA expression in MG-63 osteoblasts exposed to titanium particles17,25. To further characterize the effect of particles on osteoblast-specific gene expression and protein synthesis, MG-63 cells were exposed to titanium, titanium-alloy, chromium-orthophosphate, polystyrene, polyethylene, and Fluoresbrite particles for forty-eight hours. Particles, regardless of composition, significantly suppressed procollagen a1[I] mRNA expression in MG-63 osteoblasts (p < 0.05) (Fig. 5Fig. 5). This downregulation of collagen gene expression was accompanied by reduced type-I collagen protein synthesis. In contrast to procollagen gene expression, none of the particles significantly altered the expression of osteocalcin or other osteoblast-specific genes such as osteonectin or alkaline phosphatase. These data demonstrate that particles differentially affect gene expression in osteoblasts (for example, procollagen a1[I] compared with osteocalcin) (Fig. 5Fig. 5), and the gene-specific effect is a general response to particles and is not specific to particles of a particular composition.

    Effect of Exogenous Cytokines on Procollagen a1[I] Gene Expression

    An increased IL-6 secretion in titanium-stimulated osteoblasts (Fig. 3Fig. 3, A) correlated inversely with the suppression of procollagen a1[I] mRNA and reduced collagen synthesis in all particulate-stimulated osteoblast cultures. Neither exogenous IL-6 (Fig. 6Fig. 6, A) nor neutralizing antibodies to IL-6 (data not shown) altered the collagen gene expression in the presence or absence of titanium particles, indicating that procollagen a1[I] gene regulation was independent of IL-6 or IL-6-induced transcription factors in osteoblasts. In contrast, the effect of exogenous TNF-a on procollagen a1[I] gene expression was highly comparable with the effect of titanium particles (Fig. 6Fig. 6, A), and this correlated with reduced type-I collagen synthesis25. Prostaglandin E2 also inhibited procollagen a1[I] gene expression (data not shown). Exogenous IL-1b significantly reversed titanium-induced procollagen a1[I] gene suppression (p < 0.05) (Fig. 6Fig. 6, A). Growth factors IGF-I and TGF-b1 significantly increased collagen gene expression (p < 0.05) and could completely reverse the titanium-induced suppression of procollagen a1[I] mRNA (Fig. 6Fig. 6, B).

    Effect of Transcriptional, Translational, and Protein Transport Inhibitors on Cytokine Release and Procollagen a1[I] Gene Expression

    To determine whether an effect of a freshly synthesized cytokine was involved in the titanium-induced procollagen a1[I] gene suppression and to distinguish the mechanism of titanium-induced IL-6 production from procollagen a1[I] gene suppression at the molecular level, MG-63 cells were treated with various inhibitors prior to stimulation with titanium particles. Actinomycin D, a potent inhibitor of transcriptional events by inhibiting RNA polymerase II, was used as a positive control. This compound blocked both procollagen a1[I] mRNA transcription and IL-6 production. Translational (protein-synthesis) inhibitor cyclohexamide, protein-transport inhibitor brefeldin A, and monensin (a nonselective inhibitor of the release of newly synthesized protein from the Golgi apparatus) uniformly blocked the release of IL-6. In contrast, none of these chemicals modified titanium-particle-induced suppression of the procollagen a1[I] mRNA level (Fig. 7Fig. 7), confirming our recent observation that particle phagocytosis has a direct effect on procollagen gene expression through the activation of the protein tyrosine kinase-NF-kB pathway25. Taken together, particle phagocytosis has a direct effect on procollagen a1[I] mRNA, whereas particle-induced cytokine release requires factors for protein synthesis and intracellular trafficking.
    Particulate wear debris from prosthetic components is continuously generated and phagocytosed by cells of the periprosthetic soft tissue. Phagocytosis is a strong signal for cells, first inducing a series of upstream events of cell stimulation through the activation of protein tyrosine kinases19,23,25,36,37. The activation of protein tyrosine kinases leads to the activation of nuclear transcription factors. These nuclear transcription factors then are translocated into the nucleus, resulting in the upregulation of various genes, including proinflammatory cytokines. In a broader sense, all cell types of the periprosthetic soft tissue (macrophages, fibroblasts, osteoclasts, and osteoblasts) are able to phagocytose particulate wear debris, and virtually all cells can reach an activated state. These cells produce a number of cytokines, chemokines, and prostaglandins, which may further affect the function of cells in either an autocrine or a paracrine manner with use of distinct signaling mechanisms.
    Bone is a dynamic tissue with a well-balanced homeostasis preserved by both formation and resorption of bone. Normal turnover of bone, however, can be unbalanced by either increased osteoclast activity or decreased osteoblast function; either mechanism or both mechanisms may result in a net loss of bone. Both osteoclasts and osteoblasts phagocytose particles in vitro, and it is assumed that this process may occur in vivo as well. Osteoblasts, which phagocytose particles, become activated and produce IL-625 and prostaglandin E231, simultaneously losing their capacity to synthesize type-I collagen17,25. The secreted IL-638-42 and prostaglandin E238,43 then activate osteoclasts in a paracrine fashion, which are assumed to already be in an activated state because of phagocytosed particles at the interface16,44. Other cytokines such as IL-1b and TNF-a, secreted by particle-stimulated macrophages/monocytes6,11,15,24,26-30, are also present in the periprosthetic tissue. Tumor necrosis factor-a can activate osteoblasts to secrete IL-6 and suppress type-I collagen synthesis25,45,46, an effect similar to that described for particle phagocytosis (Fig. 3Figs. 3, A;Fig. 44, A; and Fig. 66, A). In addition, both IL-1b and TNF-a induce osteoclast differentiation from precursors and activate differentiated osteoclasts in vitro38,42,43. Taken together, phagocytosis directly affects and phagocytosis-induced cytokine release indirectly affects the bone turnover negatively by altering osteoblast and osteoclast functions.
    From the osteoblast side, a phagocytosis-induced direct signal and exogenous TNF-a (paracrine effect) seem to be the most potent inducers of diminished type-I collagen synthesis. However, the particle-induced and TNF-a-induced signaling mechanisms must be independent because (1) we were unable to detect TNF-a in either particle-treated MG-63 (Fig. 3Fig. 3) or bone-marrow-derived primary human osteoblast cultures25, (2) neutralizing anti-TNF-a antibody could abolish the exogenous TNF-a effect but did not modify the osteoblast response to titanium particles (data not shown), and (3) protein synthesis inhibitors, while blocking cytokine release, had no influence on particle-induced procollagen a1[I] gene suppression (Fig. 7Fig. 7).
    While neither exogenous nor endogenous IL-6 can affect osteoblast-specific functions, IL-6 along with the IL-6 soluble receptor could enhance different osteoblast responses47-49. The IL-6 receptor complex consists of two transmembrane proteins: a ligand-binding chain (IL-6 receptor) and a non-ligand-binding signal transducer, glycoprotein 130 (gp130). Interleukin-6 binding to the ligand-binding chain triggers heterodimerization of the two chains, and then the cytoplasmic domain of the gp130 chain transduces the signal. The soluble form of the ligand-binding chain (soluble IL-6 receptor) is also able to activate gp130 when IL-6 binds to it. It is likely that MG-63 osteoblasts express gp130 but not the ligand-binding chain47,49. Therefore, neither secreted nor exogenous IL-6 can bind to the IL-6 receptor. As a result, no signal can be transferred from the cell surface to the cell41,47-50.
    Among a number of cytokines and growth factors, IGF-I and TGF-b1 were able to completely reverse the suppressive effect of particles on procollagen a1[I] gene expression. These growth factors, when used alone, significantly upregulated the procollagen a1[I] gene expression (Fig. 6Fig. 6, B) and type-I collagen synthesis. Furthermore, these growth factors increased osteoblast proliferation without affecting cell viability or inducing substantial IL-6 secretion. Thus, IGF-I and TGF-b1 seem to be potent inducers of bone matrix formation.
    One of the most important findings of the present study is that, in addition to a direct effect of particles on osteoblast functions17,25, the proinflammatory cytokine TNF-a also exhibits a massive and substantial effect on procollagen a1[I] gene expression, cell proliferation, cell viability, and IL-6 secretion in osteoblasts. While this proinflammatory cytokine induces bone resorption via osteoclast activation, it also contributes to bone loss via reduced bone formation by osteoblasts. Since TNF-a, IL-1b, and IL-6 are present and are continuously secreted by particle-stimulated cells in the periprosthetic space, their long-term in vivo autocrine and paracrine effects are critical in the pathogenesis of the periprosthetic osteolysis. Eventually, local delivery of certain growth factors (IGF-I or TGF-b1), protein tyrosine kinase, or NF-kB inhibitors25-all of which can reverse the suppressive effect of either proinflammatory cytokines or wear particles on type-I collagen synthesis in osteoblasts-may have the therapeutic potential to prevent or treat periprosthetic bone loss.
    Note: The authors thank József Dobai, MD, Ramesh Narayanan, PhD, David Gerard, BA, and Sonja Velins, MLA, for their technical help. We also appreciate our valuable discussions with Rick Sumner, PhD, Tom Turner, DVM, and a number of visitors to the Section of Biochemistry and Molecular Biology of the Department of Orthopedic Surgery at Rush University (Chicago, Illinois).
    Bargar WL; Murzic WJ; Taylor JK; Newman MA; and Paul HA: Management of bone loss in revision total hip arthroplasty using custom cementless femoral components. J Arthroplasty,1993.8: 245-52, 8245  1993  [PubMed]
     
    Goldring SR; Clark CR; and Wright TM: The problem in total joint arthroplasty: aseptic loosening [editorial]. J Bone Joint Surg Am,1993.75: 799-801, 75799  1993  [PubMed]
     
    Huddleston HD: Femoral lysis after cemented hip arthroplasty. J Arthroplasty,1988.3: 285-97, 3285  1988  [PubMed]
     
    Turner TM; Urban RM; Sumner DR; and Galante JO: Revision, without cement, of aseptically loose, cemented total hip prostheses. Quantitative comparison of the effects of four types of medullary treatment on bone ingrowth in a canine model. J Bone Joint Surg Am,1993.75: 845-62, 75845  1993  [PubMed]
     
    Goldring SR; Schiller AL; Roelke M; Rourke CM; O'Neill DA; and Harris WH: The synovial-like membrane at the bone-cement interface in loose total hip replacements and its proposed role in bone lysis. J Bone Joint Surg Am,1983.65: 575-84, 65575  1983  [PubMed]
     
    Jiranek WA; Machado M; Jasty M; Jevsevar D; Wolfe HJ; Goldring SR; Goldberg MJ; and Harris WH.: Production of cytokines around loosened cemented acetabular components. Analysis with immunohistochemical techniques and in situ hybridization. J Bone Joint Surg Am,1993.75: 863-79, 75863  1993  [PubMed]
     
    Linder L; Lindberg L; and Carlsson A.: Aseptic loosening of hip prostheses. A histologic and enzyme histochemical study. Clin Orthop,1983.175: 93-104, 17593  1983  [PubMed]
     
    Santavirta S; Konttinen YT; Bergroth V; Eskola A; Tallroth K; and Lindholm TS: Aggressive granulomatous lesions associated with hip arthroplasty. Immunopathological studies. J Bone Joint Surg Am,1990.72: 252-8, 72252  1990  [PubMed]
     
    Ballard WT, Shanbhag AS, Jacobs JJ. Particle debris. In: Callaghan JJ, Rosenberg AG, Rubash H, editors. The adult hip. Philadelphia: Lippincott-Raven; 1998. p 279-88 
     
    Bauer TW: Identification of orthopaedic wear debris [editorial]. J Bone Joint Surg Am,1996.78: 479-83, 78479  1996  [PubMed]
     
    Glant TT; Jacobs JJ; Mikecz K; Yao J; Chubinskaja S; Williams JM; and Urban RL, Shanbhag AS, Lee S, Sumner DR: Particulate-induced, prostaglandin- and cytokine-mediated bone resorption in an experimental system and in failed joint replacements. Am J Ther,1996.3: 27-41, 327  1996  [PubMed]
     
    Jacobs JJ; Shanbhag A; Glant TT; Black J; and Galante JO: Wear debris in total joint replacements. J Am Acad Orthop Surg,1994.2: 212-20, 2212  1994  [PubMed]
     
    Margevicius KJ; Bauer TW; McMahon JT; Brown SA; and Merritt K: Isolation and characterization of debris in membranes around total joint prostheses. J Bone Joint Surg Am,1994.76: 1664-75, 761664  1994  [PubMed]
     
    Shanbhag AS; Jacobs JJ; Glant TT; Gilbert JL; Black J; and Galante JO: Composition and morphology of wear debris in failed uncemented total hip replacement arthroplasty. J Bone Joint Surg Br,1994.76: 60-7, 7660  1994  [PubMed]
     
    Blaine TA; Rosier RN; Puzas JE; Looney RJ; Reynolds PR; Reynolds SD; and O'Keefe RJ: Increased levels of tumor necrosis factor-alpha and interleukin-6 protein and messenger RNA in human peripheral blood monocytes due to titanium particles. J Bone Joint Surg Am,1996.78: 1181-92, 781181  1996  [PubMed]
     
    Wang W; Ferguson DJ; Quinn JM; Simpson AH; and Athanasou NA: Biomaterial particle phagocytosis by bone-resorbing osteoclasts. J Bone Joint Surg Br,1997.79: 849-56, 79849  1997  [PubMed]
     
    Yao J; Cs-Szabó G; Jacobs JJ; Kuettner KE; and Glant TT: Suppression of osteoblast function by titanium particles. J Bone Joint Surg Am,1997.79: 107-12, 79107  1997  [PubMed]
     
    Yao J; Glant TT; Lark MW; Mikecz K; Jacobs JJ; Hutchinson NI; Hoerrner LA; Kuettner KE; and Galante JO: The potential role of fibroblasts in periprosthetic osteolysis: fibroblast response to titanium particles. J Bone Miner Res,1995.10: 1417-27, 101417  1995  [PubMed]
     
    Allen LA, Aderem A: Mechanisms of phagocytosis. Curr Opin Immunol,1996.8: 36-40, 836  1996  [PubMed]
     
    Davis W; Harrison PT; Hutchinson MJ; and Allen JM.: Two distinct regions of FC gamma RI initiate separate signalling pathways involved in endocytosis and phagocytosis. Embo J,1995.14: 432-41, 14432  1995  [PubMed]
     
    Lowry MB; Duchemin AM; Robinson JM; and Anderson CL: Functional separation of pseudopod extension and particle internalization during Fc gamma receptor-mediated phagocytosis. J Exp Med,1998.187: 161-76, 187161  1998  [PubMed]
     
    Blaine TA; Pollice PF; Rosier RN; Reynolds PR; Puzas JE; and O'Keefe RJ: Modulation of the production of cytokines in titanium-stimulated human peripheral blood monocytes by pharmacological agents. The role of cAMP-mediated signaling mechanisms. J Bone Joint Surg Am,1997.79: 1519-28, 791519  1997  [PubMed]
     
    Greenberg S: Signal transduction of phagocytosis. Trends Cell Biol,1995.5: 93-9, 593  1995  [PubMed]
     
    Nakashima Y; Sun DH; Trindade MC; Maloney WJ; Goodman SB; Schurman DJ; and Smith RL.: Signaling pathways for tumor necrosis factor-alpha and interleukin-6 expression in human macrophages exposed to titanium-alloy particulate debris in vitro. J Bone Joint Surg Am,1999.81: 603-15, 81603  1999  [PubMed]
     
    Vermes C; Roebuck KA; Chandrasekaran R; Dobai JG; Jacobs JJ; and Glant TT.: Particulate wear debris activates protein tyrosine kinases and nuclear factor-kappaB, which down-regulates type I collagen synthesis in human osteoblasts. J Bone Miner Res,2000.15: 1756-65, 151756  2000  [PubMed]
     
    Glant TT; Jacobs JJ; Molnár G; Shanbhag AS; Valyon M; and Galante JO: Bone resorption activity of particulate-stimulated macrophages. J Bone Miner Res,1993.8: 1071-9, 81071  1993  [PubMed]
     
    González O; Smith RL; and Goodman SB: Effect of size, concentration, surface area, and volume of polymethylmethacrylate particles on human macrophages in vitro. J Biomed Mater Res,1996.30: 463-73, 30463  1996  [PubMed]
     
    Lee SH; Brennan FR; Jacobs JJ; Urban RM; Ragasa DR; and Glant TT: Human monocyte/macrophage response to cobalt-chromium corrosion products and titanium particles in patients with total joint replacements. J Orthop Res,1997.15: 40-9, 1540  1997  [PubMed]
     
    Shanbhag AS; Jacobs JJ; Black J; Galante JO; and Glant TT: Human monocyte response to particulate biomaterials generated in vivo and in vitro. J Orthop Res,1995.13: 792-801, 13792  1995  [PubMed]
     
    Shanbhag AS; Jacobs JJ; Black J; Galante JO; and Glant TT: Cellular mediators secreted by interfacial membranes obtained at revision total hip arthroplasty. J Arthroplasty,1995.10: 498-506, 10498  1995  [PubMed]
     
    Dean DD; Schwartz Z; Liu Y; Blanchard CR; Agrawal CM; Mabrey JD; Sylvia VL; Lohmann CH; and Boyan BD: The effect of ultra-high molecular weight polyethylene wear debris on MG63 osteosarcoma cells in vitro. J Bone Joint Surg Am,1999.81: 452-61, 81452  1999  [PubMed]
     
    Rippe RA; Schrum LW; Stefanovic B; Solis-Herruzo JA; and Brenner DA: NF-kappaB inhibits expression of the alpha1(I) collagen gene. DNA Cell Biol,1999.18: 751-61, 18751  1999  [PubMed]
     
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    Anchor for JumpAnchor for Jump
    +Fig. 1-A:The number of phagocytosed Fluoresbrite particles in a single cell is shown at different time-points.
    Anchor for JumpAnchor for Jump
    +Fig. 1-B:The number of phagocytosed Fluoresbrite particles in a single cell is shown at different time-points.
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    +Fig. 1-C:The number of phagocytosed Fluoresbrite particles in a single cell is shown at different time-points.
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    +Fig. 2:Effect of titanium particles and exogenous mediators on MG-63 cell proliferation. Cells were not treated or were treated either with different concentrations of titanium particles (panel A) or with exogenous cytokines and growth factors (panel B). The level of proliferation was measured with [3H]-thymidine incorporation and was normalized to untreated samples (100%) at each time-point. Error bars are omitted for clarity, but the broken line indicates significance at a minimum level of p < 0.05 in panel A. In panel B, * indicates a level of significance (relative to untreated cells) of p < 0.05 and ** indicates a level of p < 0.01.
    Anchor for JumpAnchor for Jump
    +Fig. 3:Effect of titanium particles on production of IL-6 and TGF-b1 by MG-63 cells. Confluent osteoblast cultures were not treated or were treated with 0.1% (volume/volume) titanium particles. Levels of IL-6, TNF-a, IL-1b, and TGF-b1 were measured with enzyme-linked immunosorbent assays at various time-points. Only IL-6 (panel A) and TGF-b1 (panel B) reached detectable and significantly elevated levels, with * indicating a p value of less than 0.05 and ** indicating a p value of less than 0.01.
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    +Fig. 4:Effect of exogenous cytokines on the release of cytokines by MG-63 cells. Confluent osteoblast cultures were not treated or were treated with exogenous IL-6, TNF-a, IL-1b, TGF-b1, IGF-I, or prostaglandin E2 as described in Materials and Methods. Conditioned media were collected at various time-points, and cytokine levels were measured with enzyme-linked immunosorbent assays. Only IL-6 (panel A) and TGF-b1 (panel B) reached detectable and significantly elevated levels, with * indicating a p value of less than 0.05 and ** indicating a p value of less than 0.01.
    Anchor for JumpAnchor for Jump
    +Fig. 5:The effect of various particles on procollagen a1[I] and osteocalcin gene expressions in MG-63 cells. Confluent cell cultures were deprived of serum for twenty-four hours and were left untreated (lanes 1 and 10) or were treated with different particles for forty-eight hours at the various concentrations indicated. The level of gene expression was compared with that in untreated samples. Columns represent means of duplicates of at least five independent experiments (and the standard deviation) of procollagen a1[I] gene expression. * indicates a p value of less than 0.05, and ** indicates a p value of less than 0.01. The osteocalcin gene expression in particle-treated MG-63 cells showed no significant differences, and a representative hybridization panel (OC) is shown. All types of particles significantly reduced the procollagen a1[I] mRNA expression.
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    +Fig. 6:Northern blot analysis of procollagen a1[I] rnRNA expression in MG-63 cells treated with different cytokines (panel A) or growth factors (panel B) in the presence or absence of phagocytosable-size titanium particles. Confluent osteoblast cultures were deprived of serum for twenty-four hours and were pretreated with cytokine/growth factor for three hours, and then titanium particles (0.1%, volume/volume) were added where indicated. Bottom panels show the amounts of total (ribosomal) RNA on an ethidium bromide-stained membrane prior to hybridization. Columns represent means of duplicates of at least five independent experiments and the standard deviation. Data are normalized to the mRNA level measured in nonstimulated MG-63 cells (lane 1 in both panels). * indicates a p value of less than 0.05, and ** indicates a p value of less than 0.01. Neither IL-6 nor IL-1b had an effect on procollagen a1[I] gene expression in the particle-free condition, although IL-1b could partially compensate for the suppressive effect of titanium on procollagen a1[I] gene expression.
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    +Fig. 7:Effect of protein synthesis and transport inhibitors on procollagen a1[I] gene expression. Confluent MG-63 osteoblast cultures were deprived of serum for twenty-four hours and were left untreated or were pretreated with the indicated compound for three hours, and then titanium particles (0.1% volume/volume) were added where shown. The level of gene expression was analyzed by Northern blots to determine procollagen a1[I] mRNA and was compared with that in untreated samples (lane 1). Columns represent means of duplicates of at least five independent experiments and the standard deviation. * indicates a p value of less than 0.05, and ** indicates a p value of less than 0.01. None of the compounds were able to reverse the particle-treatment-induced gene suppression.
    Bargar WL; Murzic WJ; Taylor JK; Newman MA; and Paul HA: Management of bone loss in revision total hip arthroplasty using custom cementless femoral components. J Arthroplasty,1993.8: 245-52, 8245  1993  [PubMed]
     
    Goldring SR; Clark CR; and Wright TM: The problem in total joint arthroplasty: aseptic loosening [editorial]. J Bone Joint Surg Am,1993.75: 799-801, 75799  1993  [PubMed]
     
    Huddleston HD: Femoral lysis after cemented hip arthroplasty. J Arthroplasty,1988.3: 285-97, 3285  1988  [PubMed]
     
    Turner TM; Urban RM; Sumner DR; and Galante JO: Revision, without cement, of aseptically loose, cemented total hip prostheses. Quantitative comparison of the effects of four types of medullary treatment on bone ingrowth in a canine model. J Bone Joint Surg Am,1993.75: 845-62, 75845  1993  [PubMed]
     
    Goldring SR; Schiller AL; Roelke M; Rourke CM; O'Neill DA; and Harris WH: The synovial-like membrane at the bone-cement interface in loose total hip replacements and its proposed role in bone lysis. J Bone Joint Surg Am,1983.65: 575-84, 65575  1983  [PubMed]
     
    Jiranek WA; Machado M; Jasty M; Jevsevar D; Wolfe HJ; Goldring SR; Goldberg MJ; and Harris WH.: Production of cytokines around loosened cemented acetabular components. Analysis with immunohistochemical techniques and in situ hybridization. J Bone Joint Surg Am,1993.75: 863-79, 75863  1993  [PubMed]
     
    Linder L; Lindberg L; and Carlsson A.: Aseptic loosening of hip prostheses. A histologic and enzyme histochemical study. Clin Orthop,1983.175: 93-104, 17593  1983  [PubMed]
     
    Santavirta S; Konttinen YT; Bergroth V; Eskola A; Tallroth K; and Lindholm TS: Aggressive granulomatous lesions associated with hip arthroplasty. Immunopathological studies. J Bone Joint Surg Am,1990.72: 252-8, 72252  1990  [PubMed]
     
    Ballard WT, Shanbhag AS, Jacobs JJ. Particle debris. In: Callaghan JJ, Rosenberg AG, Rubash H, editors. The adult hip. Philadelphia: Lippincott-Raven; 1998. p 279-88 
     
    Bauer TW: Identification of orthopaedic wear debris [editorial]. J Bone Joint Surg Am,1996.78: 479-83, 78479  1996  [PubMed]
     
    Glant TT; Jacobs JJ; Mikecz K; Yao J; Chubinskaja S; Williams JM; and Urban RL, Shanbhag AS, Lee S, Sumner DR: Particulate-induced, prostaglandin- and cytokine-mediated bone resorption in an experimental system and in failed joint replacements. Am J Ther,1996.3: 27-41, 327  1996  [PubMed]
     
    Jacobs JJ; Shanbhag A; Glant TT; Black J; and Galante JO: Wear debris in total joint replacements. J Am Acad Orthop Surg,1994.2: 212-20, 2212  1994  [PubMed]
     
    Margevicius KJ; Bauer TW; McMahon JT; Brown SA; and Merritt K: Isolation and characterization of debris in membranes around total joint prostheses. J Bone Joint Surg Am,1994.76: 1664-75, 761664  1994  [PubMed]
     
    Shanbhag AS; Jacobs JJ; Glant TT; Gilbert JL; Black J; and Galante JO: Composition and morphology of wear debris in failed uncemented total hip replacement arthroplasty. J Bone Joint Surg Br,1994.76: 60-7, 7660  1994  [PubMed]
     
    Blaine TA; Rosier RN; Puzas JE; Looney RJ; Reynolds PR; Reynolds SD; and O'Keefe RJ: Increased levels of tumor necrosis factor-alpha and interleukin-6 protein and messenger RNA in human peripheral blood monocytes due to titanium particles. J Bone Joint Surg Am,1996.78: 1181-92, 781181  1996  [PubMed]
     
    Wang W; Ferguson DJ; Quinn JM; Simpson AH; and Athanasou NA: Biomaterial particle phagocytosis by bone-resorbing osteoclasts. J Bone Joint Surg Br,1997.79: 849-56, 79849  1997  [PubMed]
     
    Yao J; Cs-Szabó G; Jacobs JJ; Kuettner KE; and Glant TT: Suppression of osteoblast function by titanium particles. J Bone Joint Surg Am,1997.79: 107-12, 79107  1997  [PubMed]
     
    Yao J; Glant TT; Lark MW; Mikecz K; Jacobs JJ; Hutchinson NI; Hoerrner LA; Kuettner KE; and Galante JO: The potential role of fibroblasts in periprosthetic osteolysis: fibroblast response to titanium particles. J Bone Miner Res,1995.10: 1417-27, 101417  1995  [PubMed]
     
    Allen LA, Aderem A: Mechanisms of phagocytosis. Curr Opin Immunol,1996.8: 36-40, 836  1996  [PubMed]
     
    Davis W; Harrison PT; Hutchinson MJ; and Allen JM.: Two distinct regions of FC gamma RI initiate separate signalling pathways involved in endocytosis and phagocytosis. Embo J,1995.14: 432-41, 14432  1995  [PubMed]
     
    Lowry MB; Duchemin AM; Robinson JM; and Anderson CL: Functional separation of pseudopod extension and particle internalization during Fc gamma receptor-mediated phagocytosis. J Exp Med,1998.187: 161-76, 187161  1998  [PubMed]
     
    Blaine TA; Pollice PF; Rosier RN; Reynolds PR; Puzas JE; and O'Keefe RJ: Modulation of the production of cytokines in titanium-stimulated human peripheral blood monocytes by pharmacological agents. The role of cAMP-mediated signaling mechanisms. J Bone Joint Surg Am,1997.79: 1519-28, 791519  1997  [PubMed]
     
    Greenberg S: Signal transduction of phagocytosis. Trends Cell Biol,1995.5: 93-9, 593  1995  [PubMed]
     
    Nakashima Y; Sun DH; Trindade MC; Maloney WJ; Goodman SB; Schurman DJ; and Smith RL.: Signaling pathways for tumor necrosis factor-alpha and interleukin-6 expression in human macrophages exposed to titanium-alloy particulate debris in vitro. J Bone Joint Surg Am,1999.81: 603-15, 81603  1999  [PubMed]
     
    Vermes C; Roebuck KA; Chandrasekaran R; Dobai JG; Jacobs JJ; and Glant TT.: Particulate wear debris activates protein tyrosine kinases and nuclear factor-kappaB, which down-regulates type I collagen synthesis in human osteoblasts. J Bone Miner Res,2000.15: 1756-65, 151756  2000  [PubMed]
     
    Glant TT; Jacobs JJ; Molnár G; Shanbhag AS; Valyon M; and Galante JO: Bone resorption activity of particulate-stimulated macrophages. J Bone Miner Res,1993.8: 1071-9, 81071  1993  [PubMed]
     
    González O; Smith RL; and Goodman SB: Effect of size, concentration, surface area, and volume of polymethylmethacrylate particles on human macrophages in vitro. J Biomed Mater Res,1996.30: 463-73, 30463  1996  [PubMed]
     
    Lee SH; Brennan FR; Jacobs JJ; Urban RM; Ragasa DR; and Glant TT: Human monocyte/macrophage response to cobalt-chromium corrosion products and titanium particles in patients with total joint replacements. J Orthop Res,1997.15: 40-9, 1540  1997  [PubMed]
     
    Shanbhag AS; Jacobs JJ; Black J; Galante JO; and Glant TT: Human monocyte response to particulate biomaterials generated in vivo and in vitro. J Orthop Res,1995.13: 792-801, 13792  1995  [PubMed]
     
    Shanbhag AS; Jacobs JJ; Black J; Galante JO; and Glant TT: Cellular mediators secreted by interfacial membranes obtained at revision total hip arthroplasty. J Arthroplasty,1995.10: 498-506, 10498  1995  [PubMed]
     
    Dean DD; Schwartz Z; Liu Y; Blanchard CR; Agrawal CM; Mabrey JD; Sylvia VL; Lohmann CH; and Boyan BD: The effect of ultra-high molecular weight polyethylene wear debris on MG63 osteosarcoma cells in vitro. J Bone Joint Surg Am,1999.81: 452-61, 81452  1999  [PubMed]
     
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