scholarly journals Rooibos tea extracts inhibit osteoclast formation and activity through the attenuation of NF-κB activity in RAW264.7 murine macrophages

2018 ◽  
Vol 9 (6) ◽  
pp. 3301-3312 ◽  
Author(s):  
Shaakirah Moosa ◽  
Abe E. Kasonga ◽  
Vishwa Deepak ◽  
Sumari Marais ◽  
Innocentia B. Magoshi ◽  
...  
Keyword(s):  
Inhibitory Effect ◽  
Osteoclast Formation ◽  
Murine Macrophages ◽  
Rooibos Tea ◽  
Potent Inhibitory Effect ◽  
Inhibit Osteoclast Formation

Fermented rooibos extract has more potent inhibitory effect on osteoclasts than unfermented rooibos.

scholarly journals Inhibition of osteoclast differentiation and bone resorption by polyunsaturated fatty acids in RAW 264.7 murine macrophages

2012 ◽  
Vol 31 (1) ◽  
Author(s):  
J. C. Boeyens ◽  
W-H. Chua ◽  
M.C. Kruger ◽  
A.M. Joubert ◽  
M. Coetzee
Keyword(s):  
Fatty Acids ◽  
Bone Resorption ◽  
Polyunsaturated Fatty Acids ◽  
Cell Line ◽  
Osteoclast Differentiation ◽  
Inhibitory Effect ◽  
Osteoclast Formation ◽  
Raw 264.7 ◽  
Murine Macrophages

This study investigated the effects of polyunsaturated fatty acids on osteoclast formation and bone resorption in RAW 264.7 murine pre-osteoclasts. Data obtained suggests an inhibitory effect of these compounds on osteoclastogenesis and bone resorption in the cell line tested.

scholarly journals Proteomic Analysis of Estrogen-Mediated Signal Transduction in Osteoclasts Formation

2015 ◽  
Vol 2015 ◽  
pp. 1-10 ◽  
Author(s):  
Qi Xiong ◽  
Peifu Tang ◽  
Yanpan Gao ◽  
Lihai Zhang ◽  
Wei Ge
Keyword(s):  
Signal Transduction ◽  
Bioinformatics Analysis ◽  
Osteoclast Differentiation ◽  
Inhibitory Effect ◽  
Osteoclast Formation ◽  
Nuclear Factor ◽  
Proteomics Analysis ◽  
Receptor Activator ◽  
Intracellular Pathways ◽  
Inhibit Osteoclast Formation

Estrogen plays an important role in inhibiting osteoclast differentiation and protecting against bone loss from osteoporosis, especially in postmenopausal women. However, the precise mechanisms underlying the effect of estrogen on osteoclasts are not well known. In the present study, we performed proteomics analysis and bioinformatics analysis to comprehensively compare the differential expression of proteins in receptor activator of nuclear factor-κB ligand RANKL-induced osteoclasts in the presence and absence of estrogen. We identified 6403 proteins, of which 124 were upregulated and 231 were downregulated by estrogen. Bioinformatics analysis showed that estrogen treatment interfered with 77 intracellular pathways, including both confirmed canonical and unconfirmed pathways of osteoclast formation. Our findings validate the inhibitory effect of estrogen on osteoclasts via the promotion of apoptosis and suppression of differentiation and polarization and suggest that estrogen might inhibit osteoclast formation via other pathways, which requires further investigation and verification.

scholarly journals GPR120 Inhibits RANKL-Induced Osteoclast Formation and Resorption by Attenuating Reactive Oxygen Species Production in RAW264.7 Murine Macrophages

2021 ◽  
Vol 22 (19) ◽  
pp. 10544
Author(s):  
Cynthia Sithole ◽  
Carla Pieterse ◽  
Kayla Howard ◽  
Abe Kasonga
Keyword(s):  
Reactive Oxygen Species ◽  
Reactive Oxygen ◽  
Nuclear Factor Κb ◽  
Osteoclast Formation ◽  
Ros Production ◽  
Oxygen Species ◽  
Murine Macrophages ◽  
Multinucleated Cells ◽  
Raw264.7 Macrophages ◽  
Inhibit Osteoclast Formation

Osteoclasts are large, multinucleated cells that are responsible for the resorption of bone. Bone degenerative diseases, such as osteoporosis, are characterized by overactive osteoclasts. Receptor activator of nuclear factor-κB (NF-κB) ligand (RANKL) binding to its receptor on osteoclast precursors will trigger osteoclast formation and resorption. The production of reactive oxygen species (ROS) is known to play a crucial role in RANKL-induced osteoclast formation and resorption. G-protein coupled receptor 120 (GPR120) signalling has been shown to affect osteoclast formation, but the exact mechanisms of action require further investigation. RAW264.7 murine macrophages were seeded into culture plates and exposed to the GPR120 agonist, TUG-891, at varying concentrations (20–100 µM) and RANKL to induce osteoclast formation. TUG-891 was shown to inhibit osteoclast formation and resorption without affecting cell viability in RAW264.7 macrophages. TUG-891 further decreased ROS production when compared to RANKL only cells. Antioxidant proteins, Nrf2, HO-1 and NQO1 were shown to be upregulated while the ROS inducing protein, Nox1, was downregulated by TUG-891. Gene silencing revealed that TUG-891 exerted its effects specifically through GPR120. This study reveals that GPR120 signalling may inhibit osteoclast formation and resorption through inhibition on ROS production.

scholarly journals Aquatic Toxicity of Photocatalyst Nanoparticles to Green Microalgae Chlorella vulgaris

Water ◽  
2020 ◽  
Vol 13 (1) ◽  
pp. 77
Author(s):  
Cristina Adochite ◽  
Luminita Andronic
Keyword(s):  
Chlorella Vulgaris ◽  
Advanced Oxidation Process ◽  
Growth Parameters ◽  
Aquatic Toxicity ◽  
Basal Medium ◽  
Inhibitory Effect ◽  
Synthesis Methods ◽  
Potent Inhibitory Effect ◽  
Density Surface ◽  
The Impact

In the last years, nanoparticles such as TiO2, ZnO, NiO, CuO and Fe2O3 were mainly used in wastewater applications. In addition to the positive aspects concerning using nanoparticles in the advanced oxidation process of wastewater containing pollutants, the impact of these nanoparticles on the environment must also be investigated. The toxicity of nanoparticles is generally investigated by the nanomaterials’ effect on green algae, especially on Chlorella vulgaris. In this review, several aspects are reviewed: the Chlorella vulgaris culture monitoring and growth parameters, the effect of different nanoparticles on Chlorella vulgaris, the toxicity of photocatalyst nanoparticles, and the mechanism of photocatalyst during oxidative stress on the photosynthetic mechanism of Chlorella vulgaris. The Bold basal medium (BBM) is generally recognized as an excellent standard cultivation medium for Chlorella vulgaris in the known environmental conditions such as temperature in the range 20–30 °C and light intensity of around 150 μE·m2·s−1 under a 16/8 h light/dark cycle. The nanoparticles synthesis methods influence the particle size, morphology, density, surface area to generate growth inhibition and further algal deaths at the nanoparticle-dependent concentration. Moreover, the results revealed that nanoparticles caused a more potent inhibitory effect on microalgal growth and severely disrupted algal cells’ membranes.

Osteoclast and osteoblast response to strontium-doped struvite coatings on titanium for improved bone integration

2020 ◽  
Vol 0 (0) ◽  
Author(s):  
Claus Moseke ◽  
Katharina Wimmer ◽  
Markus Meininger ◽  
Julia Zerweck ◽  
Cornelia Wolf-Brandstetter ◽  
...  
Keyword(s):  
Bone Ingrowth ◽  
Osteoclast Differentiation ◽  
Inhibitory Effect ◽  
Osteoclast Formation ◽  
Strontium Nitrate ◽  
Bone Implant ◽  
Electrochemically Deposited ◽  
Bone Integration ◽  
Titanium Substrates

AbstractTo develop implants with improved bone ingrowth, titanium substrates were coated with homogeneous and dense struvite (MgNH4PO4·6H2O) layers by means of electrochemically assisted deposition. Strontium nitrate was added to the coating electrolyte in various concentrations, in order to fabricate Sr-doped struvite coatings with Sr loading ranging from 10.6 to 115 μg/cm2. It was expected and observed that osteoclast activity surrounding the implant was inhibited. The cytocompatibility of the coatings and the effect of Sr-ions in different concentrations on osteoclast formation were analyzed in vitro. Osteoclast differentiation was elucidated on morphological, biochemical as well as on gene expression level. It could be shown that moderate concentrations of Sr2+ had an inhibitory effect on osteoclast formation, while the growth of osteoblastic cells was not negatively influenced compared to pure struvite surfaces. In summary, the electrochemically deposited Sr-doped struvite coatings are a promising approach to improve bone implant ingrowth.

scholarly journals An Anti-Inflammatory 2,4-Cyclized-3,4-Secospongian Diterpenoid and Furanoterpene-Related Metabolites of a Marine Sponge Spongia sp. from the Red Sea

Marine Drugs ◽  
2021 ◽  
Vol 19 (1) ◽  
pp. 38
Author(s):  
Chi-Jen Tai ◽  
Chiung-Yao Huang ◽  
Atallah F. Ahmed ◽  
Raha S. Orfali ◽  
Walied M. Alarif ◽  
...  
Keyword(s):  
Red Sea ◽  
Superoxide Anion ◽  
Dermal Fibroblast ◽  
Fibroblast Cell ◽  
Inhibitory Effect ◽  
Human Dermal Fibroblast ◽  
Superoxide Anion Generation ◽  
Potent Inhibitory Effect ◽  
Anti Inflammatory ◽  
New Compounds

Chemical investigation of a Red Sea Spongia sp. led to the isolation of four new compounds, i.e., 17-dehydroxysponalactone (1), a carboxylic acid, spongiafuranic acid A (2), one hydroxamic acid, spongiafuranohydroxamic acid A (3), and a furanyl trinorsesterpenoid 16-epi-irciformonin G (4), along with three known metabolites (−)-sponalisolide B (5), 18-nor- 3,17-dihydroxy-spongia-3,13(16),14-trien-2-one (6), and cholesta-7-ene-3β,5α-diol-6-one (7). The biosynthetic pathway for the molecular skeleton of 1 and related compounds was postulated for the first time. Anti-inflammatory activity of these metabolites to inhibit superoxide anion generation and elastase release in N-formyl-methionyl-leucyl phenylalanine/cytochalasin B (fMLF/CB)-induced human neutrophil cells and cytotoxicity of these compounds toward three cancer cell lines and one human dermal fibroblast cell line were assayed. Compound 1 was found to significantly reduce the superoxide anion generation and elastase release at a concentration of 10 μM, and compound 5 was also found to display strong inhibitory activity against superoxide anion generation at the same concentration. Due to the noncytotoxic activity and the potent inhibitory effect toward the superoxide anion generation and elastase release, 1 and 5 can be considered to be promising anti-inflammatory agents.

Inhibitory effect of ipriflavone on osteoclast-mediated bone resorption and new osteoclast formation in long-term cultures of mouse unfractionated bone cells

1993 ◽  
Vol 53 (3) ◽  
pp. 206-209 ◽  
Author(s):  
Kohei Notoya ◽  
Keiji Yoshida ◽  
Shigehisa Taketomi ◽  
Iwao Yamazaki ◽  
Masayoshi Kumegawa
Keyword(s):  
Bone Resorption ◽  
Bone Cells ◽  
Inhibitory Effect ◽  
Osteoclast Formation

Lipopolysaccharide-induced sensitization of adenylyl cyclase activity in murine macrophages

2006 ◽  
Vol 290 (1) ◽  
pp. C143-C151 ◽  
Author(s):  
Y. Osawa ◽  
H. T. Lee ◽  
C. A. Hirshman ◽  
D. Xu ◽  
C. W. Emala
Keyword(s):  
Protein Synthesis ◽  
Adenylyl Cyclase ◽  
Actinomycin D ◽  
Inhibitory Effect ◽  
Cytokine Release ◽  
Adenylyl Cyclase Activity ◽  
Phosphorylation State ◽  
Murine Macrophages ◽  
Dependent Pathway ◽  
New Protein

LPS is known to modulate macrophage responses during sepsis, including cytokine release, phagocytosis, and proliferation. Although agents that elevate cAMP reverse LPS-induced macrophage functions, whether LPS itself modulates cAMP and whether LPS-induced decreases in proliferation are modulated via a cAMP-dependent pathway are not known. Murine macrophages (RAW264.7 cells) were treated with LPS in the presence or absence of inhibitors of prostaglandin signaling, protein kinases, CaM, Giproteins, and NF-κB translocation or transcription/translation. LPS effects on CaMKII phosphorylation and the expression of relevant adenylyl cyclase (AC) isoforms were measured. LPS caused a significant dose (5–10,000 ng/ml)- and time (1–8 h)-dependent increase in forskolin-stimulated AC activity that was abrogated by pretreatment with SN50 (an NF-κB inhibitor), actinomycin D, or cycloheximide, indicating that the effect is mediated via NF-κB-dependent transcription and new protein synthesis. Furthermore, LPS decreased the phosphorylation state of CaMKII, and pretreatment with a CaM antagonist attenuated the LPS-induced sensitization of AC. LPS, cAMP, or PKA activation each independently decreased macrophage proliferation. However, inhibition of NF-κB had no effect on LPS-induced decreased proliferation, indicating that LPS-induced decreased macrophage proliferation can proceed via PKA-independent signaling pathways. Taken together, these findings indicate that LPS induces sensitization of AC activity by augmenting the stimulatory effect of CaM and attenuating the inhibitory effect of CaMKII on isoforms of AC that are CaMK sensitive.

Mobilization of Fibrinogen Receptor Sites on Human Platelets Stimulated with ADP is Prevented by Prostacyclin

1979 ◽  
Author(s):  
J. Hawiger ◽  
S. Parkinson ◽  
S. Timmons
Keyword(s):  
Inhibitory Effect ◽  
Human Platelets ◽  
Affinity Constant ◽  
Human Fibrinogen ◽  
Fibrinogen Receptor ◽  
Receptor Sites ◽  
Plasma Factor ◽  
Potent Inhibitory Effect

Fibrinogen is a plasma factor required for aggregation of human platelets by ADP. The mechanism of platelet-ADP-fibrinogen interaction was studied by measuring the equilibrium binding of 125I-fibrinogen to human platelets separated from plasma proteins. Binding of 125I-fibrinogen to platelets not stimulated with ADP was low and unaffected by an excess of unlabel led fibrinogen. However, when platelets were stimulated with 4μM of ADP, there was an eightfold increase In the number of available binding sites for human fibrinogen, with affinity constant of 1.9 x 109M-1. This striking increase in fibrinogen receptor sites on human platelets was specific for ADP as contrasted to ATP, AMP, and adenosine. Prostacyclin (Prostaglandin I2, PGI2), a novel prostaglandin produced by the blood vessel wall, completely blocked this ADP-induced increase in fibrinogen receptor sites on human platelets. The effect of PGI2 was prompt and concentration dependent, reaching maximum at 10-9M. 6-keto PGF2 a stable derivative ot PGI2, did not have such an effect. Thus movement of fibrinogen receptor sites on human platelet membrane stimulated with ADP is prevented by PGI2. This represents a new biologic property of this vascular hormone and contributes to better understanding of its potent inhibitory effect in vitro and in vivo on ADP-induced platelet aggregation requiring mobilization of fibrinogen receptor.

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