1.The research advancement and the application foreground of 2-methacryloyloxyethyl phosphorylcholine polymer membranes.
Changhe WANG ; Zhaoyang WANG ; Lin CAO ; Ping JIANG ; Cong GUO
Journal of Biomedical Engineering 2007;24(2):470-473
2-methacryloyloxyethyl phosphorylcholine (MPC) polymer membranes are synthesized as biomaterials of the biomembrane structure. The MPC polymer membranes have excellent biocompatibility and blood compatibility, they can effectively reduce protein adsorption and denaturation and inhibit cell adhesion even when the polymer membranes are in contact with whole blood in the absence of any anticoagulants. So, the MPC polymer membranes are widely used in blood purification, artificial organs, membrane oxygenator, and other field of biomedicine. The paper mainly expounds the research advancement and the application prospect of MPC polymer membranes.
Artificial Organs
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Biocompatible Materials
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chemistry
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Humans
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Membranes, Artificial
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Methacrylates
;
chemistry
;
Oxygenators, Membrane
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Phosphorylcholine
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analogs & derivatives
;
chemistry
;
Polymers
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Polymethacrylic Acids
2.Surface Modification of Intraocular Lenses.
Qi HUANG ; George Pak-Man CHENG ; Kin CHIU ; Gui-Qin WANG ;
Chinese Medical Journal 2016;129(2):206-214
OBJECTIVEThis paper aimed to review the current literature on the surface modification of intraocular lenses (IOLs).
DATA SOURCESAll articles about surface modification of IOLs published up to 2015 were identified through a literature search on both PubMed and ScienceDirect.
STUDY SELECTIONThe articles on the surface modification of IOLs were included, but those on design modification and surface coating were excluded.
RESULTSTechnology of surface modification included plasma, ion beam, layer-by-layer self-assembly, ultraviolet radiation, and ozone. The main molecules introduced into IOLs surface were poly (ethylene glycol), polyhedral oligomeric silsesquioxane, 2-methacryloyloxyethyl phosphorylcholine, TiO 2 , heparin, F-heparin, titanium, titanium nitride, vinyl pyrrolidone, and inhibitors of cytokines. The surface modification either resulted in a more hydrophobic lens, a more hydrophilic lens, or a lens with a hydrophilic anterior and hydrophobic posterior surface. Advances in research regarding surface modification of IOLs had led to a better biocompatibility in both in vitro and animal experiments.
CONCLUSIONThe surface modification is an efficient, convenient, economic and promising method to improve the biocompatibility of IOLs.
Animals ; Heparin ; chemistry ; Humans ; Hydrophobic and Hydrophilic Interactions ; Lenses, Intraocular ; Methacrylates ; chemistry ; Ozone ; chemistry ; Phosphorylcholine ; analogs & derivatives ; chemistry ; Ultraviolet Rays
3.A novel protein-repellent dental composite containing 2-methacryloyloxyethyl phosphorylcholine.
Ning ZHANG ; Chen CHEN ; Mary As MELO ; Yu-Xing BAI ; Lei CHENG ; Hockin Hk XU
International Journal of Oral Science 2015;7(2):103-109
Secondary caries due to biofilm acids is a primary cause of dental composite restoration failure. To date, there have been no reports of dental composites that can repel protein adsorption and inhibit bacteria attachment. The objectives of this study were to develop a protein-repellent dental composite by incorporating 2-methacryloyloxyethyl phosphorylcholine (MPC) and to investigate for the first time the effects of MPC mass fraction on protein adsorption, bacteria attachment, biofilm growth, and mechanical properties. Composites were synthesized with 0 (control), 0.75%, 1.5%, 2.25%, 3%, 4.5% and 6% of MPC by mass. A commercial composite was also tested as a control. Mechanical properties were measured in three-point flexure. Protein adsorption onto the composite was determined by the microbicinchoninic acid method. A human saliva microcosm biofilm model was used. Early attachment at 4 h, biofilm at 2 days, live/dead staining and colony-forming units (CFUs) of biofilms grown on the composites were investigated. Composites with MPC of up to 3% had mechanical properties similar to those without MPC and those of the commercial control, whereas 4.5% and 6% MPC decreased the mechanical properties (P<0.05). Increasing MPC from 0 to 3% reduced the protein adsorption on composites (P<0.05). The composite with 3% MPC had protein adsorption that was 1/12 that of the control (P<0.05). Oral bacteria early attachment and biofilm growth were also greatly reduced on the composite with 3% MPC, compared to the control (P<0.05). In conclusion, incorporation of MPC into composites at 3% greatly reduced protein adsorption, bacteria attachment and biofilm CFUs, without compromising mechanical properties. Protein-repellent composites could help to repel bacteria attachment and plaque build-up to reduce secondary caries. The protein-repellent method might be applicable to other dental materials.
Adsorption
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Biofilms
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Colony Count, Microbial
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Composite Resins
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chemistry
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Dental Plaque
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microbiology
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Methacrylates
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analysis
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Phosphorylcholine
;
analogs & derivatives
;
analysis
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Proteins
;
chemistry
4.Perifosine inhibits biofilm formation of Pseudomonas aeruginosa by interacting with PqsE protein.
Peng Fei SHE ; Lan Lan XU ; Ya Qian LIU ; Ze Hao LI ; Sha Sha LIU ; Yi Min LI ; Lin Ying ZHOU ; Yong WU
Chinese Journal of Preventive Medicine 2022;56(2):192-196
To explore the biofilm inhibitory efficacy of perifosine against Pseudomonas aeruginosa (P. aeruginos) and its mechanisms. Twenty-fourwell plate was used to form biofilms at the bottom and crystal violet staining was used to determine the biofilm inhibitory effects of perifosine against P. aeruginosa, the wells without perifosine was set as control group. Glass tubes combined with crystal violet staining was used to detect the gas-liqud interface related bioiflm inhibitory effects of perifosine, the wells without perifosine was set as control group. Time-growth curved was used to detect the effects of perifosine on the bacteial planktonic cells growth of P. aeruginosa, the wells without perifosine was set as control group. The interaction model between perifosine and PqsE was assessed by molecular docking assay. The inhibitory effects of perifosine on the catalytic activity of PqsE was determined by detection the production of thiols, the wells without perifosine was set as control group. Binding affinity between perifosine and PqsE was detected by plasma surface resonance. The biofims at the bottom of the microplates and air-liquid interface were effectively inhibited by perifosine at the concentration of 4-8 μg/ml. There was no influence of perifosine on the cells growth of P. aeruginosa. The resuts of molecular docking assay indicates that perifosine could interacted with PqsE with the docking score of -10.67 kcal/mol. Perifosine could inhibit the catalytic activity of PqsE in a dose-dependent manner. The binding affinity between perifosine and PqsE was comfirmed by plasma surface resonance with KD of 6.65×10-5mol/L. Perifosine could inhibited the biofilm formation of P. aeruginosa by interacting with PqsE.
Anti-Bacterial Agents/pharmacology*
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Bacterial Proteins/metabolism*
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Biofilms
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Molecular Docking Simulation
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Phosphorylcholine/analogs & derivatives*
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Pseudomonas aeruginosa/metabolism*
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Quorum Sensing
5.Synthesis and antitumor activity of selenophosphocholine analogues containing tegafur.
Zhong-Lin ZANG ; Shao-Qiong LIU ; Xiong CHEN ; Yan-Jie LI ; Bing ZHOU ; Xin-Hua XU
Acta Pharmaceutica Sinica 2006;41(12):1184-1187
AIMTo synthesize the selenophosphocholine analogues containing tegafur and test their antitumor activities.
METHODSThe cyclic glyceroselenophospholopid conjugate of tegafur was synthesized by the reaction of hexaethylphosphorous triamide with N1-(2-furanidyl)-N3-(hydroxyalkyl)-5-fluyorouracil and 1-O-hexadecyl glycerol as well as selenium in one-pot. Cyclic glyceroselenophospholopid conjugate of tegafur reacted with triethylamine to give title compounds.
RESULTSSix new compounds have been synthesized. Their structures were confirmed by 1H NMR, 13P NMR and elemental analysis. Antitumor activity of the title compounds against PGA1 was tested.
CONCLUSIONThe reaction of triethylamine with cyclic glyceroselenophospholopid conjugate of tegafur very readily occurred, which was finished within 2 h at room temperature. The opening-ring products of trans isomers showed antimutor activity against human uriaryl bladder cancer cell more effective than that of the tegafur.
Antineoplastic Agents ; chemical synthesis ; pharmacology ; Cell Line, Tumor ; Humans ; Magnetic Resonance Spectroscopy ; Organoselenium Compounds ; chemical synthesis ; pharmacology ; Phosphorylcholine ; analogs & derivatives ; Tegafur ; chemical synthesis ; pharmacology ; Urinary Bladder Neoplasms ; drug therapy ; pathology
6.Effect of 2-methacryloyloxyethyl phosphorylcholine on the protein-repellent property of dental adhesive.
Ning ZHANG ; Ke ZHANG ; Huakun XU ; Yuxing BAI
Chinese Journal of Stomatology 2016;51(3):172-175
OBJECTIVETo evaluate the effect of 2-methacryloyloxyethyl phosphorylcholine (MPC) and nanoparticles of amorphous calcium phosphate (NACP) on the protein-repellent property of dental adhesive.
METHODSMPC and NACP were incorporated into SBMP as the test group. Scotchbond Multi-Purpose (SBMP) was used as control group. Human dentin shear bond strengths were measured. Protein adsorption onto samples was determined by micro bicinchoninic acid (BCA) method. A dental plaque microcosm biofilm model with human saliva as inoculum was used to investigate biofilm viability.
RESULTSThe dentin bond strength of modified group was (28.7±2.2) MPa, which was not significantly different from that of the SBMP control group. The amount of protein adsorption in the modified group and the SBMP control group were (0.21±0.02) µg/cm(2) and (4.17±0.45) µg/cm(2) respectively. Lactic acid production of biofilms in modified group and SBMP control were (7.71 ± 1.01) mmol/L and (19.18 ± 2.34) mmol/L repectively.
CONCLUSIONSMPC-NACP based dental adhesive greatly reduce the protein adsorption and bacterial adhesion, without compromising dentin shear bond strength. This novel bonding agent may have wide application.
Adsorption ; Biofilms ; drug effects ; growth & development ; Calcium Phosphates ; pharmacology ; Dental Cements ; pharmacology ; Dental Plaque ; Dentin ; chemistry ; Humans ; Lactic Acid ; biosynthesis ; Methacrylates ; pharmacology ; Nanoparticles ; Phosphorylcholine ; analogs & derivatives ; pharmacology ; Resin Cements ; pharmacology ; Saliva ; Tensile Strength
7.Pilot study of a cell membrane like biomimetic drug-eluting coronary stent.
Dezeng FAN ; Zhiyuan JIA ; Xinhao YAN ; Xiaolei LIU ; Wei DONG ; Fuyu SUN ; Jian JI ; Jianping XU ; Kefeng REN ; Weidong CHEN ; Jiacong SHEN ; Hong QIU ; Runlin GAO
Journal of Biomedical Engineering 2007;24(3):599-602
A novel bioinspired phospholipid copolymer has been synthesized by the radical polymerization of poly2-Methacryloyloxyethylphosphorylcholine (MPC), stearyl methacrylate (SMA), hydroxypropyl methacrylate (HPMA) and trimethoxysilylpropyl methacrylate (TSMA). Contact angle results indicated that the coating surface rearranged to get a more hydrophilic surface at the polymer/water interface. The membrane mimic phosphorylcholine coating surface could resist the platelet adhesion and prolong plasma recalcification time significantly. Rapamycin was used as model drugs to prepare drug-eluting coating. The animal experiments showed that this novel drug-eluting stent could effectively prevent the phenomena of restenosis.
Angioplasty, Balloon, Coronary
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instrumentation
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Animals
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Coated Materials, Biocompatible
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Coronary Restenosis
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prevention & control
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Drug-Eluting Stents
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Female
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Humans
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Male
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Materials Testing
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Methacrylates
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chemistry
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Phosphorylcholine
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analogs & derivatives
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chemistry
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Pilot Projects
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Polymers
;
chemistry
;
Prosthesis Design
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Random Allocation
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Sirolimus
;
chemistry
;
Swine
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Swine, Miniature
8.Miltefosine-Induced Apoptotic Cell Death on Leishmania major and L. tropica Strains.
Shahram KHADEMVATAN ; Mohammad Javad GHARAVI ; Fakher RAHIM ; Jasem SAKI
The Korean Journal of Parasitology 2011;49(1):17-23
The aim of this study was to assess the cytotoxic effects of various concentrations of miltefosine on Leishmania major (MRHO/IR/75/ER) and L. tropica (MHOM/IR/02/Mash10) promastigotes and to observe the programmed cell death features. The colorimetric MTT assay was used to find L. major and L. tropica viability and the obtained results were expressed as 50% inhibitory concentration (IC50). Also, 50% effective doses (ED50) for L. major and L. tropica amastigotes were also determined. Annexin-V FLUOS staining was performed to study the cell death properties of miltefosine using FACS analysis. Qualitative analysis of the total genomic DNA fragmentation was performed by agarose gel electrophoresis. Furthermore, to observe changes in cell morphology, promastigotes were examined using light microscopy. In both strains of L. major and L. tropica, miltefosine induced dose-dependent death with features of apoptosis, including cell shrinkage, DNA laddering, and externalization of phosphatidylserine. The IC50 was achieved at 22 microM and 11 microM for L. major and L. tropica after 48 hr of incubation, respectively. ED50 of L. major and L. tropica amastigotes were 5.7 microM and 4.2 microM, respectively. Our results indicate that miltefosine induces apoptosis of the causative agent of cutaneous leishmaniasis in a dose-dependent manner. Interestingly, L. major did not display any apoptotic changes when it was exposed to miltefosine in concentrations sufficient to kill L. tropica.
Animals
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Apoptosis/*drug effects
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Cell Cycle/drug effects
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Cell Line
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DNA Fragmentation/drug effects
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Humans
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Leishmania major/cytology/*drug effects
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Leishmania tropica/cytology/*drug effects
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Leishmaniasis, Cutaneous/parasitology
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Mice
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Phosphorylcholine/*analogs & derivatives/pharmacology
9.Effects of water-aging for 6 months on the durability of a novel antimicrobial and protein-repellent dental bonding agent.
Ning ZHANG ; Ke ZHANG ; Michael D WEIR ; David J XU ; Mark A REYNOLDS ; Yuxing BAI ; Hockin H K XU
International Journal of Oral Science 2018;10(2):18-18
Biofilms at the tooth-restoration bonded interface can produce acids and cause recurrent caries. Recurrent caries is a primary reason for restoration failures. The objectives of this study were to synthesize a novel bioactive dental bonding agent containing dimethylaminohexadecyl methacrylate (DMAHDM) and 2-methacryloyloxyethyl phosphorylcholine (MPC) to inhibit biofilm formation at the tooth-restoration margin and to investigate the effects of water-aging for 6 months on the dentin bond strength and protein-repellent and antibacterial durability. A protein-repellent agent (MPC) and antibacterial agent (DMAHDM) were added to a Scotchbond multi-purpose (SBMP) primer and adhesive. Specimens were stored in water at 37 °C for 1, 30, 90, or 180 days (d). At the end of each time period, the dentin bond strength and protein-repellent and antibacterial properties were evaluated. Protein attachment onto resin specimens was measured by the micro-bicinchoninic acid approach. A dental plaque microcosm biofilm model was used to test the biofilm response. The SBMP + MPC + DMAHDM group showed no decline in dentin bond strength after water-aging for 6 months, which was significantly higher than that of the control (P < 0.05). The SBMP + MPC + DMAHDM group had protein adhesion that was only 1/20 of that of the SBMP control (P < 0.05). Incorporation of MPC and DMAHDM into SBMP provided a synergistic effect on biofilm reduction. The antibacterial effect and resistance to protein adsorption exhibited no decrease from 1 to 180 d (P > 0.1). In conclusion, a bonding agent with MPC and DMAHDM achieved a durable dentin bond strength and long-term resistance to proteins and oral bacteria. The novel dental bonding agent is promising for applications in preventive and restorative dentistry to reduce biofilm formation at the tooth-restoration margin.
Anti-Infective Agents
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chemistry
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pharmacology
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Biofilms
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drug effects
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Dental Bonding
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Dentin-Bonding Agents
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chemistry
;
pharmacology
;
Materials Testing
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Methacrylates
;
chemistry
;
pharmacology
;
Phosphorylcholine
;
analogs & derivatives
;
chemistry
;
pharmacology
;
Resin Cements
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Shear Strength
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Surface Properties
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Water
10.Simvastatin inhibits sphingosylphosphorylcholine-induced differentiation of human mesenchymal stem cells into smooth muscle cells.
Kyung Hye KIM ; Young Mi KIM ; Mi Jeong LEE ; Hyun Chang KO ; Moon Bum KIM ; Jae Ho KIM
Experimental & Molecular Medicine 2012;44(2):159-166
Sphingosylphosphorylcholine (SPC) induces differentiation of human adipose tissue-derived mesenchymal stem cells (hASCs) into smooth muscle-like cells expressing alpha-smooth muscle actin (alpha-SMA) via transforming growth factor-beta1/Smad2- and RhoA/Rho kinase-dependent mechanisms. 3-Hydroxy-3-methylglutaryl-coenzyme A reductase inhibitors (statins) have been known to have beneficial effects in the treatment of cardiovascular diseases. In the present study, we examined the effects of simvastatin on the SPC-induced alpha-SMA expression and Smad2 phosphorylation in hASCs. Simvastatin inhibited the SPC-induced alpha-SMA expression and sustained phosphorylation of Smad2 in hASCs. SPC treatment caused RhoA activation via a simvastatin-sensitive mechanism. The SPC-induced alpha-SMA expression and Smad2 phosphorylation were abrogated by pretreatment of the cells with the Rho kinase inhibitor Y27632 or overexpression of a dominant negative RhoA mutant. Furthermore, SPC induced secretion of TGF-beta1 and pretreatment with either Y27632 or simvastatin inhibited the SPC-induced TGF-beta1 secretion. These results suggest that simvastatin inhibits SPC-induced differentiation of hASCs into smooth muscle cells by attenuating the RhoA/Rho kinase-dependent activation of autocrine TGF-beta1/Smad2 signaling pathway.
Amides/pharmacology
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Blotting, Western
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Cell Differentiation/*drug effects
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Cells, Cultured
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Enzyme-Linked Immunosorbent Assay
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Humans
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Immunohistochemistry
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Mesenchymal Stem Cells/*cytology/*drug effects
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Myocytes, Smooth Muscle/*cytology/*drug effects
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Phosphorylcholine/*analogs & derivatives/pharmacology
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Pyridines/pharmacology
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Simvastatin/*pharmacology
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Sphingosine/*analogs & derivatives/pharmacology
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rhoA GTP-Binding Protein/antagonists & inhibitors/metabolism