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PubMedDate not supplied

[Light induced polymerization of resin composite restorative materials].

INTRODUCTION: Dimensional stability of polymer-based dental materials is compromised by polymerization reaction of the monomer. The conversion into a polymer is accompanied by a closer packing of molecules, which leads to volume reduction called curing contraction or polymerization shrinkage. Curing contraction may break the adhesion between the adhesive system and hard tooth tissues forming microgaps which may result in marginal deterioration, recurrent caries and pulp injury. POLYMERIZATION SHRINKAGE OF RESIN-BASED RESTORATIVE DENTAL MATERIALS: Polymerization of the organic phase (nonomer molecules) of resin-based dental materials causes shrinkage. The space occupied by filler particles is not associated with polymerization shrinkage. However, high filler loading within certain limits, can contribute to a lesser curing contraction. POLYMERIZATION SHRINKAGE STRESS AND STRESS REDUCTION POSSIBILITIES: Polymerization shrinkage stress of polymer-based dental resins can be controlled in various ways. The adhesive bond in tooth-restoration interface guides the contraction forces to cavity walls. If leakage occurs, complications like secondary caries and pulpal irritation may jeopardize the longevity of a restoration. Stress relieve can be obtained by modifications of the monomer and photoinitiator, or by specially designed tooth preparation and application of bases and liners of low modulus of elasticity. The polymerization contraction can be compensated by water absorption due to oral cavity surrounding. The newest approach to stress relief is based on modulation of polymerization initiation. CONCLUSION: This work deals with polymerization contraction and how to achieve leak-proof restoration. Restorative techniques that may reduce the negative effect of polymerization shrinkage stress need further research in order to confirm up-to-date findings.

Composite Resins↗
PubMed2004

FI catalysts: new olefin polymerization catalysts for the creation of value-added polymers.

This contribution reports the discovery and application of phenoxy-imine-based catalysts for olefin polymerization. Ligand-oriented catalyst design research has led to the discovery of remarkably active ethylene polymerization catalysts (FI Catalysts), which are based on electronically flexible phenoxy-imine chelate ligands combined with early transition metals. Upon activation with appropriate cocatalysts, FI Catalysts can exhibit unique polymerization catalysis (e.g., precise control of product molecular weights, highly isospecific and syndiospecific propylene polymerization, regio-irregular polymerization of higher alpha-olefins, highly controlled living polymerization of both ethylene and propylene at elevated temperatures, and precise control over polymer morphology) and thus provide extraordinary opportunities for the syntheses of value-added polymers with distinctive architectural characteristics. Many of the polymers that are available via the use of FI Catalysts were previously inaccessible through other means of polymerization. For example, FI Catalysts can form vinyl-terminated low molecular weight polyethylenes, ultra-high molecular weight amorphous ethylene-propylene copolymers and atactic polypropylenes, highly isotactic and syndiotactic polypropylenes with exceptionally high peak melting temperatures, well-defined and controlled multimodal polyethylenes, and high molecular weight regio-irregular poly(higher alpha-olefin)s. In addition, FI Catalysts combined with MgCl(2)-based compounds can produce polymers that exhibit desirable morphological features (e.g., very high bulk density polyethylenes and highly controlled particle-size polyethylenes) that are difficult to obtain with conventionally supported catalysts. In addition, FI Catalysts are capable of creating a large variety of living-polymerization-based polymers, including terminally functionalized polymers and block copolymers from ethylene, propylene, and higher alpha-olefins. Furthermore, some of the FI Catalysts can furnish living-polymerization-based polymers catalytically by combination with appropriate chain transfer agents. Therefore, the development of FI Catalysts has enabled some crucial advances in the fields of polymerization catalysis and polymer syntheses.

Journal Article↗
PubMed2000

Controlled polymerization system for fabricating precise dentures.

STATEMENT OF PROBLEM: Most processed resin denture bases do not fit the cast accurately because of polymerization changes in the resin. The fit is more noticeable in the palate between the denture base and the cast. Therefore, development of a polymerization system that will improve the fit of a denture base to the cast is lack of worth considering to improve the fit and retention of the denture. PURPOSE: A newly developed polymerization system for dentures is presented that results in excellent adaptability of the denture base to the cast when compared with 2 other polymerization systems. MATERIAL AND METHODS: Forty-five maxillary dentures were made with 3 resins and 3 polymerization systems (a new polymerization system, SR-Ivocap system, original microwave polymerization system). Each denture and cast was sectioned through the second molar area parallel to the posterior border. Discrepancies between denture base and stone cast were measured at several points immediately after polymerization and after 30 days of immersion in water. In addition, disks of 3 materials processed in each system were examined for absorption of water and hardness at 2 measurement stages. Data were analyzed with the split-plot or 2-way ANOVA test. RESULTS: Dentures made with the new polymerization system had significantly smaller discrepancies, compared with dentures processed with the SR-Ivocap system and the microwave method. The amount of water absorption of the resin disks processed by the new system was less than the disks made by the other 2 systems. Dentures made with the new system exhibited significantly better adaptation to the cast than those made with the other 2 systems. CONCLUSION: The new polymerization system produced a more accurate method of processing dentures when fit was compared with the fit of dentures made with the other 2 denture base resins.

Acrylic Resins↗
PubMed1999

Rho-family GTPases require the Arp2/3 complex to stimulate actin polymerization in Acanthamoeba extracts.

BACKGROUND: Actin filaments polymerize in vivo primarily from their fast-growing barbed ends. In cells and extracts, GTPgammaS and Rho-family GTPases, including Cdc42, stimulate barbed-end actin polymerization; however, the mechanism responsible for the initiation of polymerization is unknown. There are three formal possibilities for how free barbed ends may be generated in response to cellular signals: uncapping of existing filaments; severing of existing filaments; or de novo nucleation. The Arp2/3 complex localizes to regions of dynamic actin polymerization, including the leading edges of motile cells and motile actin patches in yeast, and in vitro it nucleates the formation of actin filaments with free barbed ends. Here, we investigated actin polymerization in soluble extracts of Acanthamoeba. RESULTS: Addition of actin filaments with free barbed ends to Acanthamoeba extracts is sufficient to induce polymerization of endogenous actin. Addition of activated Cdc42 or activation of Rho-family GTPases in these extracts by the non-hydrolyzable GTP analog GTPgammaS stimulated barbed-end polymerization, whereas immunodepletion of Arp2 or sequestration of Arp2 using solution-binding antibodies blocked Rho-family GTPase-induced actin polymerization. CONCLUSIONS: For this system, we conclude that the accessibility of free barbed ends regulates actin polymerization, that Rho-family GTPases stimulate polymerization catalytically by de novo nucleation of free barbed ends and that the primary nucleation factor in this pathway is the Arp2/3 complex.

Acanthamoeba↗
PubMed1990

Reexamination of the role of nonhydrolyzable guanosine 5'-triphosphate analogues in tubulin polymerization: reaction conditions are a critical factor for effective interactions at the exchangeable nucleotide site.

Recently it was proposed [O'Brien, E. T., & Erickson, H. P. (1989) Biochemistry 28, 1413-1422] that tubulin polymerization supported by guanosine 5'-(beta,gamma-imidotriphosphate) [p(NH)ppG], guanosine 5'-(beta,gamma-methylenetriphosphate) [p(CH2)ppG], and ATP might be due to residual GTP in reaction mixtures and that these nucleotides would probably support only one cycle of assembly. Since we had observed polymerization with these three compounds, we decided to study these reactions in greater detail in two systems. The first contained purified tubulin and a high concentration of glycerol, the second tubulin and microtubule-associated proteins (MAPs). In both systems, reactions supported by nucleotides other than GTP were most vigorous at lower pH values. In the glycerol system, repeated cycles of polymerization were observed with ATP and p(CH2)ppG, but not with p(NH)ppG. With p(NH)ppG, a single cycle of polymerization was observed, and this was caused by contaminating GTP. In the MAPs system, repeated cycles of polymerization were observed with both nonhydrolyzable GTP analogues, even without contaminating GTP, but ATP was not active at all in this system. Binding to tubulin of p(NH)ppG, p(CH2)ppG, and, to a lesser extent, ATP was demonstrated indirectly, since high concentrations of the three nucleotides displaced radiolabeled GDP originally bound in the exchangeable site, with p(NH)ppG the most active of the three compounds in this displacement assay. The failure of GTP-free p(NH)ppG to support tubulin polymerization in our glycerol system even though it displaced GDP from the exchangeable site was further investigated by examining the effects of p(NH)ppG on polymerization and polymer-bound nucleotide with low concentrations of GTP. The two nucleotides appeared to act synergistically in supporting polymerization, so that a reaction occurred with a subthreshold GTP concentration if p(NH)ppG was also in the reaction mixture. Analysis of radiolabeled exchangeable-site nucleotide in polymers formed in reaction mixtures containing both GTP and p(NH)ppG demonstrated that p(NH)ppG which entered polymer did so primarily at the expense of GDP originally bound in the exchangeable site rather than at the expense of GTP. It appears that in the glycerol reaction condition, tubulin-p(NH)ppG cannot initiate tubulin polymerization but that it can participate in polymer elongation. ATP and p(CH2)ppG also entered the exchangeable site during polymerization without GTP in glycerol, as demonstrated by displacement of radiolabeled GDP from polymer when these alternate nucleotides were used.(ABSTRACT TRUNCATED AT 400 WORDS)

Adenosine Triphosphate↗
PubMed2003

Titanium alkoxides as initiators for the controlled polymerization of lactide.

Fourteen titanium alkoxides were synthesized for comparison of their catalytic properties in the bulk and solution polymerization of lactide (LA). In bulk polymerizations, they are effective catalysts in terms of polymer yield and molecular weight. Titanatranes gave polylactides with significantly increased molecular weight over more extended polymerization times, and those with five-membered rings afforded polymers in higher yields and with larger molecular weights than their six-membered ring counterparts. Steric hindrance of the rings was found to significantly affect polymer yields. Increased heterotactic-biased poly(rac-LA) was formed as the number of chlorine atoms increased in TiCl(x)(O-i-Pr)(4)(-)(x). In solution polymerizations, titanium alkoxides catalyzed controlled polymerizations of LA, and end group analysis demonstrated that an alkoxide substituent on the titanium atom acted as the initiator. That polymerization is controlled under our conditions was shown by the linearity of molecular weight versus conversion. A tendency toward formation of heterotactic-biased poly(rac-LA) was observed in the solution polymerizations. The rate of ring-opening polymerization (ROP) and the molecular weight of the polymers are greatly influenced by the substituents on the catalyst, as well as by factors such as the polymerization temperature, polymerization time, and concentration of monomer and catalyst.

Journal Article↗
PubMed1994

Induction of the polymerization of actin from the actin:thymosin beta 4 complex by phalloidin, skeletal myosin subfragment 1, chicken intestinal myosin I and free ends of filamentous actin.

Thymosin beta 4 is able to form 1:1 complexes with monomeric (G) actin, thereby stabilizing the intracellular pool of unpolymerized actin. We have searched for factors that are able to induce the polymerization of actin from the actin:thymosin beta 4 complex. Phalloidin, subfragment 1 isolated from rabbit skeletal muscle myosin and chicken intestinal myosin I are demonstrated to be able to polymerize the actin from this complex in the presence of 1 mM MgCl2. Polymerization of actin was verified by the DNase I inhibition assay, by cosedimentation and from the fluorescence increase of pyrene-labelled actin. Actin filaments formed under the influence of subfragment 1 or phalloidin were visualized under the electron microscope after negative staining. Polymerization of skeletal muscle actin from the complex with thymosin beta 4 by phalloidin is accompanied by the hydrolysis of the actin-bound ATP to ADP. Polymerization was also induced by sonicated F-actin which possessed a high concentration of free filament ends. F-actin was severed by 0.01 M human cytoplasmic gelsolin, which is known to possess blocked+ends. Free, slowly growing-ends were unable to induce polymerization of actin from the thymosin beta 4 complex. However, when gelsolin on its own or in complex with two actin molecules was added to actin:thymosin beta 4 under nucleating conditions, it was found to be able to promote actin repolymerization provided that its concentration was close to the dissociation constant (Kd) of actin:thymosin beta 4. This Kd was found to be 0.4 microM in the presence of 1 mM MgCl2 and the absence of KCl and, thus, close to the critical concentration of actin polymerization under these conditions. The source of actin did not influence its polymerization from the thymosin beta 4 complex; rabbit skeletal muscle actin and porcine brain actin were polymerized with equal efficiency from their complexes with thymosin beta 4 by both phalloidin and myosin subfragment 1. Skeletal muscle, but not cytoplasmic actin, was found to be also polymerized in the presence of increased CaCl2 concentrations to values above 1 mM.

Actins↗
PubMed1985

Hepatic uptake and disposition of human polymeric IgA1 in perfused rat liver: evidence for incomplete biliary excretion and intrahepatic degradation.

The hepatic uptake of polymeric immunoglobulin A (IgA) is mediated by secretory component; the resulting secretory IgA is excreted intact into bile. To define the hepatic metabolism of polymeric IgA, we quantitated the uptake and transport of human polymeric IgA1 after a single pass through the perfused rat liver. Uptake of polymeric IgA1 was compared with that of asialoorosomucoid, a glycoprotein whose uptake is mediated by the asialoglycoprotein receptor. Single-pass hepatic uptake of 125I-polymeric IgA1 and of 125I-asialoorosomucoid averaged 18.0 +/- 3.1% (SE) and 71.8 +/- 2.8%, respectively. The uptake of 125I-polymeric IgA1 was inhibited by excess unlabeled polymeric IgA1 but not by asialoorosomucoid. Only 13.0 +/- 1.6% of the 125I-polymeric IgA1 extracted by the liver was excreted into bile, whereas three-fourths was released into the hepatic venous effluent in degraded form. Thus, both the uptake and biliary excretion of polymeric IgA1 by the rat liver are inefficient processes. Polymeric IgA1 follows two distinct pathways after uptake by the liver: a small proportion is excreted intact into bile, while the majority is degraded and released back into the circulation.

Animals↗
PubMed2002

PEO-like plasma polymerized tetraglyme surface interactions with leukocytes and proteins: in vitro and in vivo studies.

Polyethylene oxide (PEO) surfaces reduce non-specific protein and cell interactions with implanted biomaterials and may improve their biocompatibility. PEO-like polymerized tetraglyme surfaces were made by glow discharge plasma deposition onto fluorinated ethylene propylene copolymer (FEP) substrates and were shown to adsorb less than 10 ng/cm2 of fibrinogen in vitro. The ability of the polymerized tetraglyme surfaces to resist leukocyte adhesion was studied in vitro and in vivo. Polymerized tetraglyme and FEP were implanted subcutaneously in mice and removed after 1 day or 4 weeks. Histological analysis showed a similar degree of fibrous encapsulation around all of the 4-week implants. Darkly stained wells were present in the fibrous tissues at the tissue-material interface of both FEP and tetraglyme. Scanning electron micrographs showed that in vivo macrophage adhesion to polymerized tetraglyme was much higher than to FEP. After 2-hour contact with heparinized whole blood, polymorphonuclear leukocyte (PMN) adhesion to polymerized tetraglyme was much higher than to FEP, while platelet adhesion to polymerized tetraglyme was lower than to FEP. When PMNs isolated from blood were suspended in 10% autologous plasma, cell adhesion to polymerized tetraglyme was higher than to FEP; however when the cells were suspended in heat inactivated serum, cell adhesion to FEP was higher than to polymerized tetraglyme. The surface chemistry of polymerized tetraglyme did not change after 2-hour blood contact, but displayed nitrogen functional groups after 1-day implantation and became slightly degraded after 4-week implantation. The surface chemistry of FEP did not change significantly after blood contact or implantation. Loosely bound proteins such as fibrinogen on polymerized tetraglyme may contribute to the adhesion of PMNs and macrophages and ultimately to fibrous encapsulation (the foreign body response) around the implants.

Adsorption↗
PubMed1998

Chemical modification and photograft polymerization upon expanded poly(tetrafluoroethylene).

Poly(tetrafluoroethylene) (PTFE) films were surface-modified by employing a reaction solution of benzophenone and sodium hydride in anhydrous dimethylformamide at a temperature of 150 degrees C for 12 h. Electron spectroscopy for chemical analysis (ESCA) showed defluorination, oxygen incorporation, and extensive unsaturation within the treated PTFE surfaces. The suitably of these reduced PTFE films as substrates for graft polymerization was initially assessed via photograft polymerization of the sodium salt of styrenesulfonic acid (SS-Na), which permitted unequivocal surface analysis by the introduction of a new atom, as well as poly(ethylene glycol) monoacrylate (PEG-Ac). All photograpt polymerization was performed employing ultraviolet irradiation with 2,2-dimethoxy-2-phenylacetophenone as an initiator. Photograft polymerization of SS-Na was verified by further reduction of fluorine atomic content and the appearance of new sulfur and sodium atomic peaks on ESCA survey spectra, and that of PEG-Ac was verified by further reduction of fluorine atomic content and increase of atomic percent ratio of O/C from ESCA survey spectra as well as appearance of a new ester peak on high resolution ESCA C 1s spectra. Dynamic water contact angles on reduced and PEG-Ac photograft polymerized films were measured and showed that the PTFE film surface became more hydrophilic after reduction (from 120 to 89 deg) and the reduced film became more hydrophilic after photograft polymerization with PEG-Ac (from 89 to 36 deg). Modification of the complete surface of expanded PTFE (ePTFE), i.e. of the lumenal, outside and pore surfaces, was performed by employing the reaction described above, except at 105 degrees C for 1 day, followed by photograft polymerization of PEG-Ac. ESCA was performed on the superficial surfaces (i.e. the lumen and exterior) as well as on cross-sections of the ePTFE to permit analysis of the pore surfaces. This analysis showed that both the initial surface reduction and subsequent photograft polymerization were successful as indicated from F/C and O/C atomic percent ratios from ESCA survey spectra, from overall peaks shapes of high resolution ESCA C 1s spectra and from generation of new ester peaks on high resolution ESCA C 1s spectra of ePTFE graft polymerized with PEG-Ac, which demonstrated an O/C atomic percent ratio close to that of PEG-Ac homopolymer. Low voltage scanning electron microscopy confirmed minimal morphological damage to the ePTFE microstructure after reduction and graft polymerization. The approach explored thus provides a means for modulation of biological interactions at ePTFE surfaces with only minimal modification of material morphology, with some surface texture appearing on a length scale of 50-100 nm.

Benzophenones↗
PubMed1999

Alterations of the actin polymerization status as an apoptotic morphological effector in HL-60 cells.

The alterations of the cytoskeletal actin network have been implicated as a morphological effector in apoptosis. However, studies directly linking actin change to the morphological events in apoptosis are lacking. This study quantitatively examined the effect of actin alteration on the camptothecin (CPT)-induced apoptotic process in HL-60 cells. Actin alteration was induced by two distinctive types of agent: the polymerization-stimulating agent, Jasplakinolide (Jas), and the polymerization-blocking agent, cytochalasin B (CB). The actin polymerization status was measured by two complementary methods: the cell pellet-based DNase I inhibition method, and the individual cell-based quantitative fluorescence image analysis (QFIA) assay. Actin polymerization induced by Jas caused apoptosis directly. By contrast, CB, an actin polymerization-blocking agent, partially inhibited CPT-induced apoptosis. A similar inhibition of the CPT-induced apoptosis response was observed with a more specific actin depolymerization agent, cytochalasin E. The alterations of the actin polymerization status occurred in three sequential steps during the apoptotic process: first polymerization, followed by depolymerization, and finally degradation. However, compared with CPT-induced apoptosis, Jas-induced apoptosis was characterized by pronounced actin polymerization that corresponded morphologically with prominent membrane blebbing, but less apoptotic body formation. Furthermore, DNase I activity, which is normally inhibited by G-actin, was specifically detected in Jas-treated cells. These results show that the regulation of actin polymerization is an important apoptotic morphological effector, whereas the alterations of the actin polymerization status by chemicals have profound effects not only on altering the morphology of apoptotic cells, but on apoptosis induction in HL-60 cells as well.

Actins↗
PubMedDate not supplied

Comparison of linear polymerization shrinkage and microhardness between QTH-cured & LED-cured composites.

This study evaluated the effectiveness of second generation light emitting diode (2ndLED) units in composite curing. In order to compare their effectiveness with that of conventional quartz tungsten halogen light curing units (QTH) and first generation LEDs (1stLED), the amount of linear polymerization shrinkage, polymerization speed and microhardness were measured. Linear polymerization shrinkage was measured every 0.5-0.55 seconds for 60 seconds when composite specimens (Z250, 3M ESPE Dental Products, St Paul, MN, USA) were light cured with five different light sources: XL 3000 (QTH, 3M ESPE Dental Products), Elipar FreeLight 2 (2ndLED, 3M ESPE Dental Products), Ultra-Lume LED2 (2ndLED, Ultradent Products, South Jordan, UT, USA), Elipar FreeLight (1stLED, 3M ESPE Dental Products) and experimental product X (1stLED, Biomedisys, Seoul, Korea). The amount of linear polymerization shrinkage in 60 seconds and the speed of polymerization shrinkage in the first 15 seconds were measured for the different lighting units. The amount of polymerization was compared with one-way ANOVA using Tukey at the 95% confidence level. In order to compare the speed of polymerization, the peak time (PT) showing the highest speed of polymerization and maximum speed of polymerization (Smax) were determined from the data and compared using one-way ANOVA with Tukey at the 95% confidence level for each material. For microhardness measurements, the microhardness of 2-mm composites, Z250, which had been light cured by XL 3000 (G1), FreeLight 2 (G2), Ultra-Lume LED2 (G3), FreeLight (G4) or experimental product X (G5) were compared on the upper and lower surface. The microhardness of each surface was compared between groups using two-way ANOVA with Tukey test at 95% levels of confidence. The amount of polymerization shrinkage at 60 seconds was G1, G2, G3> G4, G5 (p<0.05). PT was G1, G3 G3 >G4, G5 (p<0.05). On the upper composite surface, there was no difference in microhardness between groups (p<0.05). On the lower surface, the microhardness was G1, G2> G3> G4, G5 (p<0.05). There was no difference in microhardness between the upper and lower surface in G1 and G2; whereas, microhardness of the lower surface was lower in G3, G4 and G5. It was concluded that 2ndLEDs and the conventional QTH unit cu red composites moreeffectively than 1stLEDs.

Composite Resins↗
PubMed1988

Lack of correlation between induction of chemotactic peptide receptors and stimulus-induced actin polymerization in HL-60 cells treated with dibutyryl cyclic adenosine monophosphate or retinoic acid.

We used the promyelocytic leukemic cell line HL-60 to explore the molecular mechanisms regulating stimulus-induced actin polymerization in myeloid cells. HL-60 cells express very few chemotactic peptide receptors in their undifferentiated state and fail to undergo actin polymerization when stimulated with the chemotactic peptide N-formyl-methionyl-leucyl-phenylalanine (FMLP). However, when the cells were induced to differentiate with dibutyryl cyclic AMP (dbcAMP) or retinoic acid, they acquired the ability to undergo actin polymerization on stimulation with FMLP or phorbol myristate acetate. Kinetic experiments revealed that in the first 48 h of retinoic acid treatment there was no increase in the chemotactic peptide receptors on HL-60 cells, but the cells were capable of undergoing actin polymerization on stimulation with FMLP. Similarly, treatment with dbcAMP showed no increase in chemotactic peptide receptors until 24 h but stimulus-induced actin polymerization was demonstrable as early as 4 h after the treatment. In addition, with dbcAMP-treated cells the magnitude of stimulus-induced actin polymerization showed large variation depending on the duration of exposure to the drug. Dual-label studies using propidium iodide to measure DNA content and NBD-phallacidin to measure the F-actin content revealed that these variations were not related to the stages of cell cycle. Cells in all stages of the cell cycle responded to stimulus-induced actin polymerization, but the magnitude of the response appeared to be more in cells in G2/M phase. The observations reported here indicate that the small number of chemotactic peptide receptors present on HL-60 cells are adequate to mount an actin polymerization response, provided the required intracellular mechanisms exist. Differentiation-inducing agents, therefore, must cause changes within the cell, such as induction of actin-binding proteins, to cause actin polymerization following FMLP stimulation. The HL-60 system serves as a useful model for studying the molecular mechanisms regulating stimulus-induced actin polymerization in human neutrophils.

Actins↗
PubMed2001

The relationship between leachability of polymerization initiator and degree of conversion of visible light-cured resin.

Recently, polymerization-initiator-induced radicals have been identified as a biohazard as well as residual monomers. The present investigation was conducted to clarify the leaching behavior of the polymerization initiator and to measure the relationship between the leached amount of polymerization initiator and the degree of conversion of visible light (VL)-cured resin. Moreover, determining a suitable ratio of polymerization initiator to the base monomer according to the above relationship was carried out. The base monomer (UDMA/TEGDMA) was activated with varying concentrations of polymerization initiator (CQ/DMPT, CQ/DMAEMA) from 0.3-0.9 wt%, respectively, which were exposed to light for 40 s. Gas chromatograph mass spectrometry (GCMS) was carried out to evaluate the leached amount of polymerization initiator. The degree of conversion (DC) of the cured sample was estimated using attenuated total reflectance-Fourier transform infrared (ATR-FTIR) spectroscopy. As the result, it was recognized that the leachability of the polymerization initiator (CQ, DMPT, and DMAEMA) depended on the degree of conversion of the VL-cured resin. Therefore, the optimal concentration of polymerization initiator can be determined from the relation between the degree of conversion and the leached amount of polymerization initiator, which is about 0.6 wt% for CQ/DMPT (1:1 in weight) and 0.5 wt% for CQ/DMAEMA (1:1 in weight) relative to the UDMA/TEGDMA (1:1 in weight) monomer.

Dental Cements↗
PubMed2007

Changes in color and color parameters of dental resin composites after polymerization.

OBJECTIVES: The objectives were to measure the color change of varied shades of dental resin composites after polymerization, and to determine the correlation among the polymerization color change and the changes in color parameters after polymerization. METHODS: Eight light-curing resin composites, a total of 41 shades, were studied. Color of specimens (1 mm in thickness) was measured on a reflection spectrophotometer before and after polymerization over a white background. Changes in color (Delta E*(ab)), and color parameters (Delta L*, Delta C*(ab), Delta a*, and Delta b*: value after polymerization - value before polymerization) were calculated. RESULTS: The range of changes in each shade of resin composites was 1.1-7.9 for color (Delta E*(ab)), -7.5 to 2.3 for Delta L*, -6.8 to 3.1 for Delta C*(ab), -0.9 to 1.2 for Delta a*, and -6.8 to 3.1 for Delta b*. Delta E*(ab), Delta L*, Delta C*(ab), Delta a*, and Delta b* were influenced by the brand and shade of resin composites, and there was a significant interaction between two independent variables (p < 0.05). On the basis of the multiple regression analysis, in which Delta E*(ab) after polymerization was set as a dependent variable and Delta L*, Delta C*(ab), Delta a* and Delta b* as independent variables, multiple correlation coefficient (r) was 0.842 and the included predictors were Delta L* [standardized partial correlation coefficient (beta) = -0.760] and Delta C*(ab) (beta = -0.715). This result indicated that the polymerization changes in color and color parameters were varied by the brand and shade of resin composites, and the polymerization color change was caused by the changes in lightness and chroma with the similar power of influence.

Color↗
PubMed1990

Lipopolysaccharide modulates chemotactic peptide-induced actin polymerization in neutrophils.

To study the effect of endotoxin (LPS) on the basal and chemotactic peptide, formyl-methionyl-leucyl-phenylalanine (fMLP)-induced alterations in neutrophil cytoskeleton, we purified (greater than 98%) LPS-free neutrophils (LPS- less than 10 pg/ml LPS), compared their cytoskeletal organization to that of circulating neutrophils, and examined the effect of LPS exposure on the basal and fMLP-induced change in the cytoskeleton as reflected by F-actin content and distribution. Shape, F-actin content and distribution were monitored by FACS analysis and fluorescence microscopy of NBDphallicidin-stained cells. The F-actin content of basal and fMLP-activated, purified LPS- cells is similar to that of circulating neutrophils (defined as cells drawn in LPS- buffers at 37 degrees C and analyzed after less than 10 seconds of ex vivo manipulation). LPS- cells are round with a diffuse F-actin distribution. Exposure of LPS- cells to LPS causes cell polarization and F-actin redistribution without net gain in F-actin content. Peptide activation of the LPS- cell causes actin polymerization, which is preceded by a brief lag time. Exposure of LPS- cells to LPS (LPS+) enhances fMLP-induced actin polymerization by: 1) increasing the maximal extent of polymerization; 2) shortening the lag time preceding polymerization and increasing the rate of polymerization; and 3) lowering fMLP dose required for half maximal F-actin response. The enhancement depends on LPS dose, duration of exposure, and temperature. To examine the mechanism whereby LPS enhances fMLP-induced actin polymerization, we determined the predominant end for filament growth in LPS- and LPS+ cells, the number of actin nuclei generated in LPS- and LPS+ by fMLP activation, and the number and affinity of fMLP receptors on LPS- and LPS+ cells by 3[H]fMLP binding. Actin polymerization in both LPS- and LPS+ occurs predominantly by monomer addition to the barbed ends of nuclei, and the number of actin nuclei in basal and fMLP-activated LPS- and LPS+ cells is similar. LPS+ cells express three times more fMLP receptors than LPS- cells. The results show that LPS- cells are similar in cytoskeletal organization to circulating neutrophils, LPS causes shape change without change in F-actin content, and LPS enhances fMLP-induced actin polymerization response in neutrophils. The results suggest that LPS enhancement of actin polymerization response is associated with an increase in the number of fMLP receptors expressed on the cell surface.

Actins↗
PubMed1997

Importance of the release of strand 1C to the polymerization mechanism of inhibitory serpins.

Serpin polymerization is the underlying cause of several diseases, including thromboembolism, emphysema, liver cirrhosis, and angioedema. Understanding the structure of the polymers and the mechanism of polymerization is necessary to support rational design of therapeutic agents. Here we show that polymerization of antithrombin is sensitive to the addition of synthetic peptides that interact with the structure. A 12-m34 peptide (homologous to P14-P3 of antithrombin reactive loop), representing the entire length of s4A, prevented polymerization totally. A 6-mer peptide (homologous to P14-P9 of antithrombin) not only allowed polymerization to occur, but induced it. This effect could be blocked by the addition of a 5-mer peptide with s1C sequence of antithrombin or by an unrelated peptide representing residues 26-31 of cholecystokinin. The s1C or cholecystokinin peptide alone was unable to form a complex with native antithrombin. Moreover, an active antitrypsin double mutant, Pro 361-->Cys, Ser 283-->Cys, was engineered for the purpose of forming a disulfide bond between s1C and s2C to prevent movement of s1C. This mutant was resistant to polymerization if the disulfide bridge was intact, but, under reducing conditions, it regained the potential to polymerize. We have also modeled long-chain serpin polymers with acceptable stereochemistry using two previously proposed loop-A-sheet and loop-C-sheet polymerization mechanisms and have shown both to be sterically feasible, as are "mixed" linear polymers. We therefore conclude that the release of strand 1C must be an element of the mechanism of serpin polymerization.

Amino Acid Sequence↗
PubMed2001

Individual expression of recombinant alpha- and beta-tubulin from Haemonchus contortus: polymerization and drug effects.

Three tubulin isotypes from the parasitic nematode Haemonchus contortus were individually expressed in Escherichia coli, purified, and induced to polymerize into microtubules in the absence of microtubule-associated proteins. The effect of different conditions on the rate of polymerization of pure tubulin was assessed. This is the first time that recombinant alpha-tubulin has been shown to be capable of polymerization into microtubule-like structures when incubated with recombinant beta-tubulin. In addition, the present study has shown that: (1) microtubule-associated proteins are not required for tubulin polymerization; and (2) pure beta-tubulin isotype, beta12-16, alone was capable of forming microtubule-like structures in the absence of alpha-tubulin. Polymerization of the recombinant invertebrate tubulin, as measured by a spectrophotometric assay, was found to be enhanced by a concentration of tubulin >0.25 mg/mL; temperature > or =20 degrees C; 2 mM GTP; glycerol; EGTA; and Mg(2+). Polymerization was inhibited by GTP (>2 mM) and albendazole. Calcium ions and a pH range of 6 to 8.5 had no measurable effect on polymerization. Individual isotypes of tubulin polymerized to approximately the same extent as an alpha-/beta-tubulin mixture. Samples of tubulin assembled under the above conditions for 60 min were also examined under a transmission electron microscope. Although the spectrophotometric assay indicated polymerization, it did not predict the structure of the polymer. In many cases tubulin sheets, folded sheets, and rings were observed in addition to, or instead of, microtubule-like structures.

Animals↗