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PubMed1997

Linear polymerization caused by the defective folding of a non-inhibitory serpin ovalbumin.

Polymerization caused by defective folding of heat-denatured ovalbumin was examined. A compactly misfolded ovalbumin that was produced by cooling heat-denatured protein rapidly tended to aggregate in the presence of salt. Two different forms of aggregates were observed as the concentration of salt was varied: a linear polymer at a physiological concentration and a massive agglomerate at a higher concentration. Salt-induced polymerization depended on the species of anion and the order of effectiveness followed the lyotropic series of Hofmeister. Defective folding of heat-denatured ovalbumin induced the exposure of cysteine residues in sequences located in the interior of the native protein. The misfolded ovalbumin, but not the native protein, bound to bovine BiP and stimulated its ATPase activity with the K(m) of 64 microM and the V(max) of 0.5 nmol/min per milligram. Measurement of surface plasmon resonance revealed that only the misfolded ovalbumin was recognized with the K(d) of 4.12 X 10(-8) M by the Fab fragment of a monoclonal antibody raised against hen ovalbumin, and its epitope was determined to be a hydrophobic segment in the beta-strand of central sheet A. Transmission electron microscopy showed that the linear polymerization was inhibited by the addition of bovine BiP and the Fab fragment. These results demonstrated that the compactly misfolded ovalbumin polymerized through hydrophobic interaction occurring among the areas exposed as a result of defective folding of the heat-denatured protein. Exposure of the region of, or adjacent to, the central beta-sheet A was required for axial contact among the misfolded molecules, suggesting that this process may be explained by reference to the mechanism proposed for loop-sheet polymerization in the Z type variant of a serpin alpha1-antitrypsin.

Animals↗
PubMed1988

Deficient polymerization in vitro of a point-mutated beta-actin expressed in a transformed human fibroblast cell line.

HUT-14 cells, tumorigenic human fibroblasts, express a mutant beta-actin which has a single amino acid substitution at position 244 (glycine to aspartic acid), in addition to normal beta- and gamma-actin. In order to characterize the biochemical function of the mutant beta-actin, actins were extracted and purified from HUT-14 cells. The partially purified actin fraction contained beta-, gamma-, and mutant beta-actins in the ratio of 1:1:1, the same ratio as in the cells. When the actin of this fraction was purified through a polymerization step, mutant beta-actin was always less incorporated into actin filaments than beta- and gamma-actin. When the polymerization ability of purified HUT-14 actins was examined by sedimentation technique, it was lower than those of muscle and of cytoplasmic actins from another human cell line (HUT-11) which expresses only normal beta- and gamma-actin, in the ratio of 2:1. The deficient polymerization of mutant beta-actin was also observed by examining the ratio of beta-, gamma-, and mutant beta-actins incorporated into actin filaments. The ratio of mutant beta-actin in polymerized actins under all conditions examined was always less than that before polymerization. These results indicate that the single amino acid substitution at position 244 caused the reduction of incorporation of the mutant beta-actin into actin filaments in vitro.

Actins↗
PubMed1978

Characterization and in vitro polymerization of Tetrahymena tubulin.

Tetrahymena tubulin was purified from the cell extract using DEAE-Sephadex A-50 ion-exchanger and ammonium sulfate precipitation. About 2.2% of the total protein in the 20,000 X g supernatant was recovered as DEAE-Sephadex-purified tubulin fraction. Applying the temperature-dependent polymerization-depolymerization method to this fraction in the presence of Tetrahymena outer fibers as a seed, almost pure tubulin was obtained. Tetrahymena tubulin dimer showed different behavior on SDS-polyacrylamide gels from porcine brain tubulin, and showed very low affinity for colchicine, amounting to about one-twentieth of the binding to porcine brain tubulin. The tubulin fraction failed to polymerize into microtubules by itself. Addition of a small amount of the ciliary outer fiber fragment induced polymerization as demonstrated by viscometric measurements, but the reconstituted microtubules were very unstable in the absence of glycerol. Microtubule-depolymerizing agents such as Ca2+ ions, low temperature, or colchicine all inhibited in vitro polymerization. Although Tetrahymena tubulin purified by the polymerization-depolymerization method could copolymerize with porcine brain microtubules, the DEAE-Sephadex-purified tubulin fraction suppressed the initial rate of porcine brain microtubule assembly in vitro. There seemed to be no differences between cytoplasmic tubulin and outer fiber tubulin in colchicine binding activity or SDS-gel electrophoretic behavior, or between the fine structure of both reconstituted microtubules observed by electron microscopy.

Animals↗
PubMed1984

Characterization of the action of porcine brain profilin on actin polymerization.

When porcine brain actin is polymerized in either KCl/MgCl2 or KCl alone, porcine brain profilin prolongs the lag phase and inhibits the rate and extent of polymerization in a concentration-dependent manner. Profilin also decreases the elongation rate in a concentration-dependent manner. Moreover, addition of profilin to steady-state actin filaments causes slow depolymerization. All these actions of profilin are explainable by a monomer sequestering mechanism. The inhibition by profilin of both the extent of polymerization and the elongation rate is stronger in KCl alone than in KCl/MgCl2. Moreover, it was found that brain profilin inhibits the polymerization of brain actin more strongly than that of muscle actin. Brain 88K protein/actin complex (88K/A), which has been shown to cap the barbed end of actin filaments, potentiates the inhibitory action of profilin; i.e. the extent of polymerization is much more reduced by profilin in the presence of 88K/A than in its absence.

Actins↗
PubMed1984

Participation of 200K or 150K subunit of neurofilament in construction of the filament core with 70K subunit and promotion of tubulin polymerization by incorporated 200K subunit.

We have already reported that neurofilaments are capable of stimulating microtubule assembly and causing gelation. After separation of each of the triplet proteins of neurofilaments it was demonstrated that only the 200K subunit shows the activity to promote tubulin polymerization (Minami, Y. & Sakai, H. (1983) J. Biochem. 94, 2023-2033). The separation of each subunit protein led us to attempt the reconstitution of filaments from the 200K and 70K subunits or from the 150K and 70K subunits. It was found that both the 200K and 150K subunits independently contribute to the formation of intermediate-sized filaments, provided that each subunit was combined with the 70K subunit before removing urea by dialysis for reconstitution. On the other hand, the 200K subunit alone formed a very short thread-like structure after removal of urea, and the 150K subunit formed a filamentous structure, both incapable of being incorporated into filaments made of the 70K subunit alone. These observations suggest that the 200K and 150K subunits are not peripherally attached to a filament core made of 70K protein, but they take part in the formation of the core. Moreover, both proteins can co-polymerize with the 70K protein at a weight ratio of about 1 : 1 at least, which is in excess of that of the intact neurofilament. We investigated whether or not the 200K subunit incorporated with the 70K subunit into filaments could also stimulate tubulin polymerization. Low-shear viscometry measurements suggested that the 200K subunit retains the activity to initiate tubulin polymerization. This was confirmed by measuring viscosity changes with an Ostwald-type viscometer. In contrast, filaments reconstituted from the 70K and 150K proteins were incapable of increasing low-shear viscosity when mixed with tubulin. These observations suggest that the domain of the 200K protein embedded in the core of intermediate-sized filament is separate from the site responsible for promotion of tubulin polymerization.

Animals↗
PubMed1997

Polymeric immunoglobulin A receptor in the rodent female reproductive tract: influence of estradiol in the vagina and differential expression of messenger ribonucleic acid during estrous cycle.

Previously we have shown that estradiol and progesterone regulate the levels of secretory component, the external domain of polymeric immunoglobin A (IgA) receptor responsible for transporting IgA from tissues into secretions, at both the mRNA and protein levels in the rodent uterus. In the present study, experiments were designed to determine whether polymeric immunoglobulin receptor (pIgR) is synthesized locally in the vagina and whether it is under the control of estradiol and progesterone. Polymeric IgR message corresponding in size to that previously reported in the liver and uterus was detected by Northern blot analysis of total RNA from the vagina. Levels of pIgR mRNA and pIgR in the vagina were found to vary with the stage of the cycle. Polymeric IgR mRNA levels were elevated at diestrus, reduced at estrus, and undetectable at proestrus. Immunohistochemical analysis of pIgR in the vagina indicated that the expression of protein correlated with the mRNA levels. When ovariectomized rats were treated with estradiol, progesterone, or a combination of the two for 3 days, pIgR mRNA levels were significantly reduced in estradiol-treated animals relative to saline-treated controls. No significant changes were observed in the pIgR mRNA levels of animals treated with progesterone alone or with a combination of estradiol and progesterone. Polymeric IgR expression analyzed by immunohistochemical staining correlated well with variations in mRNA levels seen following hormone treatment. In situ hybridization localized pIgR in uterine and vaginal epithelial cells. In the uterus, pIgR message was abundant in luminal and glandular epithelial cells at estrus and low at diestrus. In contrast, expression of pIgR mRNA was pronounced in vaginal epithelial cells at diestrus, while very little message could be localized in the epithelium at estrus. These findings demonstrate that pIgR is synthesized locally in the uterus and vagina and is under tissue-specific hormone regulation.

Animals↗
PubMed2003

Endotoxin-induced endothelial cell proinflammatory phenotypic differentiation requires stress fiber polymerization.

Endotoxin-induced intercellular adhesion molecule-1 (ICAM-1) and interleukin 8 (IL-8) production in endothelial cells, which is mediated by Toll-receptor signaling, is essential for optimal neutrophil recruitment and migration during sepsis. Endotoxin also causes stress fiber polymerization that has recently been shown to affect intracellular signaling. However, the role of this polymerization process on endothelial-induced neutrophil adhesion and migration is unknown. Human umbilical vein endothelial cells (HUVEC) were stimulated with lipopolysaccharide (LPS). Selected cells were pretreated with cytochalasin D (CD) or lactrunculin A (LA), agents that disrupt actin polymerization. Cellular protein was extracted and analyzed by Westem blot for the phosphorylated form of IL-1-associated kinase (IRAK) and production of ICAM-1. Extracted nuclear protein was analyzed by Western blot and electrophoretic mobility shift assay (EMSA) for nuclear translocation and activity of NF-kappaB. IL-8 production was determined by enzyme-linked immunoabsorbant assay (ELISA). Neutrophil adhesion was assayed fluorometrically using calcein-AM-labeled neutrophils on treated endothelial cells. LPS treatment led to phosphorylation of IRAK, and subsequent NF-kappaB translocation and activation. This cellular signaling was followed by ICAM-1 expression and IL-8 production. Pretreatment of cells with CD or LA led to a significant inhibition of IRAK phosphorylation, and NF-kappaB nuclear translocation and activation. Actin depolymerization also significantly inhibited LPS-induced ICAM-1 and IL-8 production. HUVEC pretreated with CD or LA demonstrated significant inhibition of LPS-induced neutrophil adhesion. Endotoxin-induced actin polymerization is essential for optimal intracellular signaling through IRAK and NF-kappaB. Failure of these signaling events is associated with a marked reduction in adhesion molecule production, IL-8 production, and neutrophil adhesion. These findings support the necessity of stress fiber polymerization for optimal recruitment of neutrophils during sepsis.

Actins↗
PubMed2003

Dynamic FtsZ polymerization is sensitive to the GTP to GDP ratio and can be maintained at steady state using a GTP-regeneration system.

In vitro polymerization of the essential bacterial cell division protein FtsZ, in the presence of GTP, is rapid and transient due to its efficient binding and hydrolysis of GTP. In contrast, the in vivo polymeric FtsZ structure which drives cell division - the Z-ring - is present in cells for extended periods of time whilst undergoing constant turnover of FtsZ. It is demonstrated that dynamic polymerization of Escherichia coli FtsZ in vitro is sensitive to the ratio of GTP to GDP concentration. Increase of GDP concentration in the presence of a constant GTP concentration reduces both the duration of FtsZ polymerization and the initial light-scattering maximum which occurs upon addition of GTP. It is also demonstrated that by use of a GTP-regeneration system, polymers of FtsZ can be maintained in a steady state for up to 85 min, while preserving their dynamic properties. The authors therefore present the use of a GTP-regeneration system for FtsZ polymerization as an assay more representative of the in vivo situation, where FtsZ polymers are subject to a constant, relatively high GTP to GDP ratio.

Bacterial Proteins↗
PubMed1995

Polymerization of Actin from Maize Pollen.

Here we describe the in vitro polymerization of actin from maize (Zea mays) pollen. The purified actin from maize pollen reported in our previous paper (X. Liu, L.F. Yen [1992] Plant Physiol 99: 1151-1155) is biologically active. In the presence of ATP, KCl, and MgCl2 the purified pollen actin polymerized into filaments. During polymerization the spectra of absorbance at 232 nm increased gradually. Polymerization of pollen actin was evidently accompanied by an increase in viscosity of the pollen actin solution. Also, the specific viscosity of pollen F-actin increased in a concentration-dependent manner. The ultraviolet difference spectrum of pollen actin is very similar to that of rabbit muscle actin. The activity of myosin ATPase from rabbit muscle was activated 7-fold by the polymerized pollen actin (F-actin). The actin filaments were visualized under the electron microscope as doubly wound strands of 7 nm diameter. If cytochalasin B was added before staining, no actin filaments were observed. When actin filaments were treated with rabbit heavy meromyosin, the actin filaments were decorated with an arrowhead structure. These results imply that there is much similarity between pollen and muscle actin.

Journal Article↗
PubMed1997

Time-resolved X-ray powder diffraction using a large-area CCD-based detector and Rietveld refinement: solid-state polymerization of S2N2 to (SN)x.

A kinetic study of the solid-state polymerization of disulfur dinitride (S2N2) to polysulfur nitride [(SN)x] has been performed, combining monochromatic high-energy (lambda = 0.3263 A) synchrotron radiation X-ray powder diffraction, a large-area (ø = 220 mm) CCD-based X-ray image-intensifier detector and Rietveld refinement. Recently developed techniques for detector calibration and reduction of two-dimensional images to one-dimensional diffraction patterns have been employed for data processing/analysis. Good fits were obtained after Rietveld refinement [Rp = 8.4%, wRp = 9.4%, sin(theta(max))/lambda = 0.585 A(-1)] of diffraction patterns of S2N2 from images with 2 s exposure time. The solid-state polymerization of S2N2 to (SN)x, was followed at a maximum rate of two diffraction images per minute. Scale factors and cell parameters for S2N2 and beta-(SN), as functions of time were readily obtained after Rietveld refinement of the diffraction patterns obtained from each individual image throughout the polymerization. The polymerization was preceded by a lattice distortion of S2N2, and at 50% conversion the a axis had decreased by about 1% and the c axis had increased about 1%. The polymerization yielded not only the expected polymer beta-(SN)x, but also a small amount of a compound that could be another phase of (SN)x.

Journal Article↗
PubMed1993

In vitro posterior composite polymerization recovery following hygroscopic expansion.

Post-operative pain has been associated with composite polymerization shrinkage. This study aimed to quantify the cuspal deflection resulting from the initial shrinkage and the subsequent hygroscopic expansion of a standard posterior composite resin. Thirty hydrated permanent molars were marked on the buccal and lingual cusp tips. Standardized conventional Class II preparations were made and restorations with composite resin were placed and: (A) polymerized as one complete unit; (B) polymerized in gingivo-occlusal increments; (C) polymerized in buccolingual increments. Ten untreated teeth were marked and acted as controls. All specimens were placed in water. Pre-operative, post-operative and 6-month photographs were projected on a digitizer pad and measured by two independent investigators. The mean cuspal deflection (micron) immediately post-operatively and 6 months respectively, was: (A) 22.4, 8.7; (B) 12.4, 5.3; (C) 9.8, 3.0. The percentage of natural tooth dimensional recovery, following hygroscopic expansion was: (A) 97.5%; (B) 98.6%; (C) 99.4%. Buccolingual incremental polymerization led to significantly less initial cuspal deflection and the most cuspal recovery after hygroscopic expansion. The technique of resin placement therefore may provide a decrease in post-operative sensitivity.

Composite Resins↗
PubMed2006

Polymerization of SopA partition ATPase: regulation by DNA binding and SopB.

In bacteria, mitotic stability of plasmids and many chromosomes depends on replicon-specific systems which comprise a centromere, a centromere-binding protein and an ATPase. Dynamic self-assembly of the ATPase appears to enable active partition of replicon copies into cell-halves, but for most ATPases (the Walker-box type) the mechanism is unknown. Also unknown is how the host cell contributes to partition. We have examined the effects of non-sequence-specific DNA on in vitro self-assembly of the SopA partition ATPase of plasmid F. SopA underwent polymerization provided ATP was present. DNA inhibited this polymerization and caused breakdown of pre-formed polymers. Centromere-binding protein SopB counteracted DNA-mediated inhibition by itself binding to and masking the DNA, as well as by stimulating polymerization directly. The results suggest that in vivo, SopB smothers DNA by spreading from sopC, allowing SopA-ATP polymerization which initiates plasmid displacement. We propose that SopB and nucleoid DNA regulate SopA polymerization and hence partition.

Adenosine Triphosphate↗
PubMed1988

Polymerization of actin modified with fluorescein isothiocyanate.

Solution properties of skeletal muscle actin, modified at lysine-61 with fluorescein isothiocyanate (FITC) [Burtnick, L.D. (1984) Biochim. Biophys. Acta 791, 57-62], were re-examined in this work by light scattering, analytical ultracentrifugation, fluorescence, electron microscopy and myosin ATPase activity measurements. Fluorescence measurements using trace amounts of actin labeled with N-(1-pyrenyl)iodoacetamide showed that the FITC modification inhibited but did not block completely the polymerization of actin by KCl and MgCl2. Sedimentation velocity runs of FITC-actin, incubated with 100 mM KCl and 2 mM MgCl2, revealed the presence in these solutions of polymeric, oligomeric and monomeric species. The critical concentration for FITC-actin polymerization under these conditions was 12 microM. As judged by electron microscopy, FITC-actin polymers were similar to but generally shorter than standard F-actin filaments. Light scattering measurements indicated that FITC modification inhibited also the polymerization of actin by myosin subfragment 1 (S1) but the resulting complexes were indistinguishable from standard, decorated actin filaments. MgATPase measurements showed that FITC-actin, polymerized by preincubation with S1, activated the MgATPase activity of S1 while the monomeric labeled protein did not. Thus, in analogy to native actin, the activating function of FITC-actin depended on the formation of actin filaments. Results presented in this study suggest that the region around lysine-61 of actin plays an important role in actin-actin contact and is less crucial to actomyosin interaction.

Actins↗
PubMed1992

Reversed micelles of polymeric surfactants in nonpolar organic solvents. A new microheterogeneous medium for enzymatic reactions.

A new microheterogeneous non-aqueous medium for enzymatic reactions, based on reversed micelles of a polymeric surfactant, was suggested. The surfactant termed CEPEI, was synthesized by successive alkylation of poly(ethyleneimine) with cetyl bromide and ethyl bromide and was found to be able to solubilize considerable amounts of water in benzene/n-butanol mixtures. The hydrodynamic radius of polymeric-reversed micelles was estimated to be in the range 22-51 nm, depending on the water content of the system, as determined by means of the quasi-elastic laser-light scattering. Polymeric reversed micelles were capable of solubilizing enzymes (alpha-chymotrypsin and laccase) in nonpolar solvents with retention of catalytic activity. Due to the strong buffering properties of CEPEI over a wide pH range, it could maintain any adjusted pH inside hydrated reversed micelles. It was found that catalytic behavior of enzymes entrapped in polymeric reversed micelles was rather insensitive to the pH of the buffer solution introduced into the system as an aqueous component, but determined mostly by acid-base properties of the polymeric surfactant itself. Both catalytic activity and stability of entrapped alpha-chymotrypsin and laccase were found to increase with increasing water content of the system. Under certain conditions, the entrapment of alpha-chymotrypsin into CEPEI reversed micelles resulted in a considerable increase in catalytic activity and stability as compared to aqueous solution. CEPEI reversed micelles were demonstrated to be promising enzyme carriers for use in membrane reactors. Owing to the large dimensions of CEPEI reversed micelles, they are effectively kept back by a semipermeable membrane, thus allowing an easy separation of the reaction product and convenient recovery of the enzyme.

Buffers↗
PubMed1993

Effects of adenosine and its analogues on actin polymerization in human polymorphonuclear leucocytes.

1. The effects of adenosine and its analogues on actin polymerization in human polymorphonuclear leucocytes (PMN) induced by three different chemotactic stimulants, platelet-activating factor (PAF), N-formyl-methionyl-leucyl-phenylalanine (FMLP) and an activated fragment of C5 (C5a) were investigated. 2. Adenosine and its analogues inhibited the actin polymerization induced by these three agents in a concentration-dependent manner and theophylline, a competitive antagonist at adenosine receptors, abolished these inhibitory effects. 3. The adenosine analogue 5'-N-ethylcarboxamideadenosine (NECA) was a more potent inhibitor of actin polymerization than either L-N6-phenylisopropyladenosine (PIA) or adenosine itself; the rank order of potency of these agonists was characteristic of adenosine A2 receptors. 4. Adenosine deaminase (ADA) abolished the inhibitory effect of adenosine and augmented PAF-induced actin polymerization. 5. It was concluded that, at physiological concentrations, adenosine inhibits actin polymerization in PMN via activation of PMN surface membrane adenosine A2 receptors and thus modulates chemotactic stimulus-induced PMN motility.

Actins↗
PubMed1999

Actin polymerization stimulated by contractile activation regulates force development in canine tracheal smooth muscle.

1. The role of actin polymerization in the regulation of smooth muscle contractility was investigated in canine trachealis muscle strips. The effect of contractile activation on the content of monomeric globular (G)-actin was estimated by the method of DNase I inhibition. The G-actin content was 30 % lower in extracts of muscle strips activated with 10-4 M acetylcholine (ACh) than in extracts from unstimulated muscle strips. The decrease in G-actin in response to contractile stimulation was prevented by latrunculin-A, an agent that prevents actin polymerization by binding to G-actin monomers. 2. The inhibition of actin polymerization by latrunculin-A markedly depressed force development in response to ACh but had no effect on ACh-induced myosin light chain (MLC) phosphorylation. Latrunculin also suppressed the length sensitivity of force during ACh-induced isometric contractions. The actin-capping agent cytochalasin-D also markedly inhibited force and caused only a slight decrease in MLC phosphorylation. Cytochalasin-D also inhibited force in alpha-toxin-permeabilized muscle strips that were activated either by Ca2+ or by ACh at constant pCa. No disorganization of smooth muscle cell ultrastructure was detected by electron microscopy or by immunofluorescence microscopy of muscles treated with either agent. 3. The results suggest that the polymerization of actin is stimulated by the contractile activation of tracheal smooth muscle and that this actin polymerization contributes directly to force development. In addition, actin filament remodelling contributes to the length sensitivity of tracheal smooth muscle contractility.

Acetylcholine↗
PubMed1991

Evidence against impaired brain microtubule protein polymerization at high glucose concentrations or during diabetes mellitus.

Previous studies suggest that brain microtubule protein exposed to high glucose levels or isolated from diabetic rats can become glucosylated and that this impairs GTP-induced microtubule polymerization. We set out to extend that investigation to define the mechanistic basis for inhibition of microtubule assembly during diabetes or on incubation at high glucose levels. Rat and bovine brain microtubule protein was purified by cycles of polymerization/depolymerization. When microtubules were incubated for 1 h in either buffer or buffer containing glucose (up to 165 mM), there was no difference in polymerization, a finding contrary to the earlier study. Other rats were injected with vehicle or streptozotocin (90 mg/kg) to induce diabetes as evidenced by serum glucose in excess of 300 mg%, and at 4 weeks, brain microtubule protein was isolated by the polymerization cycling method. Again, there was no difference in the amount or purity of isolated microtubule protein between control or diabetic rats. We also observed no increase in microtubule glucosylation, and GTP-induced polymerization in vitro was indistinguishable for protein derived from brains of normal rats and rats with diabetes as measured by turbidity or electron microscopy. Our results suggest that in vitro incubation with glucose or in vivo elevation of glucose during diabetes fails to impair microtubule polymerization, pointing to other mechanisms for the neuropathy associated with diabetes.

Animals↗
PubMed1996

Accuracy of wax, autopolymerized, and light-polymerized resin pattern materials.

PURPOSE: The marginal fit of MOD inlay and full-crown patterns fabricated from wax, autopolymerized acrylic resin, and two light-polymerized, diacrylate resin pattern materials was compared on standardized dies. MATERIALS AND METHODS: Four pattern materials were studied-two light-polymerized, diacrylate resin materials (Palavit G LC and Triad VLC Burnout Paste), an inlay wax, and an autopolymerized resin (Duralay). Patterns were fabricated using incremental and bulk techniques on stone dies made from addition silicone impressions of American Dental Association MOD and full-crown master dies. Gaps were measured with a measuring microscope in four marginal areas on the master dies at 1 and 24 hours after fabrication. RESULTS: For the MOD inlay patterns, marginal gaps ranged from 7 to 23 microns, and the light-polymerized, diacrylate resins and autopolymerized acrylic resin material had statistically smaller gaps than the inlay wax. For the full-crown patterns, marginal gaps ranged from 10 to 23 microns, with the exception of the autopolymerized acrylic resin prepared by the bulk technique (40 to 46 microns). With the incremental technique, the light-polymerized, diacrylate resins and inlay wax had statistically smaller gaps than the autopolymerized acrylic resin material. Overall, the incremental technique produced equal or smaller marginal gaps than the bulk technique for full-crown patterns. Generally, the patterns measured at 1 hour had smaller marginal gaps than at 24 hours. CONCLUSIONS: When measured on intra- and extracoronal master dies, the light-polymerized, diacrylate resins had equal or better marginal fit, compared with wax or autopolymerized acrylic resin, and were less affected by placement technique and storage. The marginal gaps of all four pattern materials ranged from 7 to 46 microns and are within the range of clinical acceptability.

Acrylic Resins↗