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PubMed2006

Polymerized rodlike nanoparticles with controlled surface charge density.

Stable rodlike nanoparticles with highly controlled surface charge density have been developed by the free radical polymerization of the mixture of polymerizable cationic surfactant, cetyltrimethylammonium 4-vinylbenzoate (CTVB), and hydrotropic salt sodium 4-styrenesulfonate (NaSS) in aqueous solution. The surface charge of the polymerized CTVB/NaSS rodlike nanoparticles was controlled by varying the NaSS concentration during the polymerization process, and the charge variation was interpreted in terms of the overcharging effect in colloidal systems. The SANS measurements show that the diameter of the polymerized CTVB/NaSS rodlike nanoparticles is constant at 4 nm and the particle length ranges from 24 to 85 nm, depending on the NaSS concentration. The polymerized particles are longest when the NaSS concentration is 5 mol % which corresponds to the charge inversion or neutral point. The SANS and zeta potential measurements show that the Coulomb interactions between the particles are strongly dependent on the NaSS concentration and the zeta potential of the polymerized CTVB/NaSS nanoparticles changes from positive to negative (+12.8 approximately -44.2 mV) as the concentration of NaSS increases from 0 to 40 mol %. As the NaSS concentration is further increased, the zeta potential is saturated at approximately -50 mV.

Journal Article↗
PubMed2001

Myorod, a thick filament protein in molluscan smooth muscles: isolation, polymerization and interaction with myosin.

Myorod, a new protein of molluscan smooth muscles, is localized on the surface of paramyosin core of thick filaments together with myosin [Shelud'ko et al. (1999) Comp Biochem Physiol, 122, 277]. This protein is an alternatively spliced product of the myosin heavy chain gene. It contains the C-terminal rod part of myosin and a unique N-terminal domain [Yamada et al. (2000) J Mol Biol, 295, 169]. In the present study, the methods of myorod and myorod-free myosin preparation are developed and some properties of myorod are compared with those of myosin and myosin rod. We found that, in spite of the identity of filament-forming domains, the properties of polymeric myorod are clearly distinct from those of myosin and myosin rod. Myorod is much more soluble at intermediate ionic strength. The critical monomer concentration for polymerization of myorod is many times higher. The size of polymer particles of myorod is considerably smaller than that of myosin and myosin rod. The pure polymeric myorod forms a low turbid and unexpectedly high viscous suspension. The low-shear intrinsic viscosity of myorod is an order of magnitude higher than that of myosin or myosin rod and is close to that of F-actin. A trace admixture of myosin in myorod preparations or a small addition of myosin (0.2-1.0%) to myorod drastically alters the myorod polymerization. The suspensions of polymeric myorod nucleated by myosin have a high turbidity and low viscosity and consist of large particles. As judged from the changes in particle size distribution during polymerization, these particles are formed by successive dimerization steps. Electron micrographs show that the particles are typically spindle-shaped filaments in contrast to polymers of pure myorod which forms a network-like structure consisting of small particles. Possible participation of myorod in the catch-contraction of molluscan smooth muscles is discussed.

Actin Cytoskeleton↗
PubMed2000

Melanosomal proteins promote melanin polymerization.

In melanocytes, enzymes involved in the generation of melanin monomers are present and active in coated vesicles which are known to be acidic. Melanin polymerization however, occurs only in melanosomes. In vitro, it is not possible to generate melanin at the acidic pH of melanosomes using 3,4-dihydroxyphenylalanine (DOPA) and tyrosinase alone whereas melanin readily forms at higher pH with these reagents. Dimerization and elongation of the melanin polymer is known to require deprotonation. We have hypothesized that the amino acid side chains of melanosomal proteins act as proton acceptors to initiate polymerization and that the protonated basic groups serve to attract the negatively charged oligomers thus aiding polymerization and binding to proteins. We show that basic model proteins and basic premelanosomal proteins promote polymerization at an acidic pH and that positively charged surfaces allow binding of the growing melanin polymer. With progressive polymerization and exhaustion of the proton abstracting ability of melanosomal proteins, melanosomal pH drops further, which, we argue, is an additional controlling step that limits tyrosinase activity and melanin polymerization.

Animals↗
PubMed1999

Spatial control of actin polymerization during neutrophil chemotaxis.

Neutrophils respond to chemotactic stimuli by increasing the nucleation and polymerization of actin filaments, but the location and regulation of these processes are not well understood. Here, using a permeabilized-cell assay, we show that chemotactic stimuli cause neutrophils to organize many discrete sites of actin polymerization, the distribution of which is biased by external chemotactic gradients. Furthermore, the Arp2/3 complex, which can nucleate actin polymerization, dynamically redistributes to the region of living neutrophils that receives maximal chemotactic stimulation, and the least-extractable pool of the Arp2/3 complex co-localizes with sites of actin polymerization. Our observations indicate that chemoattractant-stimulated neutrophils may establish discrete foci of actin polymerization that are similar to those generated at the posterior surface of the intracellular bacterium Listeria monocytogenes. We propose that asymmetrical establishment and/or maintenance of sites of actin polymerization produces directional migration of neutrophils in response to chemotactic gradients.

Actin-Related Protein 2↗
PubMed2001

Role of actin polymerization and actin cables in actin-patch movement in Schizosaccharomyces pombe.

Factors that are involved in actin polymerization, such as the Arp2/3 complex, have been found to be packaged into discrete, motile, actin-rich foci. Here we investigate the mechanism of actin-patch motility in S. pombe using a fusion of green fluorescent protein (GFP) to a coronin homologue, Crn1p. Actin patches are associated with cables and move with rates of 0.32 microm s(-1) primarily in an undirected manner at cell tips and also in a directed manner along actin cables, often away from cell tips. Patches move more slowly or stop when actin polymerization is attenuated by Latrunculin A or in arp3 and cdc3 (profilin) mutants. In a cdc8 (tropomyosin) mutant, actin cables are absent, and patches move with similar speed but in a non-directed manner. Patches are sites of Arp3-dependent F-actin polymerization in vitro. Rapid F-actin turnover rates in vivo indicate that patches and cables are maintained continuously by actin polymerization. Our studies give rise to a model in which actin patches are centres for actin polymerization that drive their own movement on actin cables using Arp2/3-based actin polymerization.

Actin-Related Protein 2↗
PubMed1997

Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes.

The pathogenic bacterium Listeria monocytogenes is capable of directed movement within the cytoplasm of infected host cells. Propulsion is thought to be driven by actin polymerization at the bacterial cell surface, and moving bacteria leave in their wake a tail of actin filaments. Determining the mechanism by which L. monocytogenes polymerizes actin may aid the understanding of how actin polymerization is controlled in the cell. Actin assembly by L. monocytogenes requires the bacterial surface protein ActA and protein components present in host cell cytoplasm. We have purified an eight-polypeptide complex that possesses the properties of the host-cell actin polymerization factor. The pure complex is sufficient to initiate ActA-dependent actin polymerization at the surface of L. monocytogenes, and is required to mediate actin tail formation and motility. Two subunits of this protein complex are actin-related proteins (ARPs) belonging to the Arp2 and Arp3 subfamilies. The Arp3 subunit localizes to the surface of stationary bacteria and the tails of motile bacteria in tissue culture cells infected with L. monocytogenes; this is consistent with a role for the complex in promoting actin assembly in vivo. The activity and subunit composition of the Arp2/3 complex suggests that it forms a template that nucleates actin polymerization.

Actin-Related Protein 2↗
PubMed1996

Increased binding of polymeric lambda-IgA to cultured human mesangial cells in IgA nephropathy.

IgA nephropathy (IgAN) is characterized by raised plasma lambda-IgA1 and mesangial polymeric lambda-IgA1 deposits. It remains uncertain whether the predominant glomerular lambda-IgA1 deposits represent a selective uptake of polymeric IgA or a non-specific uptake due to elevated circulating lambda-IgA1 levels in response to an unidentified antigen. In this study, we explored whether there is an increased binding of monomeric IgA1 (mIgA1) or polymeric IgA1 (pIgA1) from patients with IgAN to cultured human mesangial cells (HMC). Total IgA1 in plasma from patients or healthy controls was isolated by jacalin-agarose column as jacalin-bound proteins (JBP). Monomeric IgA1 and pIgA1 were distinctly separated by FPLC. HMC were incubated with IgA preparations and IgA bound to HMC was determined by flow cytometry analysis using standard curves constructed by known concentrations of kappa-IgA1 or lambda-IgA1. In order to avoid any increased binding of IgA to HMC due to elevated kappa- or lambda-IgA concentrations in JBP samples from patients, JBP samples from patients or controls were appropriately diluted to achieve comparable levels of total IgA1. No differences in the total mIgA1 or pIgA1 concentration, percentage of mIgA1 or pIgA1, or the kappa/lambda ratio of mIgA1 or pIgA1 were found between adjusted JBP samples from patients or healthy controls. We found a sharp rise in percentage of pIgA1 among IgA1 bound to HMC (70%), despite the fact that only 3% of the IgA1 in the adjusted JBP samples were polymeric, suggesting that pIgA1 had a higher affinity to HMC than mIgA1. Furthermore, the kappa/lambda ratios of pIgA1 bound to HMC were significantly lower than the kappa/lambda ratios of pIgA1 in adjusted JBP only with IgAN patients but not healthy controls (P = 0.0026). Our data suggest a preferential mesangial binding of polymeric lambda-IgA1 from patients with IgAN. These polymeric lambda-IgA immune complexes are likely to be "pathogenic" and are important in the pathogenesis of IgAN.

Adult↗
PubMed2006

Photocontrolled living polymerizations.

Living polymerizations involve the creation of polymer chains without significant irreversible chain transfer or chain termination. Such processes are widely used to access well-defined macromolecular materials with controlled architectures, such as block and star polymers. Although this concept was first realized for anionic polymerizations in the 1950s, many key recent advances have been made, most notably in the area of radical polymerization. Here, we report a living photopolymerization that involves photoexcited monomers. Exposure of metal-containing ferrocenophane monomers to Pyrex-filtered light from a mercury lamp (lambda>310 nm) or to bright sunlight in the presence of an anionic initiator leads to living polymerizations, in which the conversion and molecular weight of the resulting polymer can be controlled by the irradiation time. Photoirradiation selectively weakens the iron-cyclopentadienyl bond in the monomer, allowing the use of moderately basic and highly functional-group-tolerant initiators. The polymerization proceeds through attack of the initiator and propagating anion on the iron atom of the photoexcited monomer and, remarkably, the polymerization rate decreases with increasing temperature. Block copolymer formation is possible when the light source is alternately switched on and off in between sequential addition of different monomers, providing unprecedented, photocontrolled access to new types of functional polymers.

Journal Article↗
PubMed1976

Observations on the different substrate behavior of tropocollagen molecules in solution and intermolecularly cross-linked tropocollagen within insoluble polymeric collagen fibrils.

Bacterial collagenase was used to compare the extent of digestion of tropocollagen monomers in solution and in reconstituted fibrils with that of tropocollagen molecules intermolecularly cross-linked within insoluble polymeric collagen fibrils obtained from mature tendons at given time-intervals. The extent of digestion of tropocollagen monomers in solution was directly proportional to the enzyme concentration (a range of enzyme substrate molar ratios 1:200 to 1:10 was used). The extent of digestion of polymeric collagen was followed by measuring the solubilization of fluorescent peptides from fluorescent-labelled insoluble polymeric collagen fibrils. The extent of digestion of tropocollagen within polymeric collagen was linear over a very small range of enzyme concentrations, when the enzyme/substrate ratio in the reaction mixture was less than 1:400 on a molecular basis. The behavior of tropocollagen in the form of reconstituted collagen fibrils, which had been matured at 37 degrees C for 8 weeks, was intermediate between the behaviour of solutions of tropocollagen and insoluble polymeric collagen fibrils. The significance of the results is discussed in terms of the structure of polymeric collagen fibrils and the protection against enzymic attack provided by tropocollagen molecules on the circumference of the fibril. The results suggest that assays of collagenase activities based on tropocollagen as substrate cannot be directly related to the ability of these enzymes to degrade mature insoluble collagen fibrils.

Animals↗
PubMed2006

Polymerization of human angiotensinogen: insights into its structural mechanism and functional significance.

In the present study, we have investigated the in vitro polymerization of human plasma AGT (angiotensinogen), a non-inhibitory member of the serpin (SERine Protease INhibitor) family. Polymerization of AGT is thought to contribute to a high molecular mass form of the protein in plasma that is increased in pregnancy and pregnancy-associated hypertension. The results of the present study demonstrate that the polymerization of AGT occurs through a novel mechanism which is primarily dependent on non-covalent linkages, while additional disulfide linkages formed after prolonged incubation are not essential for either formation or stability of polymers. We present the first analyses of AGT polymers by electron microscopy, CD spectroscopy, stability assays and sensitivity to proteinases and we conclude that their structure differs from the 'loop-sheet' polymers typical of inhibitory serpins. Histidine residues within the unique N-terminal extension of AGT appear to influence polymer formation, although polymer formation can still take place after their removal by renin. At a functional level, we show that AGT polymers are not substrates for renin, so polymerization of AGT in plasma would predictably lead to decreased formation of AngI (angiotensin I) with blood pressure lowering. Polymerization may therefore be an appropriate response to hypertension. The ability of AGT to protect its renin cleavage site through polymerization may explain why the AngI decapeptide has remained linked to the large and apparently inactive serpin body throughout evolution.

Angiotensinogen↗
PubMed1987

Use of rapid gel-permeation chromatography to explore the inter-relationships between polymerization, phosphorylation and activity of acetyl-CoA carboxylase. Effects of insulin and phosphorylation by cyclic AMP-dependent protein kinase.

Superose 6 chromatography was used to separate rapidly the polymeric and dimeric forms of acetyl-CoA carboxylase. With preparations of acetyl-CoA carboxylase purified by Sepharose-avidin chromatography, it is shown that citrate promotes polymerization and that the extent of polymerization is diminished, but not eliminated, after phosphorylation by cyclic-AMP-dependent protein kinase. After exposure of rat epididymal adipose tissue to insulin, evidence was obtained for a marked increase in polymerization. The polymeric form, which was active in the absence of citrate, exhibited increased phosphorylation, particularly on a tryptic peptide designated the I-peptide in an earlier study [Brownsey & Denton (1982) Biochem. J. 202, 77-86]. In contrast, in tissue exposed to the beta-agonist isoprenaline, most of the phosphorylated acetyl-CoA carboxylase appeared to be in the dimeric form if chromatography was carried out in the absence of citrate, whereas in the presence of citrate the degree of polymerization was diminished.

Acetyl-CoA Carboxylase↗
PubMed1990

Actin polymerization in neutrophils is triggered without a requirement for a rise in cytoplasmic Ca2+.

Stimulation of rat neutrophils with the peptide fMetLeuPhe caused (i) the appearance of a 40 kDa protein in the Triton-X-100-insoluble cytoskeleton, (ii) the disappearance of DNAase inhibition from the cytosol and (iii) the appearance of N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)phallacidin (NBD-phallacidin) binding sites. All three observations were consistent with a rapid and transient assembly of polymerized actin, peaking at approximately 5 s and returning to near resting levels within 40 s. By experimentally depleting the cells of Ca2+ and increasing the cytoplasmic Ca2+ buffering capacity, the peptide-induced Ca2+ transient was reduced from a peak of 900 nM to 250 nM, without inhibiting actin polymerization, and this peak was sustained for at least 2 min. A further dissociation between the triggering of actin polymerization and peptide-induced Ca2+ elevation and oxidase activation was demonstrated at low concentrations of peptide (1-100 pM), actin polymerization being triggered without an elevation in Ca2+ or activation of the oxidase. Two other agents which induced actin polymerization, phorbol 12-myristate 13-acetate and latex beads, failed to elevate cytoplasmic Ca2+. It was therefore concluded that neither Ca2+ nor those intracellular messengers which act with Ca2+ to trigger the neutrophil oxidase are responsible for triggering actin polymerization in neutrophils.

Actins↗
PubMed2004

The efficiency of different light sources to polymerize resin cement beneath porcelain laminate veneers.

Plasma arc light units for curing resin composites have been introduced with the claim of relatively short curing times. The purpose of this study was to evaluate the efficiency of two different light sources to polymerize dual curing resin cement beneath porcelain laminate veneers. Twenty extracted healthy human maxillary centrals were used. Teeth were sectioned 2 mm below the cemento-enamel junction and crown parts were embedded into self-cure acrylic resin, labial surface facing up. Cavity preparation was carried out on labial surfaces. These teeth were divided into two groups of 10 each. The resin cement/veneer combination was exposed to two different photo polymerization units. A conventional halogen light (Hilux 350, Express Dental Products) and a plasma arc light (Power PAC, ADT) were used to polymerize resin cement. Ten specimens were polymerized conventionally (40 s) and the other specimens by plasma arc curing (PAC) (6 s). Two samples from each tooth measuring 1.2 x 1.2 x 5 mm were prepared. These sections were subjected to microshear testing and failure values were recorded. Statistically significant differences were found between the bond strength of veneers exposed to conventional light and PAC unit (P < 0.001). Samples polymerized with halogen light showed better bond strength. The results of this study suggest that the curing efficiency of PAC through ceramic was lower compared with conventional polymerization for the exposure durations tested in this study.

Adhesiveness↗
PubMed1976

Comparison of polymerized and unpolymerized antigen E for immunotherapy of ragweed allergy.

Polymerization of ragweed antigen into high-molecular-weight polymers could improve immunotherapy for ragweed pollinosis by reducing side effects while retaining immunogenicity. To study this thesis, 23 ragweed-sensitive patients were treated with either ordinary ragweed antigen E or ragweed antingen E polymerized by glutaraldehyde. Four patients received the polymerized antigen, and six controls ordinary antigen according to the standard immunotherapy schedule; two groups of three patients received either form by a "doubling-dose" schedule. Seven subjects received the polymerized antigen by a schedule in which each successive dose was tripled. Serum antigen E binding capacity (blocking antibody) increased significantly in all subjects (P less than 0.001 by Student-test). Patients treated with polymerized antigen had fewer local and generalized reactions than those receiving the monomeric preparation. Polymerized ragweed antigen permits more rapid immunization of atopic persons, with fewer side effects than standard monomeric preparations.

Adult↗
PubMed2005

Compressible models of equilibrium polymerization.

Flory-Huggins-type models of equilibrium polymerization are extended to describe compressible systems and, hence, the pressure dependence of thermodynamic properties. The theory is developed for three different mechanisms of equilibrium polymerization (the free association, monomer-activated polymerization, and chemically initiated polymerization models). In contrast to previous approaches for describing the pressure dependence, the theory delineates the thermodynamic consequences of the size disparities between solvent molecules, unpolymerized monomers, and the monomers within polymers. Basic thermodynamic properties (the extent of polymerization, density, heat capacities C(P) and C(V), etc.) are calculated analytically as functions of pressure, temperature, and composition of the associating species. Illustrative calculations refer to systems that polymerize upon cooling and demonstrate general agreement with numerous experimental trends. Comparisons with results from other theories are also discussed.

Journal Article↗
PubMed2006

Does equilibrium polymerization describe the dynamic heterogeneity of glass-forming liquids?

A significant body of evidence indicates that particles with excessively high or low mobility relative to Brownian particles form in dynamic equilibrium in glass-forming liquids. We examine whether these "dynamic heterogeneities" can be identified with a kind of equilibrium polymerization. This correspondence is first checked by demonstrating the presence of a striking resemblance between the temperature dependences of the configurational entropy s(c) in both the theory of equilibrium polymerization and the generalized entropy theory of glass formation in polymer melts. Moreover, the multiple characteristic temperatures of glass formation are also shown to have analogs in the thermodynamics of equilibrium polymerization, supporting the contention that both processes are varieties of rounded thermodynamic transitions. We also find that the average cluster mass (or degree of polymerization) varies in nearly inverse proportionality to s(c). This inverse relation accords with the basic hypothesis of Adam-Gibbs that the number of particles in the cooperatively rearranging regions (CRR) of glass-forming liquids scales inversely to s(c) of the fluid. Our identification of the CRR with equilibrium polymers is further supported by simulations for a variety of glass-forming liquids that verify the existence of stringlike or polymeric clusters exhibiting collective particle motion. Moreover, these dynamical clusters have an exponential length distribution, and the average "string" length grows upon cooling according to the predictions of equilibrium polymerization theory. The observed scale of dynamic heterogeneity in glass-forming liquids is found to be consistent with this type of self-assembly process. Both experiments and simulations have revealed remarkable similarities between the dynamical properties of self-assembling and glass-forming liquids, suggesting that the development of a theory for the dynamics of self-assembling fluids will also enhance our understanding of relaxation in glass-forming liquids.

Journal Article↗
PubMed1978

Role of nucleotides in tubulin polymerization: effect of guanosine 5'-methylene diphosphonate.

Incubation of purified rat brain tubulin with guanosine 5'-methylene diphosphonate [GMP(CH2)P] (1 mM), a GDP analog resistant to hydrolysis, results in the polymerization of 20-30% of the total tubulin present. Analogous incubations with GDP (1 mM) do not result in tubulin polymerization. Polymerization with GMP(CH2)P occurs in the presence of alkaline phosphatase (EC 3.1.3.1) under conditions that completely hydrolyze the likely phosphate donors (GTP, GDP, and GMP) as well as the potential product [GMP(CH2)PP] of the transphosphorylase activity present in purified tubulin preparations. Tubulin polymerization in vitro thus can occur in the absence of gamma-phosphate and phosphate bond hydrolysis at the exchangeable nucleotide-binding site of tubulin. Polymerization of tubulin by GMP(CH2)P is neither prevented nor reversed by concentrations of calcium (2 mM) that prevent microtubule assembly and disrupt already formed microtubules induced by GTP. However, tubulin polymerized with GMP(CH2)P is readily depolymerized by cold (4 degrees, 30 min). The possible involvement of GTP alpha-beta bond hydrolysis must be considered seriously as playing a role in the process of microtubule depolymerization.

Alkaline Phosphatase↗
PubMed1998

The C terminus of beta-tubulin regulates vinblastine-induced tubulin polymerization.

Oligoanions such as sodium triphosphate or GTP prevent and/or reverse vinblastine-induced polymerization of tubulin. We now show that the anions of glutamate-rich extreme C termini of tubulin are similarly involved in the regulation of the vinblastine effect. Cleavage of the C termini by limited proteolysis with subtilisin enhances vinblastine-induced tubulin polymerization and abolishes the anion effect. Only the beta-tubulin C terminus needs to be removed to achieve these changes and the later cleavage of the alpha-tubulin C terminus has little additional effect. In fact, vinblastine concentrations >20 microM block cleavage of the alpha-tubulin C terminus in the polymer, whereas cleavage of the beta-tubulin C terminus proceeds unimpeded over the time used. The vinblastine effect on tubulin polymerization is also highly pH-dependent between pH 6.5 and 7.5; this is less marked, but not absent, after subtilisin treatment. A working model is proposed wherein an anionic domain proximal to the extreme C terminus must interact with a cationic domain to permit vinblastine to promote polymerization. Both exogenous and extreme C-terminal anions compete for the cationic domain with the proximal anionic domain to prevent vinblastine-induced polymerization. We conclude that the electrostatic regulation of tubulin polymerization induced by vinblastine resides primarily in the beta-tubulin C terminus but that additional regulation proximal in the tubulin molecule also plays a role.

Animals↗