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PubMed1983

[Effects of poly-L-lysine, poly-L-glycine and poly-L-glutamic acid on ANS fluorescence and electrokinetic potential of splenic lymphocytes in the mouse].

The in vivo effect of either poly-L-Lysine, poly-L-Glutamic acid or poly-L-Glycine on mouse spleen cell populations was investigated. The membrane fluorescence changes of activated splenic lymphocytes were studied. Experiments were performed with the hydrophobic fluorescent probe: 1-anilino-8-naphthalene sulphonate (ANS). Kinetic studies further indicated that the course of fluorescence changes may vary considerably depending upon homopolymers. These fluorescence intensity changes would be in direct or inverse relation to the electrokinetic surface potential changes of activated lymphocytes, as assessed by the electrophoretic mobility analysis. It could be concluded that the relation (direct or inverse) between ANS fluorescence and electrokinetic potential depends upon the net electrical charge of the homopolymer used. In further experiments, the determination of the net electrical charge of some tumour antigens could be considered without hard purifications.

Action Potentials↗
PubMed1983

Supramolecular regulation of the actin-activated ATPase activity of filaments of Acanthamoeba Myosin II.

Acanthamoeba myosin II has three phosphorylation sites clustered near the end of the tail of each of its two heavy chains (six phosphorylation sites/molecule). Myosin II has little or no actin-activated ATPase activity when four to six of these sites are phosphorylated. Maximal actin-activated ATPase activity is obtained when all six sites are dephosphorylated. Under assay conditions, both phosphorylated and dephosphorylated myosin II form bipolar filaments. Filaments of dephosphorylated myosin II have larger sedimentation coefficients than filaments of phosphorylated myosin II but this difference does not explain the difference in their actin-activated ATPase activities. Heteropolymers, formed by mixing soluble dephosphorylated and phosphorylated myosins and then diluting the mixture into low ionic strength buffer containing MgCl2, have sedimentation coefficients close to those of the homopolymer of phosphorylated myosin. The actin-activated ATPase activities of heteropolymers are, under most conditions, lower than the equivalent mixtures of homopolymers of dephosphorylated and phosphorylated myosins. It is concluded, therefore, that the phosphorylation of myosin tails regulates the actin-activated ATPase activity of Acanthamoeba myosin II by affecting the myosin filament as a whole rather than specifically affecting the heads of the phosphorylated myosin molecules only.

Actins↗
PubMedDate not supplied

Glycosaminoglycans and neoplastic transformation.

Two classes of mammalian glycosaminoglycans (GAGs) are distinguished: hyaluronic acid and chondroitin sulphate homopolymers, exhibiting identical repetitive building blocks, versus heparan and dermatan sulphate co-polymers, with differently substituted disaccharidic units. Evidence reported herein suggests that the latter compounds are positive co-factors of matrix assembly promoting the interaction of collagenous and non-collagenous proteins and inhibiting proteolytic activity. Homopolymers, on the contrary, are recognized as negative co-factors impairing the interaction of matrix proteins. The effect of GAGs on matrix assembly influences all the cell periphery because of trans-membrane relationships between submembranous cytoskeletal structures and the outer pericellular matrix. Molecular mechanisms involving GAGs in neoplastic transformation are proposed and discussed.

Animals↗
PubMed1980

Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro.

The DNA-dependent conversion of incorrect deoxynucleoside triphosphate precursors to monophosphates (turnover) by bacteriophage T4 DNA polymerase was determined using either poly(dA) x (dT) or poly(dG) x (dC) homopolymer templates. Competition between correct and incorrect triphosphates for incorporation into DNA, and the use of chain-terminating dideoxynucleoside triphosphates enabled us to determine the amount of turnover occurring at the end of each strand of the homopolymer duplex (e.g. amount of turnover of dATP occurring at the 3'-OH of poly(dG) and the 3'-OH of poly(dC)). These determinations suggest that nearest neighbor interactions between incoming dNTPs and the growing strand terminal residue play a major role in the occurrence of substitution errors during DNA synthesis in vitro byDNA polymerase. When considered together with existing evidence from studies of turnover (Gillin, F. D., and Nossal, N. G. (1976) J. Biol. Chem. 251, 5225-5232) and direct incorporation (Hall, Z. W., and Lehman, I. R. (1968) J. Mol. Biol. 36, 321-333) these results demonstrate that pyrimidine-pyrimidine and purine-purine as well as purine-pyrimidine oppositions have a role in error production at least during DNA replication in vitro. The implications of these results for the role of the "accessory" replication proteins in maintaining accuracy during the DNA biosynthetic process are discussed.

Base Sequence↗
PubMed1994

Construction of a ferroxidase center in human ferritin L-chain.

Ferritins are 24-mer proteins which store and detoxify intracellular iron. Mammalian ferritins are made of two subunit types, the H- and L-chains, with different functional specificity. The H-chain has a metal-binding site (the ferroxidase center) which confers ferroxidase activity to the protein and accelerates iron incorporation. In the L-chain the center is substituted by a salt bridge. We performed several site-directed mutageneses in the L-chain with the aim to construct the center and confer ferroxidase activity to the protein. Most variants were insoluble and did not refold into homopolymers, probably due to electrostatic repulsion introduced by the substitutions. However, they formed hybrids when they were renatured together with the L- or H-chains. The heteropolymers made of 90% L-chain and 10% of an L-variant with all the ligand residues of the H-chain center had 25-30% of the ferroxidase activity of the H-chain homopolymer. This corresponds to the activity of an H/L heteropolymer with 7% H-chain. It is concluded that: (i) it is possible to construct a ferroxidase center in the L-chain with an activity equivalent to that of the H-chain, (ii) the residues of the center interfere with the folding/assembly of the L-, but not of the H-chain, (iii) heteropolymers can be made even between ferritin subunits with large differences of refolding rates.

Amino Acid Sequence↗
PubMed1993

Meso-oligodeoxyribonucleotides.

Meso-DNAs, containing L-sugar and D-sugar in an alternate sequence as the backbone [Fig. 1, designated as LD-(dN)n], were prepared as a modificated oligonucleotides of natural- and enantio-DNA. The characteristics of meso-DNAs were analyzed, focusing on LD-(dA)n and LD-(dT)n. These L-sugar containing oligomers show resistancy to phosphodiesterases. Though both LD-(dA)n and LD-(dT)n bound their corresponding complementary homopolymers, apparent differences of the interaction mode between these two meso-DNAs were observed: [1] Concerning the complex formation with the complementary homopolymers, LD-(dA)n favors a triplex formation while LD-(dT)n forms only duplex, and [2] Concerning DNA/RNA selectivity for the complex formation, LD-(dA)n interacted with poly U more strongly than poly dT (RNA-selective), while LD-(dT)n showed stronger interaction with poly dA than poly A (DNA-selective). The similarities in CD-spectra of LD-oligomer/natural polymer complexes to natural complexes suggest that the conformation possesses a structure close to a natural right-handed helix conformation.

Adenine↗
PubMed1995

The lipopolysaccharide of Legionella pneumophila serogroup 1 (strain Philadelphia 1): chemical structure and biological significance.

The lipopolysaccharide (LPS, endotoxin) of Legionella pneumophila serogroup 1 (Philadelphia 1) exhibits peculiar chemical features which may account for its importance as a bacterial virulence factor. The O-chain of this LPS constitutes a homopolymer of an unusual sugar, 5-acetamidino-7-acetamido-8-O-acetyl-3,5,7, 9-tetradeoxy-D-glycero-L-galacto-nonulosonic acid (legionaminic acid) of which about 10-75 residues are present. Due to the lack of free hydroxyl groups, this homopolymer renders the cell surface highly hydrophobic and, therefore, supports adherence to the membrane of target cells including alveolar macrophages. Investigations of the serological specificity of the serogroup 1 LPS revealed a monoclonal antibody (mAb 3/1) which recognizes an epitope located in the environment of the 8-O-acetyl group of legionaminic acid. According to epidemiological studies, this determinant appears to be associated with L. pneumophila virulence. The outer core oligosaccharide of L. pneumophila LPS exhibits also hydrophobic properties due to the presence of N- and O-acetyl groups as well as 6-deoxy sugars. The inner core expresses both similarities and differences as compared to enterobacterial core oligosaccharides in containing Kdo but lacking heptose and phosphate groups. Lipid A possesses some unique structural features since its backbone consists of a bisphosphorylated beta-GlcpN3N-(1-->6)-GlcpN3N disaccharide with only amide-linked acyl groups having 14-22 carbon atoms. Long chain fatty acids [28:0(27-oxo) and 27:0-dioic] possessing the double length as enterobacterial acyl groups, may be responsible for the low endotoxicity of L. pneumophila lipid A.

Animals↗
PubMed1998

Analysis of ferritins in lymphoblastoid cell lines and in the lens of subjects with hereditary hyperferritinemia-cataract syndrome.

Hereditary hyperferritinemia-cataract syndrome (HHCS) is an autosomal and dominant disease caused by heterogeneous mutations in the iron responsive element (IRE) of the 5' untranslated flanking region of ferritin L-chain mRNA, which reduce the binding to the trans iron regulatory proteins and make L-chain synthesis constitutively upregulated. In the several families identified so far, the serum and tissue L-ferritin levels are fivefold to 20-fold higher than in nonaffected control subjects, iron metabolism is apparently normal, and the only relevant clinical symptom is early onset, bilateral cataract. Some pathogenetic aspects of HHCS remain obscure, with particular reference to the isoferritins produced by HHCS cells, as well as the mechanism of cataract formation. We analyzed lymphoblastoid cell lines obtained from two nonaffected control subjects and from HHCS patients carrying the substitution A40G (Paris-1), G41C (Verona-1), and the deletion of the residues 10-38 (Verona-2) in the IRE structure. Enzyme-linked immunosorbent assays specific for the H- and L-type ferritins showed that L-ferritin levels were up to 20-fold higher in HHCS than in control cells and were not affected by iron supplementation or chelation. Sequential immunoprecipitation experiments of metabolically-labeled cells with specific antibodies indicated that in HHCS cells about half of the L-chain was assembled in L-chain homopolymers, which did not incorporate iron, and the other half was assembled in isoferritins with a high proportion of L-chain. In control cells, all ferritin was assembled in functional heteropolymers with equivalent proportion of H- and L-chains. Cellular and ferritin iron uptake was slightly higher in HHCS than control cells. In addition, we analyzed the lens recovered from cataract surgery of a HHCS patient. We found it to contain about 10-fold more L-ferritin than control lens. The ferritin was fully soluble with a low iron content. It was purified and partially characterized. Our data indicate that: (1) in HHCS cells a large proportion of L-ferritin accumulates as nonfunctional L-chain 24 homopolymers; (2) the concomitant fivefold to 10-fold expansion of ferritin heteropolymers, with a shift to L-chain-rich isoferritins, does not have major effects on cellular iron metabolism; (3) L-chain accumulation occurs also in the lens, where it may induce cataract formation by altering the delicate equilibrium between other water-soluble proteins (ie, crystallins) and/or the antioxidant properties.

Antioxidants↗
PubMed1996

Developmental increases in expression of neurofilament mRNA selectively in projection neurons of the lamprey CNS.

Neurofilaments of the sea lamprey are unique in being homopolymers of a single subunit (NF-180). Digoxigenin-labeled RNA probes complementary to NF-180 were used to determine the distribution and timing of expression of neurofilament message in the brain and spinal cord of the lamprey. In the brainstem, detection of NF-180 mRNA was restricted to neurons with axons projecting to the spinal cord or the periphery. The majority of brainstem neurons, whose axons project locally, did not express NF-180 within the detection limits of this technique. NF-180-positive neurons included cells with a wide range of axon diameters, suggesting neurofilament mRNA expression was linked to axon length rather than caliber. To further evaluate this hypothesis, expression was studied in animals of different developmental stages between larvae and adults. In younger (shorter) larvae, the large Mauthner and rhombencephalic Müller cells did not express NF-180 mRNA, even though their axons are among the largest caliber in the animal and extend the entire length of the spinal cord. In contrast, many other reticulospinal neurons, whose axons are smaller in diameter than those of the Müller and Mauthner cells, expressed NF-180 message throughout larval development. Furthermore, neurons of the cranial motor nuclei did not express NF-180 until later developmental stages and the extraocular motor neurons did not label until metamorphosis. Therefore, while detectable neurofilament mRNA expression in the lamprey is restricted to neurons with long axons, its expression in this population of neurons appears to be developmentally regulated by factors still not determined. It is postulated that need for NF message is determined by a balance between the volume of axon to be filled and the rate of turnover of NF in that axon.

Animals↗
PubMedDate not supplied

Structural studies on polymer whiskers by transmission electron microscopy: I. Morphological and high-resolution observations.

The structures of poly(p-hydroxybenzoic acid) (PHBA) whisker crystals and crystalline fine fibrils of copolymer prepared from p-hydroxybenzoic acid (HBA) and 2-hydroxy-6-naphthoic acid (HNA), namely poly(HBA/HNA) (monomer molar ratio: 97/3), were investigated by transmission electron microscopy (TEM). As for a PHBA whisker, microfibril-like bright regions were recognized in the 210 dark-field image. In the high-resolution TEM image of another PHBA whisker, however, lattice fringes were continuous through the whisker, showing that the whisker is highly crystalline and almost perfect. On the other hand, in the high-resolution images of poly(HBA/HNA) fine fibrils, granular crystallites (20-40 nm in lateral dimension) were observed. The lattice fringes in the crystallites were not successfully indexed with the orthorhombic unit cells of the homopolymer crystal, suggesting the coexistence of another different structure as a minor component.

Crystallization↗
PubMed1999

Inhibition of heparanase activity and tumor metastasis by laminarin sulfate and synthetic phosphorothioate oligodeoxynucleotides.

Heparanase activity correlates with the metastatic potential of tumor cells. Moreover, the anti-metastatic effect of non-anti-coagulant species of heparin and certain sulfated polysaccharides was attributed to their heparanase-inhibiting activity. We investigated the effect of a chemically sulfated polysaccharide (laminarin), consisting primarily of beta-1,3 glucan (sodium laminarin), and of synthetic phosphorothioate oligodeoxynucleotides, primarily phosphorothioate homopolymer of cytidine (SdC28), on heparanase activity and tumor metastasis. Investigation of the ability of tumor cells to degrade heparan sulfate in intact extracellular matrix revealed that heparanase activity expressed by B16-BL6 mouse melanoma cells and 13762 MAT rat mammary adenocarcinoma cells was effectively inhibited by LS (50% inhibition at 0.2-1 microgram/ml), but there was no inhibition by sodium laminarin up to a concentration of 50 microgram/ml. Complete inhibition of the melanoma heparanase was obtained in the presence of 0.1 microM SdC28. A single i.p. injection of laminarin sulfate, but not of sodium laminarin, before i.v. inoculation of the melanoma or breast-carcinoma cells inhibited the extent of lung colonization by the tumor cells by 80 to 90%. Similar inhibition was exerted by 0.1 microM SdC28. At the effective concentrations, both compounds had a small effect on proliferation of the tumor cells and on growth of the primary tumors in vivo. These results further emphasize the involvement of heparanase in tumor metastasis and the potential clinical application of diverse heparanase-inhibiting molecules such as sulfated polysaccharides and synthetic polyanionic molecules.

Animals↗
PubMed1999

Characterization of partially transesterified poly(beta-hydroxyalkanoate)s using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.

Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) was used for the characterization of a partially transesterified poly(beta-hydroxyalkanoate), PHA, polymer produced by the bacterial strain Alcaligenes eutrophus using saponified vegetable oils as the sole carbon sources. The transesterification was carried out separately under acidic and basic conditions to obtain PHA oligomers weighing less than 10 kDa. The intact oligomers were detected in their cationized [M + Na](+) and [M + K](+) forms by MALDI-TOFMS. A composition analysis, using the MALDI-TOF spectra, indicate that the oligomers obtained via acid catalysis were terminated with a methyl 3-hydroxybutyrate end group, and those obtained by base catalysis had a methyl crotonate (olefinic) termination. In addition to HB (hydroxy butyrate), the oligomers were found to contain a small percentage of HV (hydroxy valerate). This was independently confirmed using gas chromatography/mass spectrometry (GC/MS). In comparison, the analysis of a commercial PHA polymer, transesterified under identical conditions, only showed the presence of HB, i.e. a pure PHB homopolymer. Copyright 1999 John Wiley & Sons, Ltd.

Journal Article↗
PubMed1997

Ordered aggregation of ribonucleic acids by the human immunodeficiency virus type 1 nucleocapsid protein.

The nucleocapsid protein NCp7, which is the major genomic RNA binding protein of human immunodeficiency virus type 1, plays an important role in several key steps of the viral life cycle. Many of the NCp7 activities, notably the nucleic acid annealing and the genomic RNA wrapping ones, are thought to be linked to a nonspecific binding of NCp7 to its nucleic acid targets. The mechanism of these activities is still debated but several clues are in favor of an intermediate aggregation of nucleic acids by NCp7. To check and characterize the nucleic acid aggregating properties of NCp7, we investigated the interaction of NCp7 with the model RNA homopolymer, polyA, by quasielastic light scattering and optical density measurements. The ordered growth of monodisperse large particles independently of the nucleic acid size and the almost complete covering of polyA by NCp7 strongly suggested an ordered aggregation mechanism. The aggregate kinetics of growth in the optimum protein concentration range (> or = 2 microM) were governed by a so-called Ostwald ripening mechanism limited by transfer of NCp7-covered polyA complexes from small to large aggregates. The aggregation process was strongly dependent on both Na+ and Mg2+ concentrations, the optimum concentrations being in the physiological range. Similar conclusions held true when polyA was replaced by 16S + 23S ribosomal RNA, suggesting that the NCp7 aggregating properties were only poorly dependent on the nucleic acid sequence and structure. Finally, as in the NCp7 annealing activities, the basic regions of NCp7, but not the zinc fingers, were found critical in nucleic acid aggregation. Taken together, our data indicate that NCp7 is a highly efficient nucleic acid aggregating agent and strengthen the hypothesis that aggregation may constitute a transient step in various NCp7 functions.

Amino Acid Sequence↗
PubMed1997

Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: comparison with Zimm-Bragg and Lifson-Roig formalisms.

In this work we present the development of the multiple sequence approximation (AGADIRms) and the standard one-sequence approximation (AGADIRls) within the framework of AGADIR's alpha-helix formation model. The extensive comparison between these new formulations and the original one [AGADIR; V. Muñoz and L. Serrano (1994). Nat. Struct. Biol., Vol. 1, pp. 399-409] indicates that the standard one-sequence approximation is virtually identical to the multiple sequence approximation, while the previously used residue partition function approximation [Muñoz and Serrano (1994); (1995), J. Mol. Biol., Vol. 245, pp. 275-296] is less precise. The calculations of the average helical content performed with AGADIR are precise for peptides of less than 30 residues and progressively diverge from the multiple sequence formulation for longer peptides. The helicity distribution of heteropolypeptides with less than 50% average helical content is also well described, while those of quasi-homopolymers with high helical content tend to be-flattened. These inaccuracies lead to an underestimation of 0.017 kcal/mol for the mean-residue enthalpic contribution in AGADIR, as compared to AGADIRms and AGADIRls. The other energy contributions to alpha-helix stability are not affected by the original statistical approximation. We also discuss the particularities of the model for alpha-helix formation utilized in AGADIR and compare it with the classical Zimm-Bragg and Lifson-Roig theories. Moreover, we develop the mathematical relationships between the basic AGADIR energy contributions and helix nucleation and elongation, which permit the quantitative comparison between formalisms. Remarkably, the comparison between AGADIRms and the Lifson-Roig formalism shows that, despite the differences on treating helix/coil cooperativity, both theories give virtually identical results when an equivalent set of parameters is used. This indicates that the helix/coil transition is a solid theory independent of the particularities of the model for alpha-helix formation.

Mathematics↗
PubMed1996

Effect of fibronectin amount and conformation on the strength of endothelial cell adhesion to HEMA/EMA copolymers.

The effect of substrate surface hydrophobicity on fibronectin (Fn) adsorption and endothelial cell adhesion strength was studied. Bovine aortic endothelial cells (BAEC) were plated for 2 h with and without preadsorbed Fn on slides coated with homopolymers and copolymers of hydrophilic polyhydroxyethylmethacrylate (polyHEMA) and hydrophobic polyethylmethacrylate (polyEMA). The polarity of the substrate was determined by Wilhelmy plate contact angle. The amount of adsorbed Fn was determined using 125I-labeled Fn. Attenuated total reflection Fourier transform infrared (ATR-FTIR) spectroscopy was used to detect gross conformational changes of adsorbed Fn on polyHEMA or polyEMA. BAEC were cultured in serum-free medium for 2 h and subjected to a brief exposure of laminar flow in a variable-height flow chamber that provided a range of shear stresses of 15-185 dynes/cm2. The critical shear stress to detach 50% of the cells increased with increasing EMA content to a maximum at 20% HEMA/80% EMA copolymer irrespective of the presence of preadsorbed Fn. However, the critical force increased even though there were similar amounts of Fn adsorbed on all substrates. ATR-FTIR spectroscopy showed only minor changes in beta-sheet structure of Fn adsorbed to polyHEMA and polyEMA. These results show that the force to detach cells did not increase solely with increasing amounts of adsorbed Fn; rather, these results indicate a more complex interplay involving both the amount and conformation of adsorbed Fn.

Animals↗
PubMed1998

Active platelet movements on hydrophobic/hydrophilic microdomain-structured surfaces.

The early motion and interaction of platelets on a microdomain-structured block copolymer surface composed of 2-hydroxyethyl methacrylate (HEMA)-styrene were analyzed and compared with those on a compositionally identical random copolymer, homopolymer poly (HEMA) (hydrophilic) and polystyrene (hydrophobic) surfaces. Contacting platelets were quantitatively more active, with motions including rolling, detachment, oscillatory vibration, and change of direction only on the HEMA-St block copolymer surface. Active platelet movements were observed for long time periods (>20 min) on HEMA-St block copolymer surfaces and were distinct from those for inert PSt latex particles on these same surfaces, demonstrating that platelet movements were not due to physical forces such as convection, hydrophobic interactions, or microbrownian movement. To study the cause and mechanism underlying the platelet movements, platelets treated with an adenosine triphosphate (ATP) synthesis inhibition, NaN3, or a membrane skeleton-disrupting chemical agent, dibucaine, were also studied on these surfaces. Both treatments reduced platelet movement and demonstrated that platelets in contact with the HEMA-St block copolymer surface require metabolic processes consuming ATP and involve dynamics of their membrane skeleton. These energy-consuming active movements might explain the previously observed lower platelet activation and low thrombogenicity of the HEMA-St block copolymers. Enhanced platelet movements on the HEMA-St block copolymer surface show that the microdomain surface interacts uniquely with platelets to hinder activation and preserve passive platelet function despite surface contact.

Adenosine Triphosphate↗
PubMed1999

Hydrophilic acrylic biomaterials derived from vitamin E with antioxidant properties.

Hydrogels based on polymeric derivatives of vitamin E for biomedical purposes have been prepared by copolymerization reaction of the alpha-tocopheryl methacrylate (V) with 2-hydroxyethyl methacrylate (H) in a range of composition between 5-20 wt % of V. The swelling behavior of the hydrogels in water, alkaline, and acidic media showed a slight decrease in the equilibrium water content with the content of V in the copolymer although in all cases it was superior to an EWC > 20%. The diffusion mechanism followed a Fickian behavior in all media. The values of the diffusion coefficients were in the range 2.5-1.6 10(-7) cm2/s. The states of water in the hydrogels were determined by DSC. A decrease in the content of freezing water was obtained with the V content for all media, and for all compositions lower values of freezing water were obtained in acidic or basic pHs than in distilled water. The copolymeric xerogels, analyzed by contact angle measurements, deviated from those expected taking into consideration those of the homopolymers and the average fraction of the monomers in the copolymer. The polar contribution dropped with the introduction of a small content (4 wt %) of the vitamin E-containing monomer, and it reached a value similar to that of poly-V for a composition of 49 wt % of V in the copolymer. This behavior is accounted for by the segregation of the macromolecular chains of both kinds of monomers, due mainly to differences in their polarity, molecular weights, and the reactivity of both monomers. Finally, thermogravimetric analysis showed a higher thermal (antioxidant) stability of the poly-V with respect to poly-H, giving rise to a residue of 18 wt %. The V-containing copolymers also showed an improved stability (antioxidant behavior), indicating the possibility of the V unit's interfering with the oxidative process, based on free-radical species, and, therefore, with the aging process at the cellular level.

Algorithms↗
PubMed1999

Synthesis, physical characterization, and biological performance of sequential homointerpenetrating polymer network sponges based on poly(2-hydroxyethyl methacrylate).

A limitation in the use of hydrophilic poly(2-hydroxyethyl methacrylate) (PHEMA) sponges as implantable devices is their inherently poor mechanical strength. This precludes proper surgical manipulation, especially in the eye where the size of the implant is usually small. In this study a new method was developed to produce mechanically stronger PHEMA sponges. Sequential homointerpenetrating polymer network (homo-IPN) sponges were made by using HEMA as the precursor for generating both the first network and the successive interpenetrated networks. Following the formation of network I, the sponge was squeezed to remove the interstitial water, soaked in the second monomer (also HEMA), and squeezed again to remove the excess monomer from the pores before being subjected to the second polymerization leading to the formation of network II. Two two-component IPN sponges (K2 and K4) with increasing HEMA content in the network II and a three-component IPN sponge (K3) were produced, and their properties were compared to those of a homopolymer PHEMA sponge (control). Apart from elongation, the tensile properties were all significantly enhanced in the IPN sponges; the water content was the same as in the control sponge, except for sponge K4, which was lower. Light microscopy revealed similar pore morphologies of the control and IPN sponges K2 and K3, and the majority of the pores were around 25 microm. Sponge K4 displayed smaller pores of around 10 microm. Cellular invasion into the sponges was examined in vitro (incubation with 3T3 fibroblasts) and in vivo (implantation in rabbit corneas). Although the in vitro assay detected a change in the cell behavior in the early stage of invasion, which was probably due to the formation of IPNs, such changes were not reflected in the longer term in vivo experiment. There was a proper integration of sponges K2 and K3 with the corneal stroma, but much less cellular invasion and no neovascularization in sponge K4. We concluded that IPN formation is a valid method to enhance the strength of PHEMA sponges, provided that the content of HEMA in the successive networks is not too high.

Animals↗