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PubMed1996

Prediction of potential protein-protein interaction sites from amino acid sequence. Identification of a fibrin polymerization site.

Identification of a protein-protein interaction site is an important step that has significant potential to clarify structure-function relationships of proteins and drug design. We propose here a unique predictive method to identify protein-protein interaction sites based on the observation that proline is the most common residue found in the flanking segments of interaction sites [Kini, R.M. and Evans, H.J. (1995) Biochem. Biophys. Res. Commun. 212, 1115-1124]. Accordingly, the interaction sites of proteins might be predicted directly from the amino acid sequence based on the presence of proline brackets. Using this strategy, we have predicted a polymerization site in the epitope of the Aalpha-chain of fibrinogen recognized by a monoclonal antibody, 9E9 which inhibits fibrin polymerization [Cierniewski, C.S. and Budzynski, A.Z. (1992) Biochemistry 31, 4248-4253]. The synthetic peptide comprising this predicted site inhibited the coagulation of human blood and allosterically interfered in fibrin polymerization. This is the first known allosteric polymerization site of fibrinogen. Thus the results validate the predicted site and the method for prediction. This unique predictive method should help in identifying the interaction sites of many proteins.

Allosteric Regulation↗
PubMed1989

Characterization of the binding sites for glutaraldehyde-polymerized albumin on purified woodchuck hepatocyte plasma membranes.

Highly purified woodchuck hepatocyte plasma membranes demonstrated tight specific binding to glutaraldehyde-polymerized serum albumin immobilized on Sepharose macrobeads. This phenomenon was characterized in detail and used for recognition of the plasma membrane constituents involved in binding of the albumin polymer. The hepatocyte membrane-polyalbumin interaction was found to be ligand-specific, saturable, and time-dependent. Other characteristics of a specific receptor-ligand interaction were also noted, including a dependence on the temperature, pH, and ionic strength of the binding medium. Kinetic studies revealed the presence of two classes of binding sites for glutaraldehyde-polymerized albumin on purified membranes. The sites mediating the saturable high-affinity binding of polymer to hepatocyte membranes could not be solubilized by Triton X-100. Binding activity of Triton-insoluble membrane residues was inhibited by heat treatment and proteolysis, and was significantly suppressed by neuroaminidase digestion. These findings suggest a glycoprotein nature for the high-affinity binding sites and indicate that the corresponding receptors apparently are tightly associated with the plasma membrane matrix. In contrast, low-affinity binding of polymeric albumin was inhibited by both Triton X-100 and pronase, was resistant to neuraminidase, and was activated by lipase, suggesting that membrane lipids are important for the binding conduct. In conclusion, these results provide clear evidence that hepatocyte plasma membranes are endowed with at least two classes of chemically distinct binding components, which are able to specifically recognize serum albumin artificially modified by glutaraldehyde treatment. Therefore, they suggest that in vivo hepatocytes may perform a specific receptor-dependent uptake of ligands expressing glutaraldehyde-polymerized albumin specificity. This phenomenon may play an important role in the proposed participation of naturally modified human serum albumin as a bridge in the attachment and penetration into host hepatocyte of hepatitis B virus, which is known to possess a receptor that is specific for glutaraldehyde-cross-linked human serum albumin.

Animals↗
PubMed1983

Preparation and evaluation of pyridoxalated-polymerized human hemoglobin.

A solution of hemoglobin has several potential applications as a blood substitute. However, because of high oxygen affinity (P50 approximately 14 mm Hg) and short vascular retention time of hemoglobin (plasma half-disappearance time approximately 3.5 hr), a solution of hemoglobin presents limitations for its general use in blood replacement therapy. To overcome these limitations crystalline hemoglobin was modified by pyridoxalation and subsequent polymerization. Pyridoxalation yielded a product with a P50 ranging from 23 to 26 mm Hg. The pyridoxalated hemoglobin was then polymerized with glutaraldehyde and the final modified hemoglobin showed a P50 of 19 to 22 mm Hg. The modified hemoglobin was tested in vitro for coagulation activities. The results indicated that no adverse coagulant activity was demonstrated by the modified products. In vivo studies in the rat have shown that pyridoxalated-polymerized hemoglobin has a plasma half-disappearance time of about 25 hr. The data demonstrated that a solution of pyridoxalated-polymerized hemoglobin, because of its lower oxygen affinity and longer vascular retention than unmodified hemoglobin, has significant potential as a basis for an efficient resuscitation solution.

Animals↗
PubMed1989

Incomplete polymerization of Cavalite with the use of recommended photopolymerization times: a warning of possible cytotoxic effects.

As part of a study of the suitability of new materials for use as a retrofilling material, we examined the polymerization properties of Cavalite, a light-cured, hydroxyapatite and glass ionomer-containing cavity liner. By varying the time of photopolymerization, it was found that polymerization for 20 to 30 seconds according to the manufacturer's recommendations is not sufficient to ensure complete polymerization. The implications of this incomplete polymerization are discussed in terms of possible cytotoxic effects on tissues exposed to unpolymerized Cavalite, both when used in retrofilling situations and as a deep cavity liner.

Acrylic Resins↗
PubMed1984

Effects of methylmercury and some metal ions on microtubule networks in mouse glioma cells and in vitro tubulin polymerization.

Mercury compounds and some other metal ions were investigated with respect to their effect on in vitro tubulin polymerization and on cellular microtubules in mouse glioma. In vitro tubulin polymerization was completely inhibited by 2.5 X 10(-5) M Hg2+, 5 X 10(-5) M CH3Hg+, 2 X 10(-4) M Cr3+, 2.5 X 10(-4) M Cu2+, and 5 X 10(-4) M Cd2+. Zn2+ did not affect the polymerization up to 5 X 10(-4) M. Indirect immunofluorescence study with rabbit antiporcine tubulin antibody revealed that methylmercury disrupted the microtubule network at an early stage of growth inhibition. On the other hand, in the presence of Cd2+, Cu2+, and Cr3+ at their growth inhibitory concentrations, no effects on microtubule networks were observed for the first 1 hr. These results indicate that only methylmercury affects cellular microtubules, while other ions seem to interfere with other sites in the cells, although these ions showed the ability to depress in vitro tubulin polymerization.

Animals↗
PubMed1985

The molecular localization of the ability of certain monoclonal immunoglobulins to interfere with fibrin polymerization.

When a purified myeloma protein with the ability to inhibit fibrin polymerization was preincubated with sheep anti-human F(ab')2 antibodies, there was a marked reduction of the ability to prolong the thrombin clotting time, while anti-Fc antibodies had only a slight effect. A monoclonal immunoglobulin which shortens the thrombin time was uninfluenced by anti-F (ab')2 as well as by anti-Fc antibodies. Partial reduction and alkylation of the immunoglobulins did not modify their effect on the thrombin time. None of the immunoglobulins bound to fibrinogen or fibrin monomer that had been linked to CNBr-activated agarose. Myeloma proteins may interfere with fibrin polymerization in two ways: some proteins inhibit polymerization in a reaction that depends on the Fab (antigen binding) part of the molecule; however, antibody binding activity against fibrinogen or fibrin monomer has not been demonstrated. Other (rare) myeloma proteins accelerate fibrin polymerization; this effect cannot be ascribed to any particular portion of the molecule and is probably of an unspecific nature.

Animals↗
PubMed1980

Polymerized insoluble bee venom.

Using a polymerization process previously used for ragweed allergens, honeybee venom was polymerized. Instead of soluble polymers, an insoluble precipitate, polymerized insoluble bee venom (PIBV), is the result. A major allergen of honeybee venom, 125I phospholipase A (PL-A) incorporated into PIBV, was shown to have decreased dissemination from subcutaneous injection sites. After thorough mixing, samples of PIBV can be withdrawn from a vial with a syringe with no more than 10% error. Approximately 90% of PL-A was incorporated with PIBV. The soluble PL-A was removed during subsequent washing of the PIBV and this soluble PL-A was shown to be polymerized mainly to high-molecular weight PL-AS. PIBV (20 mg) injected in each of six rabbits resulted in formation of precipitating antibody in all rabbits. The rabbit antisera bound 125I PL-A and reacted with PL-A in whole been venom. These physical and immunologic characteristics of PIBV suggest further study of its potential for human use.

Absorption↗
PubMed1980

Regulation of actin polymerization by villin, a 95,000 dalton cytoskeletal component of intestinal brush borders.

A 95,000 dalton actin-binding polypeptide, villin, has been purified to 98% homogeneity from brush border cytoskeletons of chicken intestinal epithelial cells. In vitro, this protein exerts control over the polymerization of actin. In the presence of villin, the lag phase preceding detectable actin polymerization is shortened and the steady state equilibrium viscosity is reduced in proportion to the amount of villin present. A molar ratio of villin:actin of 1:40 results in a 70% reduction of the Ostwald viscosity. Significant effects can be detected at a ratio of 1:600. These ratios are physiologically relevant because the ratio of villin:actin in brush borders is 1:13 and in isolated microvilli is 1:9-12. Reduction of viscosity is mirrored by an increase in the amount of protein which fails to sediment at 150,000 X g for 60 min. An assay of the nonsedimentable protein for actin monomers by the inhibition of DNAase I showed that the concentration of monomer was not significantly altered by the presence of villin. Electron microscopic examination of negatively stained, nonsedimentable actin demonstrated that the presence of villin during actin polymerization results in the production of short oligomers which cannot anneal with each other to form long filaments. Villin is also effective in reducing the viscosity of F-actin when it is added to a fuly polymerized actin sample. In view of these striking properties, villin is likely to be an important in vivo regulator of cytoskeletal structure and, by implication, of cell shape and motility.

Actins↗
PubMed1980

The polymerization of fibrinogen under the influence of diazomethane modification.

To study the effect of the acidic amino acid residues on the physiological polymerization and clot formation of fibrinogen, the fibrinogen system was polymerized by interaction with diazomethane, a specific group reagent which modifies the carboxylic acid residues via the process of methylation. The extent of methylation of fibrinogen by diazomethane was estimated by methoxyl determination on the modified fibrinogen. Under the present experimental conditions, no significant amounts of ammonia were detected as a result of amide hydrolysis concomitant with esterification of the fibrinogen. Chemical methylation of approximately 214 residues resulted in polymerization of the fibrinogen molecule to a product which resembled the physiological clot formation. The application of paper chromatographic techniques identified the modification of other amino acid residues in addition to the methylation of the carboxylic acid groups of glutamic and aspartic acids. These results are interpreted in terms of methylation of carboxylic acid groups in fibrinogen by diazomethane providing a reduction of both negative charge and intermolecular repulsion, thereby enabling the modified fibrinogen molecules to polymerize.

Animals↗
PubMed1987

Polymers for biodegradable medical devices. III. Polymerization and copolymerization of cyclic derivatives of tartronic acid.

The syntheses of anhydrosulphite and anhydrocarboxylate derivatives of tartronic acid are described. These compounds, more correctly named 5-carboxy-1,3,2-dioxathiolan-4-one-2-oxide and 5-carboxy-1,3-dioxolan-2,4-dione have been shown to undergo polymerization and copolymerization to poly-alpha-esters containing the tartonic acid residue, characterized by the presence of a pendant carboxyl group. Thermal polymerization of the anhydrosulphite appears to proceed in a substantially identical manner to other members of the series in which the monomer decomposes by a first order process to yield an alpha-lactone which polymerizes by a rapid chain growth reaction. Because the rate of thermal polymerization of tartronic acid anhydrosulphite is much more rapid than simple alkyl substituted anhydrosulphites, copolymerization favours the former residues. More successful copolymerization was achieved by the use of tertiary base initiators and the anhydrocarboxylate derivative of tartronic acid. The polymers and copolymers described are of potential value in the synthesis of drug-carrying biodegradable matrices or more hydrophilic analogues of poly(glycolic acid) which combine the known bioerodibility of the moiety with that presence of a pendant carboxyl group.

Biocompatible Materials↗
PubMed1989

Cross-linking and ring opening during polymerization of heterocyclic methacrylates and acrylates.

Heterocyclic methacrylates have been shown to have low polymerization shrinkage. In this paper, the extent of ring opening has been assessed by the degree of consequent cross-linking. In polymers of tetrahydrofurfuryl methacrylate and acrylate, tetrahydropyranyl and tetrahydropyran-2-ylmethyl methacrylate, fewer than 1% monomer units were involved in cross-linking and hence ring-opening reactions. 2-epoxypropyl methacrylate, when polymerized, was very extensively cross-linked indicating prolific ring opening. However, the polymerization shrinkage of this material was the highest of the heterocyclic methacrylates studied and was that predicted from the known molar volume change of methacrylate esters. Ring opening does not, therefore, appear to be a significant factor in the polymerization shrinkage of heterocyclic methacrylates.

Acrylates↗
PubMed1990

Prevention of calcification of glutaraldehyde pretreated bovine pericardium through controlled release polymeric implants: studies of Fe3+, Al3+, protamine sulphate and levamisole.

Calcification is the principal cause of the clinical failure of bioprosthetic heart valves fabricated from glutaraldehyde pretreated porcine aortic valves or bovine pericardium. The present study investigated controlled-release implants for prevention of the calcification of glutaraldehyde pretreated bovine pericardium in a rat subdermal model. Either Al3+ and Fe3+ (inhibitors of the growth and dissolution rate of hydroxyapatite crystals), levamisole (alkaline phosphatase inhibitor) or protamine sulphate (charge modifier) were individually incorporated into various polymeric carriers (either silicone rubber, polyurethane or silicone rubber-polyurethane copolymer). Polymeric implants were evaluated for in vitro release kinetics, which revealed that sustained drug release was obtained from 21 d to more than 90 d from various drug matrices. In vivo efficacy was studied by co-implanting the polymeric delivery systems with glutaraldehyde pretreated bovine pericardium for 21 d using a subdermal rat model; glutaraldehyde pretreated bovine pericardium calcium levels were quantitated by atomic absorption spectroscopy in the explanted tissues. Fe3+ and Al3+ polymeric implants were the most effective for inhibiting deposition of calcium mineral. Al3+ demonstrated 82% inhibition of calcification compared to controls and Fe3+ resulted in 80% inhibition of calcification. Specific histologic staining methods showed that Fe3+ and Al3+ were localized within the devitalized cells of the explanted glutaraldehyde pretreated bovine pericardium. No adverse effects on somatic growth or recipient bone morphology were noted following controlled-release drug administration. Controlled release of protamine sulphate or levamisole did not significantly inhibit glutaraldehyde pretreated bovine pericardium calcification. It is concluded that regional controlled release of Fe3+ or Al3+ inhibits glutaraldehyde pretreated bovine pericardium calcification in the rat subdermal model without adverse effects.

Aluminum↗
PubMed1994

Polymerization kinetics, glass transition temperature and creep of acrylic bone cements.

Sulfix-6 and Zimmer LVC 60/30 bone cements were selected and the polymerization kinetics and resulting glass transition temperature Tg; creep behaviour in the dry or water-saturated state; and sorption and diffusion of water were studied. The calculation of conversion was based on a comparison of the residual polymerization heat measured by differential scanning calorimetry and the corresponding theoretical value. The conversion reached 99% after 90 min of quasi-adiabatic polymerization starting at 23 degrees C or after 10 min of isothermal polymerization at 37 degrees C. The Tgs of the cements prepared in the former way were about 82 and 100 degrees C, respectively. Creep rate of the bone cements at 37 degrees C decreased with the time of creeping. Sorbed water enhanced the compliance, but reduced the creep rate for long times so that water sorption during the service time may not have detrimental effects on the creep resistance of the cements. Both types of cements contained about 1% of low molar mass substances extractable by water. Measurements of the sorption kinetics of water showed that the diffusion coefficient is 0.14 x 10(-11) and 0.22 x 10(-11) m2/s and 1 yr sorption achieves 2.11% and 2.89% for Sulfix and Zimmer, respectively.

Adsorption↗
PubMed1996

In situ analysis of the degree of polymerization of bone cement by using FT-Raman spectroscopy.

A method has been developed which enables an in situ analysis of the degree of polymerization of bone cement. The concentration of monomeric double bond is monitored continuously during the entire curing process and hence the method can be used for quantitative studies of polymerization kinetics. In this study, Fourier Transform Raman (FTR) spectroscopy was utilized to investigate the degree of polymerization of a novel bone cement in situ, and the results are compared with the thermal profile obtained for polymerization.

Biocompatible Materials↗
PubMed1995

In situ polymerization of pyrrole in animal tissue in the formation of hybrid biomaterials.

Porcine pericardium was impregnated with pyrrole or its derivative, sodium 4-(3-pyrrolyl)butanesulphonate (SPBS), by soaking the animal tissue in the monomer. Subsequent in situ chemical polymerization of the monomer-rich tissue using FeCl3 as initiator produced black polypyrrole-tissue hybrid biomaterials. The rate and extent of polymerization was found to be greater in 0.5 M acetic acid than in Hepes-buffered saline (HBS) and also greater for SPBS than for pyrrole. However, better tissue integrity was obtained for polymerization in HBS. Histological examination showed that the monomers do not permeate through the entire tissue, restricting polymerization to the surface layers of the tissue. The samples so formed do not exhibit detectable electrical conductivity.

Acetates↗
PubMed1985

Bovine aorta actin. Development of an improved purification procedure and comparison of polymerization properties with actins from other types of muscle.

Crude actin extracts from acetone-dried powder of the muscle layer of bovine aorta contain an actin-modulating protein which promotes nucleation of actin monomers and decreases the average length of actin filaments in a Ca2+-dependent manner. This observation has allowed the development of an improved purification procedure for aorta actin which increases the yield 2- to 3-times. The actin obtained with this procedure consists of 77% alpha- and 23% gamma-isoelectric species. Pure aorta actin is indistinguishable from actins from skeletal, cardiac and chicken-gizzard smooth muscle in its polymerization rate, critical concentration, and reduced viscosity when polymerized with KCl at 25 degrees C. It differs from sarcomeric actins, but not from chicken-gizzard smooth muscle actin, in the temperature dependence of polymerization equilibria in KCl. This difference correlates with the amino acid replacements Val-17----Cys-17 and Thr-89----Ser-89, supporting a conclusion drawn from other studies that the N-terminal portion of actin polypeptide chain contains sites important for polymerization.

Actins↗
PubMed1990

The heterogeneity of the polymeric intracellular hemoglobin of Glycera dibranchiata and the cDNA-derived amino acid sequence of one component.

The erythrocytes of the marine polychaete Glycera dibranchiata contain a number of different, single-chain hemoglobins, some of which self-associate into a 'polymeric' fraction. An oligodeoxynucleotide probe was synthesized based on partial amino acid sequences determined by chemical methods, and used to screen a cDNA library constructed from the poly(A+)mRNA of Glycera erythrocytes (Simons, P.C. and Satterlee, J.D. (1989) Biochemistry 28, 8525-8530). The longest positive inserts found were sequenced using the dideoxy nucleotide chain termination method. One complete clone was obtained: clone 5A, 816 bases long, contained 59 bases of 5'-untranslated RNA, an open reading frame of 441 bases coding for 147 amino acids and a 3'-untranslated region of 316 bases. The derived amino acid sequence of Glycera globin P1 was in agreement with the partial amino acid sequences obtained by chemical methods. Three additional inserts obtained in the screening were also sequenced: the inferred amino acid sequences proved to be partial globin sequences which were different from each other and from the sequence of P1. Thus, the 'polymeric' fraction of the intracellular hemoglobin of Glycera probably consists of at least four different globin chains much like the 'monomeric' fraction. Comparison of the 'polymeric' sequence with the two known 'monomeric' sequences, M-II and M-IV, shows that they share 54 identical residues. At 74 positions, the identical residues in M-II and M-IV differ from the corresponding residue in P1, including at E-7, where P1 has a distal His, in contrast to Leu in M-II and M-IV. The alignment of Bashford et al. ((1987) J. Mol. Biol. 196, 199-216) and their templates were used to examine the principal differences between the two types of Glycera globin sequences. They appear to consist of uncommon surface amino acid residues at positions C6 (Phe vs. Ala), E10 (Val vs. Lys), E17 (Lys vs. Val), G1 (Arg vs. Lys), G10 (Met vs. Ala) and H5 (Arg vs. Lys). One or more of these residues could be responsible for the self-association exhibited by the 'polymeric' Glycera globins.

Amino Acid Sequence↗
PubMed1987

Actin polymerization modifies stimulus-oxidase coupling in rat neutrophils.

Oxidase activity in rat neutrophils was monitored by oxygen consumption rate and luminol-dependent chemiluminescence. Two agents which inhibit actin polymerization, cytochalasin B and dihydrocytochalasin B, produced a marked enhancement (up to 10-fold) of oxidase activation induced by two Ca2+-dependent stimuli, chemotactic peptide and ionophore A23187. In contrast, activation by the calcium-independent stimulus, phorbol myristate acetate, was unaffected by these agents. Other agents that interact with the cytoskeleton, phalloidin and colchicine have no effect on activation by any stimulus tested. The effect of cytochalasin B, when added after stimulation by chemotactic peptide, was transient with t0.5 approx. 10 s. Similarly, the degree of actin polymerization following stimulation by chemotactic peptide was transient, decaying with a t0.5 of approx. 10 s. The half-maximal concentration of cytochalasin B for inhibition of actin polymerization was similar to that for enhancement of oxidase activation. It was concluded, therefore, that the intracellular Ca2+ rise in rat neutrophils that accompanies stimulation by chemotactic peptide affects actin polymerization in a manner that modifies oxidase activation.

Actins↗