Activation of the kallikrein-kinin system in hemodialysis: role of membrane electronegativity, blood dilution, and pH. (1/1060)

BACKGROUND: The kallikrein-kinin system activation by contact with a negatively charged surface has been promulgated to be responsible for hypersensitivity reactions. However, to explain the low frequency and heterogeneity of hypersensitivity reactions, we hypothesized that not only the electronegativity of the membrane, but also other physicochemical parameters could influence the activation of the contact phase system of plasma assessed by the measurement of kallikrein activity and bradykinin concentration. METHODS: Plasma kallikrein activity using chromogenic substrate (S2302) and plasma bradykinin concentration (enzyme immuno assay) were measured during the perfusion of human plasma (2.5 ml/min) through minidialyzers mounted with six different membranes [polyacrylonitrile (PAN) from Asahi (PANDX) and from Hospal (AN69), polymethylmethacrylate (PMMA) from Toray, cellulose triacetate (CT) from Baxter, cuprophane (CUP) from Akzo and polysulfone (PS) from Fresenius]. RESULTS: A direct relationship was shown between the electronegativity of the membrane assessed by its zeta potential and the activation of plasma during the first five minutes of plasma circulation. With the AN69 membrane, the detection of a kallikrein activity in diluted plasma but not in undiluted samples confirmed the importance of a protease-antiprotease imbalance leading to bradykinin release during the first five minutes of dialysis. With PAN membranes, the use of citrated versus heparinized plasma and the use of various rinsing solutions clearly show a dramatic effect of pH on the kallikrein activity and the bradykinin concentration measured in plasma. Finally, increasing the zeta potential of the membrane leads to a significant increase of plasma kallikrein activity and bradykinin concentration. CONCLUSIONS: Our in vitro experimental approach evidences the importance of the control of these physicochemical factors to decrease the activation of the contact system.  (+info)

Intravitreous transplantation of encapsulated fibroblasts secreting the human fibroblast growth factor 2 delays photoreceptor cell degeneration in Royal College of Surgeons rats. (2/1060)

We developed an experimental approach with genetically engineered and encapsulated mouse NIH 3T3 fibroblasts to delay the progressive degeneration of photoreceptor cells in dark-eyed Royal College of Surgeons rats. These xenogeneic fibroblasts can survive in 1. 5-mm-long microcapsules made of the biocompatible polymer AN69 for at least 90 days under in vitro and in vivo conditions because of their stable transfection with the gene for the 18-kDa form of the human basic fibroblast growth factor (hFGF-2). Furthermore, when transferred surgically into the vitreous cavity of 21-day-old Royal College of Surgeons rats, the microencapsulated hFGF-2-secreting fibroblasts provoked a local delay of photoreceptor cell degeneration, as seen at 45 days and 90 days after transplantation. This effect was limited to 2.08 mm2 (45 days) and 0.95 mm2 (90 days) of the retinal surface. In both untreated eyes and control globes with encapsulated hFGF-2-deficient fibroblasts, the rescued area (of at most 0.08 mm2) was significantly smaller at both time points. Although, in a few ocular globes, surgical trauma induced a reorganization of the retinal cytoarchitecture, neither microcapsule rejection nor hFGF-2-mediated tumor formation were detected in any treated eyes. These findings indicate that encapsulated fibroblasts secreting hFGF-2 or perhaps other agents can be applied as potential therapeutic tools to treat retinal dystrophies.  (+info)

The crystal growth technique--a laboratory evaluation of bond strengths. (3/1060)

An ex vivo study was carried out to determine differences in the bond strengths achieved with brackets placed using a crystal growth technique compared with a conventional acid-etch technique. A solution of 37 per cent phosphoric acid was used for acid-etching and a commercially available polyacrylic acid gel, Crystal-lok for crystal growth. A heavily-filled composite resin was used for all samples to bond brackets to healthy premolar teeth extracted for orthodontic purposes. Polycrystalline ceramic and stainless steel brackets were used and tested to both tensile and shear failure using an Instron Universal Testing machine. The tensile and shear bond strengths were recorded in kgF. In view of difficulties experienced with previous authors using different units to describe their findings, the data were subsequently converted to a range of units in order to facilitate direct comparison. The crystal growth technique produced significantly lower bond strengths than the acid-etch technique for ceramic and stainless steel brackets, both in tensile and shear mode. The tensile bond strength for stainless steel brackets with crystal growth was 2.2 kg compared with 6.01 kg for acid-etch, whilst with ceramic brackets the tensile bond strengths were 3.9 kg for crystal growth and 5.55 kg for acid-etch. The mean shear bond strength for stainless steel brackets with crystal growth was 12.61 kg compared with 21.55 kg for acid-etch, whilst with ceramic brackets the shear bond strengths were 7.93 kg with crystal growth compared with 16.55 kg for acid-tech. These bond strengths were below those previously suggested as clinically acceptable.  (+info)

High resolution detection of mechanical forces exerted by locomoting fibroblasts on the substrate. (4/1060)

We have developed a new approach to detect mechanical forces exerted by locomoting fibroblasts on the substrate. Cells were cultured on elastic, collagen-coated polyacrylamide sheets embedded with 0. 2-micrometer fluorescent beads. Forces exerted by the cell cause deformation of the substrate and displacement of the beads. By recording the position of beads during cell locomotion and after cell removal, we discovered that most forces were radially distributed, switching direction in the anterior region. Deformations near the leading edge were strong, transient, and variable in magnitude, consistent with active local contractions, whereas those in the posterior region were weaker, more stable, and more uniform, consistent with passive resistance. Treatment of cells with cytochalasin D or myosin II inhibitors caused relaxation of the forces, suggesting that they are generated primarily via actin-myosin II interactions; treatment with nocodazole caused no immediate effect on forces. Immunofluorescence indicated that the frontal region of strong deformation contained many vinculin plaques but no apparent concentration of actin or myosin II filaments. Strong mechanical forces in the anterior region, generated by locally activated myosin II and transmitted through vinculin-rich structures, likely play a major role in cell locomotion and in mechanical signaling with the surrounding environment.  (+info)

Adhesion of adhesive resin to dental precious metal alloys. Part I. New precious metal alloys with base metals for resin bonding. (5/1060)

New dental precious metal alloys for resin bonding without alloy surface modification were developed by adding base metals (In, Zn, or Sn). Before this, binary alloys of Au, Ag, Cu, or Pd containing In, Zn, or Sn were studied for water durability and bonding strength with 4-META resin. The adhesion ability of the binary alloys was improved by adding In equivalent to 15% of Au content, Zn equivalent to 20% of Ag content, and In, Zn, or Sn equivalent to 5% of Cu content. There was no addition effect of the base metals on Pd, however 15% of In addition improved adhesion with Pd-based alloys containing equi-atomic % of Cu and Pd. The alloy surfaces were analyzed by XPS and showed that oxides such as In2O3, ZnO, or SnO play an important role in improving the adhesive ability of the alloys.  (+info)

Adhesion of adhesive resin to dental precious metal alloys. Part II. The relationship between surface structure of Au-In alloys and adhesive ability with 4-META resin. (6/1060)

Adhesion of 4-META to Au-In alloy was improved by adding In equivalent to .15% of Au content. On the basis of the results of Au-In alloys analyzed by XPS, the present study investigated the reason why adhesion of the Au-In alloy was improved. The O 1s spectrum could be separated into three oxygen chemical states, In2O3, chemisorbed H2O, and physisorbed H2O. The amount of chemisorbed H2O decreased remarkably with increasing amount of In. It is considered that the poor adhesive ability of the pure gold and alloys containing only small amounts of In was due to the chemisorbed H2O molecules and insufficient indium oxide on the alloy surface. It was established that excellent adhesion requires an oxide with chemical affinity for 4-META to cover at least 50% of the alloy surface.  (+info)

Super pulse CO2 laser for bracket bonding and debonding. (7/1060)

A super pulse and a normal pulse CO2 laser were used to carry out enamel etching and bracket debonding in vitro and in vivo. The shear bond strength of the orthodontic brackets attached to laser-etched and conventional chemically-etched extracted premolars was measured. The pulp cavity temperature was also measured using the same laser irradiation conditions as the shear test. Both super pulse and normal pulse CO2 laser etching resulted in a lower shear bond strength (super pulse: 6.9 +/- 3.4 kg, normal pulse: 9.7 +/- 5.2 kg) than that of chemical etching (15.3 +/- 2.8 kg). Furthermore, the super pulse CO2 laser was able to create debonding at 2 watts within a period of less than 4 seconds (2.9 +/- 0.9 seconds). The super pulse, when irradiating the ceramic brackets from above, during debonding showed a 1.4 degrees C temperature increase in the dental pulp at 2 watts and an increase of 2.1 degrees C at 3 watts. While etching, directly irradiating the enamel surface at 3 watts, the dental pulp showed a temperature increase of 3.5 degrees C. These temperature increases were within the physiologically acceptable limits of the pulp. These results indicate that, in orthodontic treatments, super pulse CO2 laser debonding is more useful than laser etching.  (+info)

Subcellular localization and partial purification of prelamin A endoprotease: an enzyme which catalyzes the conversion of farnesylated prelamin A to mature lamin A. (8/1060)

The nuclear lamina protein, lamin A is produced by proteolytic cleavage of a 74 kDa precursor protein, prelamin A. The conversion of this precursor to mature lamin A is mediated by a specific endoprotease, prelamin A endoprotease. Subnuclear fractionation indicates that the prelamin A endoprotease is localized at the nuclear membrane. The enzyme appears to be an integral membrane protein, as it can only be removed from the nuclear envelope with detergent. It is effectively solubilized by the detergent n-octyl-beta-D-glucopyranoside and can be partially-purified (approximately 1200-fold) by size exclusion and cation exchange (Mono S) chromatography. Prelamin A endoprotease from HeLa cells was eluted from Mono S with 0.3 M sodium chloride as a single peak of activity. SDS-PAGE analysis of this prelamin A endoprotease preparation shows that it contains one major polypeptide at 65 kDa and smaller amounts of a second 68 kDa polypeptide. Inhibition of the enzyme activity in this preparation by specific serine protease inhibitors is consistent with the enzyme being a serine protease.  (+info)

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