Variable tinted spectacle lenses: a comparison of aesthetics and visual preference.

PURPOSE: To determine the correlation between the aesthetics of lens tints preferred for cosmesis and lens tints preferred for viewing. METHODS: Thirty-five subjects (mean age: 25; 49% male, 51% female) with no significant ocular pathology participated in the study. Median visual acuity was 20/20. Color vision testing was performed on each subject using Ishihara plates, and those with abnormal scores were excluded from the study. Subjects were shown nine pre-selected tinted lenses (50% transmittance) of variable wavelengths. These lenses were mounted on two separate color backgrounds, one white and the other approximating their skin tone. Subjects were asked to choose from each background which tinted lens they would most prefer to wear and which lens they would least prefer to wear. The subjects were then shown a series of eight pictures (four nature photographs and four paintings) with different dominant wavelengths. Subjects were asked to grade the aesthetic effect of a clear lens and each of the nine tinted lenses on the appearance of the pictures. Chromaticity coordinates were calculated for each lens and picture. RESULTS: The blue lens was the most frequently chosen preferred lens to wear, followed by green, purple, and gray. The least preferred lenses were yellow, brown, and pink. For viewing the nature photographs, the clear lens was preferred over any of the tinted lenses. For viewing the paintings, the purple lens was most preferred. The yellow lens was least preferred for both photographs and paintings. CONCLUSIONS: Younger individuals with no significant ocular pathology preferred viewing both nature photographs and paintings through tinted lenses that did not, or only slightly, altered the chromaticity of the image. Whereas a clear lens was favored over the tinted lenses for viewing the photographs, some tinted lenses (purple and pink) were preferred for viewing paintings. There was no correlation between the most favored lens tint chosen based purely on cosmesis and the most favored lens tint based on viewing preference. However, the least preferred lens tint for cosmesis and viewing was yellow.

Hirudin reduces tissue factor expression in neointima after balloon injury in rabbit femoral and porcine coronary arteries.

BACKGROUND: Tissue factor (TF) is a transmembrane glycoprotein that, after binding to factor VII/VIIa, initiates the extrinsic coagulation pathway, resulting in thrombin generation and its sequelae. Thrombin has been shown to induce TF mRNA in endothelium, monocytes, and smooth muscle cells, further perpetuating the thrombogenic cycle. This study was designed to determine the effect of specific inhibition of thrombin by recombinant hirudin (r-hirudin) on TF distribution after balloon angioplasty in the cholesterol-fed rabbit femoral artery and porcine coronary artery models. METHODS AND RESULTS: Thirty-five femoral arteries from 32 cholesterol-fed New Zealand White rabbits and 84 coronary arteries from 55 Yorkshire-Albino swine were studied by use of a recently developed in situ method of TF localization based on digoxigenin labeling of recombinant factor VIIa (Dig-VIIa), with correlative studies of TF immunoreactivity by use of anti-rabbit (AP-1) or anti-human (sTF) antibodies. At sites of balloon angioplasty in rabbit femoral or pig coronary arteries (double or single injury), TF-antibody and Dig-VIIa staining were noted in association with endothelial cells, smooth muscle cells, and foam cells and within the fibrous tissue matrix primarily of the adventitia and neointima. Staining was significantly greater after balloon angioplasty than in vessels that had not undergone angioplasty but was similar after single and double balloon injury. Animals treated with r-hirudin (rabbits, 1 mg/kg bolus plus 2-hour infusion; pigs, 1 mg/kg bolus plus 0.7 mg x kg(-1) x d(-1) infusion for 14 days with implantable pump) had diminished TF-antibody and Dig-VIIa staining 28 days after balloon angioplasty compared with controls (bolus heparin only). This effect was more prominent on the neointima and was more striking in the porcine than the rabbit model. CONCLUSIONS: TF expression, persistent 1 month after balloon angioplasty in rabbit femoral arteries and porcine coronary arteries, is attenuated by specific thrombin inhibition with hirudin. These results suggest that thrombin inhibition, in addition to its effect on acute thrombus formation and its effect on luminal narrowing by plaque in experimental animals, may result in a prolonged reduction in thrombogenicity of the restenotic plaque through this effect on TF expression.

Relationship between antibacterial activity and porin binding of lactoferrin in Escherichia coli and Salmonella typhimurium.

The effect of lactoferrin (Lf) on bacterial growth was tested by measuring conductance changes in the cultivation media by using a Malthus-AT system and was compared with the magnitude of 125I-labeled Lf binding in 15 clinical isolates of Escherichia coli. The binding property was inversely related to the change in bacterial metabolic rate (r = 0.91) and was directly related to the degree of bacteriostasis (r = 0.79). The magnitude of Lf-bacterium interaction showed no correlation with the MIC of Lf. In certain strains, Lf at supraoptimal levels reduced the bacteriostatic effect. Thus, the Lf concentration in the growth media was critical for the antibacterial effect. The cell envelopes of Salmonella typhimurium 395MS with smooth lipopolysaccharide (LPS) and its five isogenic rough mutants revealed 38-kDa porin proteins as peroxidase-labeled-Lf-reactive components in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blot (ligand blot) analysis. However, in the whole cell binding assay, parent strain 395MS demonstrated a very low interaction with 125I-Lf. On the other hand, Lf interaction gradually increased in correspondence with the decrease in LPS polysaccharide moiety in the isogenic rough mutants. Conductance measurement studies revealed that the low-level-Lf-binding (low-Lf-binding) strain 395MS with smooth LPS was relatively insusceptible to Lf, while the high-Lf-binding mutant Rd was more susceptible to Lf. These data suggested a correlation between Lf binding to porins and the Lf-mediated antimicrobial effect. The polysaccharide moiety of LPS shielded porins from the Lf interaction and concomitantly decreased the antibacterial effect.

Specific binding of lactoferrin to Escherichia coli isolated from human intestinal infections.

The degrees of human lactoferrin (HLf) and bovine lactoferrin (BLf) binding in 169 Escherichia coli strains isolated from human intestinal infections, and in an additional 68 strains isolated from healthy individuals, were examined in a 125I-labelled protein binding assay. The binding was expressed as a percentage calculated from the total labelled ligand added to bacteria. The HLf and BLf binding to E. coli was in the range 3.7 to 73.4% and 4.8 to 61.6%, respectively. Enterotoxigenic strains demonstrated a significantly higher HLf binding (median = 19%) than enteropathogenic, enteroinvasive, enterohaemorrhagic strains or normal intestinal E. coli isolates (medians 6 to 9). Enteropathogenic strains belonging to serotypes O44 and O127 demonstrated significantly higher HLf binding compared to O26, O55, O111, O119 and O126. No significant differences in the degree of HLf or BLf binding were found between aerobactin-producing and non-producing strains. The interaction was further characterized in a high Lf-binding EPEC strain, E34663 (serotype O127). The binding was stable in the pH range 4.0 to 7.5, did not dissociate in the presence of 2M NaCl or 2M urea, and reached saturation within two h. Unlabelled HLf and BLf displaced the 125I-HLf binding to E34663 in a dose-dependent manner. Apo- and iron-saturated forms of Lf demonstrated similar binding to E34663. Among various unlabelled subepithelial matrix proteins and carbohydrates tested (in 10(4)-fold excess) only fibronectin and fibrinogen caused a moderate inhibition of 125I-HLf binding. According to Scatchard plot analysis, 5,400 HLf-binding sites/cell, with an affinity constant (Ka) of 1.4 x 10(-7) M, were estimated in strain E34663. These data establish the presence of a specific Lf-binding mechanism in E. coli.

Specific binding of lactoferrin to Aeromonas hydrophila.

The interaction of lactoferrin (Lf) with Aeromonas hydrophila (n = 28) was tested in a 125I-labeled protein-binding assay. The mean per cent binding values for human Lf (HLf) and bovine Lf (BLf) were 13.4 +/- 2.0 (SEM), and 17.5 +/- 2.7 (SEM), respectively. The Lf binding was characterized in type strain A. hydrophila subsp. hydrophila CCUG 14551. The HLf and BLf binding reached a complete saturation within 2 h. Unlabeled HLf and BLf displaced 125I-HLf binding in a dose-dependent manner, and more effectively by the heterologous (1 microgram for 50% inhibition) than the homologous (10 micrograms for 50% inhibition) ligand. Apo- and holo-forms of HLf and BLf both inhibited more than 80%, while mucin caused approx. 50% inhibition of the HLf binding. Various other proteins (including transferrin) or carbohydrates did not block the binding. Two HLf-binding proteins with an estimated molecular masses of 40 kDa and 30 kDa were identified in a boiled-cell-envelope preparation, while the unboiled cell envelope demonstrated a short-ladder pattern at the top of the separating gel and a second band at approx. 60 kDa position. These data establish a specific interaction of Lf and the Lf-binding proteins seem to be porins in A. hydrophila.