Therapeutic effect of phenolic compounds isolated from <Emphasis Type="Italic">Rhododendron ungernii</Emphasis> leaves

The sum of phenolic compounds was obtained from the leaves of Caucasian endemic plant Rhododendron ungernii (Trautv.) in the amount of 7%. The extract contains flavonoids, catechins, and anthocyanidins, in particular, quercetin, isoquercetin, quercitrin, hyperin, rutin, (+)-catechin, (−)-epicatechin, (+)-gallocatechin, and leucoanthocyanidins. The sum of phenolic compounds from Rhododendron ungernii completely inhibits Herpes simplex virus reproduction in a bioassay. A new medicinal preparation (Rhodopes) in the form of a 5% ointment was created on the basis of this extract and tested under clinical conditions at a dental clinic and three other specialized medical departments. The results showed a high therapeutic efficacy: Rhodopes favorably influenced the state of patients and caused neither mucosa irritation nor allergic and other adverse reactions. Rhodopes has received State Registration and is recommended for the treatment of all forms of herpetic disorders. __________ Translated from Khimiko-Farmatsevticheskii Zhurnal, Vol. 41, No. 1, pp. 10–13, January, 2007.     

IgE antibodies to protein and mannan antigens of pityrosporum ovale in atopic dermatitis patients

Background Pityrosporum ovale is a common saprophyte on the skin capable of inducing IgE antibody production in atopic dermatitis (AD) patients. Allergens ofP. ovale have been examined in several studies, but consensus on them is lacking. Objective This study was carried out to obtain more information about the IgE antibody response against P. ovale. including niunnun. Methods Sera from 64 AD patients and 10 healthy controls were analysed with immuno-blotting and the nitrocellulose radio allergosorbent test (RAST) method specifically developed to detect antimannan P. ovale IgE antibodies. Results In immunoblotting a total of 39 different IgE stained protein bands were seen. A high molecular weight staining was also seen especially in patients who displayed elevated mannan P. ovale RAST values. The most commonly stained protein bands in immunoblotting were 9 and 96 kD bands with antibodies in 73 and 65% of AD patients who had been positive in commercial P. orbiculare RAST with total serum IgE less than 4000 kU/I. Mannan RAST appeared positive in 77% of them. Positive immunoblotting to either of these bands was seen in 90% and, if added with staining with ihe 20 kD band, in 100% of these AD patients. A comhination of 9 kD IgE staining and mannan P. ovale RAST was positive in 92% of the patients and % kD and mannan P. ovale RAST in 85% of the patients. Conclusion It is evident that P. ovale has several allergens, the 9. 96 and 20 kD regions being the most important. According to our results mannan is also an important allegen of P. ovale     

Ocular findings in familial adenomatous polyposis

Background: Retinal pigment epithelium (RPE)lesions are predictive congenital phenotypic markersfor familial adenomatous polyposis (FAP). Thisprospective screening study aims at assessing theincidence and significance of these lesions in FAPpatients and their family members.Methods: Sixty-two members from three familiesincluding five patients with the diagnosis of FAP havebeen ophthalmologically surveyed. All RPE lesions weredocumented with fundus photography and fluoresceinangiography was performed in 13 subjects.Sigmoidoscopy and/or radiological examination wereperformed annually in 9 family members with typicalRPE lesions during 4 years to allow early diagnosis ofFAP.Results: Typical RPE lesions were present infive FAP patients and 15 family members.Telangiectatic dilatations in the retinal peripherywith small dot-like hemorrhages were detected in 6subjects from 3 families These lesions wereparticularly evident on fluorescein angiography.Annual colon analysis showed polyps in 3 out of 9subjects who were positive for RPE lesions.Conclusion: RPE lesions are valuable as aclinical marker in predicting FAP. The co-existingperipheral vascular alterations which have not beenreported before, are probably related to FAP.     

Non-invasive temperature imaging of muscles with magnetic resonance imaging using spin-echo sequences

The application of spin-echo magnetic resonance imaging sequences on non-invasive temperature imaging for temperature mapping of human limbs is investigated. In an in vitro expriment performed on a meat sample, the equilibrium magnetisation P and the spin-lattice relaxation time T₁ are calculated from the values for the repetition time TR and the signal intensities obtained by a spin-echo sequence at different tissue temperatures tures as measured by a fibre-optic probe. T₁ is linearly correlated to the tissue temperature, and P is linearly correlated to the reciprocal value of the absolute temperature. Both effects, taken together, lead to a non-linear dependency of the signal intensity on temperature. Therefore a TR leading to maximum temperature dependency of the signal intensity is calculated and used in the futher experiments. In the in vivo experiments, the lower legs of two volunteers are cooled from outside. Images are acquired with a spin-echo sequence (1.5T, TR=1200 ms, TE=10 ms). A rise in signal intensity in the muscle with falling skin temperature is observed, particularly in more peripheral muscle layers. This study shows that spin-echo sequences can be used to monitor temperature changes and temperature differences in living muscle tissue.     

Back pain in in-vitro fertilized and spontaneous pregnancies

The influence of ovarian stimulation in in-vitro fertilization (IVF) on the prevalence of back pain with onset during pregnancy was studied in 31 women who became pregnant after IVF treatment and compared with that of 200 spontaneously pregnant women. A two times higher prevalence rate of sacral pain in late pregnancy was reported among IVF pregnant women (P < 0.0001), as well as a significantly higher prevalence rate of positive results of pelvic pain provocation tests performed in late pregnancy (0.0001 < or = P < or = 0.015), as compared with that of the spontaneously pregnant women. Among the IVF pregnant women, there was a significant positive correlation between relaxin concentrations in early pregnancy and the outcome of pelvic pain provocation tests (0.44 < or = r < or = 0.51, P < 0.05). In addition, the serum relaxin concentration was the factor that best explained differences in sacral pain prevalence. When the influence of serum relaxin concentration on back pain prevalence was taken into account, women carrying multiple pregnancies had no more pain than women carrying singletons, and IVF pregnant women had no more pain than spontaneously pregnant women. These results support the hypothesis that relaxin is involved in the generation of pelvic pain in pregnant women.      

Polymerization of human prion peptide HuPrP 106–126 to amyloid in nucleic acid solution

Summary.  The human prion peptide PrP106–126 polymerizes in the presence of DNA both in its circular and linearized forms under solution conditions where the peptide alone does not polymerize. The polymerization process has been monitored by the increase in the fluorescence of anilino naphthalene sulfonic dye which detects the availability of the hydrophobic surface(s) in the aggregate as a consequence of polymerization. The polymerization is a nucleation dependent phenomenon as is evidenced from an existence of a lag period before the onset of the polymerization and a strong dependence of the polymerization on the prion peptide concentrations. The reaction is dependent on the pH as seen from rapid polymerization at pH 5 compared to the reaction at neutral pH where no polymerization is observed after a relatively long period of incubation. The polymer has been characterized as amyloid by using new absorbing and emitting species resulting from the interaction of the polymer with the amyloid specific fluorescent dye, Thioflavine S. This is probably the first demonstration that an endogenous macromolecule can influence the polymerization of a prion peptide. We have previously shown that there is a conformational change in the nucleic acid as a consequence of this interaction. This prion peptide is considered as a model to understand prion diseases as is evidenced from its toxicity towards primary brain cells in culture. The peptide encompasses one of the important amyloidogenic regions of the normal cellular prion protein. Demonstration of nucleic acid induced polymerization of the normal and scrapie prion isoforms accompanying a change in the nucleic acid conformation can establish a possible role of nucleic acid in prion disease. Received January 8, 1997 Accepted March 4, 1998     

Lactoferrin Interaction with Actinobacillus actinomycetemcomitans

The interaction of lactoferrin with Actinobacillus actinomycetemcomitans was examined in a ¹²⁵I-labeled protein binding assay. The binding of human and bovine lactoferrins reached maximum within 1 h. Lactoferrin binding to the bacterium was pH-dependent and reversible. Scatchard analysis indicated the existence of two different types of binding sites on the bacterium, one with a high affinity constant k_α=8.8×10⁻⁷ M) and the other with a low one (k_α=1.8×10⁻⁶ M). Bacteria in the exponential phase of growth showed higher binding than cells in the stationary phase. Bacteria grown in medium containing serum and/or lysed erythrocytes bound lactoferrin to a lesser extent. Heat-inactivated serum, lysed erythrocytes and other proteins such as mucin and laminin inhibited lactoferrin binding to A. actinomycetemcomitans in a competitive binding assay. Sodium dodecyl sulfate polyacrylamidegel electrophoresis and Western blot analysis of the cell envelope as well as the outer membrane of A. actinomycetemcomitans revealed lactoferrin-reactive protein bands at 29 kDa and 16.5 kDa. The 29-kDa band displayed a heat-modifiable lactoferrin-reactive form with a molecular weight of 34 kDa. Neither proteinase K-treated cell envelope nor lipopolysaccharide of this bacterium showed reactivity with lactoferrin. These data suggests a specific interaction of lactoferrin with outer membrane proteins of A. actinomycetemcomitans .