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Biomedical subjects

B Endres

Publications and source records attributed to B Endres.

13 recordsLinked to original sources

Bulk glasses and ultrahard nanoceramics based on alumina and rare-earth oxides.

Although often regarded as a network-former in conventional silicate glasses, Al(2)O(3) alone cannot be obtained as a bulk glass. Until now, glasses comprising continuously linked [AlO(x)] polyhedra have been prepared in only a few systems under very fast cooling conditions, which limits their dimensions to a few millimetres. Yet it is desirable to prepare bulk, or monolithic, alumina-rich glasses, with the prospect of superior mechanical, chemical and optical properties. Here we report a novel process for preparing very-high-alumina glasses and nanoscale glass-ceramics. Fully dense bulk articles in net shape are obtained through viscous sintering of glass microbeads. Additional heat treatment of the consolidated glasses leads to fully crystallized transparent glass-converted nanoceramics with a hardness similar to that of alumina. This method avoids the impracticably high applied pressures (more than 1 GPa) that have been required in most cases to prepare nanocrystalline ceramics by sintering, owing to the concurrent nature of densification and grain growth under pressureless conditions. The reported techniques can be extended to form glasses and nanoceramics in other oxide systems that do not include a conventional glass-forming component.

Journal Article↗

[Cycling with a visual handicap].

PURPOSE OF THE STUDY: To examine bicycling habits of visually handicapped people in order to learn about the visual requirements. MATERIAL AND METHODS: Survey of patients (age range: 14-60 years) suffering from macular or tapetoretinal degeneration with no additional relevant handicap using a questionnaire. RESULTS: A total of 232 questionnaires were returned (62% of the questionnaires received by the participants). The results showed that if visual acuity dropped below 0.1, only 15% of the patients were able to ride a bicycle without accidents or near-accidents. This percentage increased for higher acuities between 33% (<0.2 > or = 0.1) and 67% (> or = 0.2 < or = 0.4). For visual field diameters <60 degrees and > or = 20 degrees approximately 18% were able to ride a bicycle safely and only 8% if the visual field diameter was below 20 degrees. For visual fields larger than 60 degrees diameter approximately 40% were able to ride a bicycle without problems. With a central scotoma of more than 10 degrees diameter only 21% of the patients could cycle safely, whereas with a central scotoma of 10 degrees and less this percentage increased to 47%. CONCLUSIONS: A visual acuity of less than 0.1 is not sufficient to ride a bicycle, and a visual acuity of less than 0.2 leads to a higher accident rate. A visual field diameter of less than 60 degrees or a central scotoma of more than 10 degrees diameter for the vast majority of patients does not allow safe cycling

Accidents, Traffic↗

26-Hydroxylation of 1alpha,25-dihydroxyvitamin D3 does not occur under physiological conditions.

The 26-hydroxylation of 1alpha,25-dihydroxyvitamin D3 in rats in vitro and in vivo was studied under physiological conditions. Incubation of 1alpha,25-dihydroxy-[26,27-3H]vitamin D3 with rat kidney or rat liver homogenate showed formation of a metabolite that was identified as 1alpha,25(S),26-trihydroxy-[26,27-3H]vitamin D3 by comigration on three different HPLC systems and a periodate cleavage reaction. This metabolite was not generated by hydroxylation of 1alpha,25-dihydroxy-[26,27-3H]vitamin D3 itself but by an enzymatic conversion of a precursor that was formed nonenzymatically in substantial amounts upon storage of 1alpha,25-dihydroxy-[26,27-3H]vitamin D3 in ethanol at -20 degrees C under argon for more than three weeks. An in vivo metabolism study in rats dosed with a physiological dose of 1alpha,25-dihydroxy-[26,27-3H]vitamin D3 confirmed the absence of 26-hydroxylation of the hormone. As expected at 6 h postinjection of purified 1alpha,25-dihydroxy-[26,27-3H]vitamin D3, 1alpha,24(R),25-trihydroxy-[26,27-3H]vitamin D3, as well as traces of (23S,25R)-1alpha,25-dihydroxy-[3H]vitamin D3-lactone were detected and identified on straight phase and reverse phase HPLC in serum, kidney, and liver.

Animals↗

Metabolism of 1alpha,25-dihydroxyvitamin D(3) in vitamin D receptor-ablated mice in vivo.

The metabolism of 1alpha,25-dihydroxyvitamin D(3) was studied in vitamin D receptor-ablated mice following the administration of a physiological dose of 1alpha,25-dihydroxy-[26,27-(3)H]vitamin D(3). The degradation of 1alpha,25-dihydroxy-[26,27-(3)H]vitamin D(3) in the vitamin D receptor null mutant mice was substantially reduced compared to the wild-type control mice. At 24 h postadministration of radiolabeled 1alpha,25-dihydroxyvitamin D(3) more than 50% of the radioactivity was recovered unmetabolized, whereas in wild-type mice nearly all of the 1alpha,25-dihydroxy-[26,27-(3)H]vitamin D(3) was degraded. In wild-type mice three polar metabolites other than 1alpha,25-dihydroxyvitamin D(3) were detected and identified on straight-phase and reverse-phase high-performance liquid chromatography as 1alpha,24(R),25-trihydroxy-[26,27-(3)H]vitamin D(3), 1alpha,25(S),26-trihydroxy-[26,27-(3)H]vitamin D(3), and (23S, 25R)-1alpha,25-dihydroxy-[(3)H]vitamin D(3)-26,23-lactone. Only one metabolite was detected in the plasma and kidneys of vitamin D receptor null mutant mice at 3 h following an intrajugular dose of 1alpha,25-dihydroxy-[26,27-(3)H]vitamin D(3). This metabolite was clearly identified as 1alpha,25(S),26-trihydroxy-[26,27-(3)H]vitamin D(3) by comigration on two HPLC systems and periodate cleavage reaction. At 6, 12, and 24 h postinjection 1alpha,24(R), 25-trihydroxy-[26,27-(3)H]vitamin D(3) was also detected at low levels in plasma, kidneys, and liver of some but not all mutant mice. The presence of 25-hydroxyvitamin D(3)-24-hydroxylase mRNA in the kidneys of these vitamin D receptor null mutant mice was confirmed by ribonuclease protection assay.

Animal Nutritional Physiological Phenomena↗

7-Azabenzimidazolylcobamide and 5,6-dimethyl-7-azabenzimidazolylcobamide, new vitamin B12-analogs synthesized from 4(5)-aminoimidazole by Eubacterium limosum.

In anaerobic bacteria, glycine, formate, and the amide-N of glutamine are building blocks for the biosynthesis of the imidazole moiety of the vitamin B12-base 5,6-dimethylbenzimidazole. These building blocks are also used for the biosynthesis of the imidazole moiety of purine bases. Therefore we tested 4(5)-aminoimidazole, the base moiety of the purine nucleotide precursor 5-aminoimidazole ribonucleotide, for its putative function as precursor of 5,6-dimethylbenzimidazole. The anaerobic vitamin B12-producer Eubacterium limosum, grown in the presence of [2-13C]4(5)-aminoimidazole, synthesized nonlabeled vitamin B12, but also [2-13C]7-azabenzimidazolylcobamide and [2-13C]5,6-dimethyl-7-azabenzimidazolylcobamide. [2-13C]limidazole was used by E. limosum to form [2-13C]imidazolylcobamide. Simultaneously nonlabeled vitamin B12 was synthesized. This shows that 4(5)-aminoimidazole and imidazole are not intermediates in the biosynthesis of 5,6-dimethylbenzimidazole. However, 4(5)-aminoimidazole has obviously a structure similar to the structure of an as yet unknown precursor of the vitamin B12-base, and is therefore transformed into the aza analogs. In order to prepare a reference compound 4(5)-azabenzimidazole was added to a culture of Propionibacterium shermanii and to a culture of E. limosum, P. shermanil transformed this base mainly to 4-azabenzimidazolylcobamide, as determined by 1H NMR-spectroscopy (NOE experiment). In contrast E. limosum produced mainly 7-azabenzimidazolylcobamide. The reason for this difference is discussed.

Anaerobiosis↗

Biosynthesis of vitamin B12 in anaerobic bacteria. Transformation of 5-hydroxybenzimidazole and 5-hydroxy-6-methylbenzimidazole into 5,6-dimethylbenzimidazole in Eubacterium limosum.

Eubacterium limosum transformed [2-13C]5-hydroxybenzimidazole not only into [2-13C]5-hydroxybenzimidazolylcobamide, but also into [2-13C]5-methoxy-6-methylbenzimidazolylcobamide and into [2-13C]5,6-dimethylbenzimidazolylcobamide (vitamin B12). [2-13C]5-Hydroxy-6-methyl-benzimidazole was used by this bacterium to form [2-13C]5-hydroxy-6-methylbenzimidazolyl-cobamide, [2-13C]5-methoxy-6-methylbenzimidazolylcobamide and [2-13C]5,6-dimethylbenzimidazolylcobamide. The 1H-NMR spectrum of the 5,6-dimethylbenzimidazole isolated from the 13C-labeled vitamin B12 preparations revealed that the externally added bases had been transformed into the vitamin B12 base almost without dilution of the label. This suggests that 5-hydroxybenzimidazole and 5-hydroxy-6-methylbenzimidazole are precursors of 5,6-dimethylbenzimidazole. On the basis of these results, a hypothetical scheme for the biosynthesis of 5,6-dimethylbenzimidazole via 5-hydroxybenzimidazole and 5-hydroxy-6-methylbenzimidazole is discussed. This scheme can also explain the formation of the other benzimidazole bases found in natural vitamin B12 analogs.

Benzimidazoles↗

Unresponsiveness to experimental allergic encephalomyelitis in Lewis rats pretreated with complete Freund's adjuvant.

A single injection of complete Freund's adjuvant blended with aluminum hydroxide gel (ALU-CFA) was successfully used to prevent clinical as well as histologic experimental allergic encephalomyelitis (EAE) in Lewis rats for more than 330 days. Adjuvant preparations with Mycobacterium tuberculosis were more potent than those with Mycobacterium butyricum. Neither the removal of the ALU-CFA inoculum nor a splenectomy 1 month after immunization arrested the adjuvant induced unresponsiveness. However cyclophosphamide restored responsiveness in more than half of the treated animals when applied 2 days before the encephalitogenic challenge at a dose of 20 mg/kg. Passive EAE was not prevented by the ALU-CFA pretreatment. The disease was induced by the transfer of 4 X 10(6) T lymphocytes of a cell line reactive against myelin basic protein. This indicates that the adjuvant prevents EAE at the inductive rather than at the effector phase of the autoimmune response.

Age Factors↗

The influence of trauma from occlusion on the bacterial repopulation of periodontal pockets in dogs.

Pockets were surgically created in the two upper external incisors of four beagle dogs, and a copper band adapted to prevent reattachment. After 4 weeks the copper bands were removed, the teeth scaled and root-planed and crowns placed on both experimental teeth in such a way that one of them was forced bucally when the teeth occluded. An orthodontic appliance anchored in bands cemented to the cuspid teeth brought the tooth back to its original position when disclusion occurred. Experimental time was 12 weeks. Clinical indices and bacterial samples for darkfield examination were taken at baseline and weekly thereafter. The dogs were fed a diet that favored plaque accumulation and no oral hygiene was performed. Surgically created pockets initially became populated by cocci (65%-75%) and small amounts of motile bacteria (12%-15%) including 3% to 4% spirochetes. In 4 weeks the percentage of cocci declined steadily (42%-45%) and motile bacteria increased to 37% to 43% with spirochetes representing 24% to 27%. After scaling and root planing, the number of cocci increased again and motile bacteria declined although the baseline values were not reached. This decline persisted for 2 weeks after scaling. Repopulation of the pocket in traumatized and nontraumatized teeth followed the same initial pattern, taking again 5 weeks to return to prescaling levels. No difference was found between traumatized and nontraumatized teeth. Clinical measurements, however, revealed a statistically greater loss of attachment in traumatized teeth as compared with nontraumatized teeth.

Animals↗

The effect of metronidazole on human periodontal disease. A clinical and bacteriological study.

Fifteen female subjects undergoing treatment for nonspecific vaginitis with metronidazole 250 mg q.i.d. for 7 days were studied. Clinical and microbiological evaluations were carried out initially and at 2 and 4 weeks. The following parameters were measured in two quadrants: plaque index, sulcular bleeding index, pocket depth, attachment level and amount of gingival fluid. Dark field microscopy was used to quantitate the plaque constituents. One quadrant was subjected to root planing at the initial visit; the other quadrant received no therapy. No oral hygiene instructions were given. All the clinical parameters were significantly reduced in all areas. Gingival fluid, sulcular bleeding index and pocket depth showed greater improvement in the root-planed quadrant compared to the nonroot-planed quadrant. Dark field microscopy showed decreases in fusiforms, curved rods and spirochetes in all areas with a concomitant increase in cocci. The root-planed quadrant showed no significant differences in microbiological aspects when compared to the nonplaned quadrant. Clinically, metronidazole therapy resulted in improvement of periodontal status with some additional but small enhancement due to root planing. Microbiologically, metronidazole dramatically changed the quality of plaque with no supplemental effect when root planing was added.

Adult↗

Synthesis of 4-aza-5,6-dimethylbenzimidazole and biosynthetic preparation of 4- and 7-aza-5,6-dimethylbenzimidazolylcobamide.

We report on the preparation of 4-aza-5,6-dimethylbenzimidazolylcobamide and 5,6-dimethyl-7-azabenzimidazolylcobamide. These vitamin B12-analogs were required as reference compounds for comparison with a corrinoid previously isolated in small amounts for Eubacterium limosum grown in the presence of 4(5)-aminoimidazole. 4(7)-Aza-5,6-dimethylbenzimidazole was synthesized from N-1-benzyl-4-nitroimidazole which was reduced to N-1-benzyl-4-aminoimidazole and condensed with 1-dimethylamino-2-methylbutan-3-one to yield N-1-benzyl-4-aza-5,6-dimethylbenzimidazole. The benzyl group of this compound was split off by catalytic hydrogenation to form 4(7)-aza-5,6-dimethylbenzimidazole. 4(7)-Aza-5,6-dimethylbenzimidazole was transformed by a growing culture of Propionibacterium shermanii into 4-aza-5,6-dimethylbenzimidazolylcobamide and 5,6-dimethyl-7-azabenzimidazolylcobamide. Both vitamin B12-analogs were almost as active as Vitamin B12 in a growth test with the vitamin B12-dependent Escherichia coli-mutant DSM 4261.

Cobamides↗