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Biomedical subjects

R Welsch

Publications and source records attributed to R Welsch.

10 recordsLinked to original sources
PubMed2004

[Cost-of-illness Study for the Treatment of COPD in Germany].

The present cost-of-illness study is focused on the costs of COPD in Germany. In a pre-study, data on 814 randomly selected patients were collected to achieve reliable figures for the distribution of COPD severity grades and the frequencies of exacerbations. The main study was performed on 321 randomly selected patients from the pre-study. Data on resource use were collected in a face-to-face interview with the respective physicians using the patient records as a basis. Costs associated with resource consumption were weighted with the frequencies of COPD severity grades as assessed in the pre-study to determine the costs of COPD. Annual COPD-related costs per patient were 3,027 from the societal perspective. Main cost components were hospitalisations (26 %), medication (23 %) and early retirement (17 %). Annual COPD-related costs from the perspective of the German health insurance system (GKV) were 1,944 euros per patient.

Cost of Illness↗
PubMed2000

Identification of a novel gene coding for neoxanthin synthase from Solanum tuberosum.

The polymerase chain reaction analysis of potato plants, transformed with capsanthin capsorubin synthase ccs, revealed the presence of a highly related gene. The cloned cDNA showed at the protein level 89.6% identity to CCS. This suggested that the novel enzyme catalyzes a mechanistically similar reaction. Such a reaction is represented by neoxanthin synthase (NXS), forming the xanthophyll neoxanthin, a direct substrate for abscisic acid formation. The function of the novel enzyme could be proven by transient expression in plant protoplasts and high performance liquid chromatography analysis. The cloned NXS was imported in vitro into plastids, the compartment of carotenoid biosynthesis.

Abscisic Acid↗
PubMed2000

Regulation and activation of phytoene synthase, a key enzyme in carotenoid biosynthesis, during photomorphogenesis.

During photomorphogenesis in higher plants, a coordinated increase occurs in the chlorophyll and carotenoid contents. The carotenoid level is under phytochrome control, as reflected by the light regulation of the mRNA level of phytoene synthase (PSY), the first enzyme in the carotenoid biosynthetic pathway. We investigated PSY protein levels, enzymatic activity and topological localization during photomorphogenesis. The results revealed that PSY protein levels and enzymatic activity increase during de-etiolation and that the enzyme is localized at thylakoid membranes in mature chloroplasts. However, under certain light conditions (e.g., far-red light) the increases in PSY mRNA and protein levels are not accompanied by an increase in enzymatic activity. Under those conditions, PSY is localized in the prolamellar body fraction in a mostly enzymatically inactive form. Subsequent illumination of dark-grown and/or in far-red light grown seedlings with white light causes the decay of these structures and a topological relocalization of PSY to developing thylakolds which results in its enzymatic activation. This light-dependent mechanism of enzymatic activation of PSY in carotenoid biosynthesis shares common features with the regulation of the NADPH:protochlorophyllide oxidoreductase, the first light-regulated enzyme in chlorophyll biosynthesis. The mechanism of regulation described here may contribute to ensuring a spatially and temporally coordinated increase in both carotenoid and chlorophyll contents.

Alkyl and Aryl Transferases↗
PubMed1997

Light-dependent regulation of carotenoid biosynthesis occurs at the level of phytoene synthase expression and is mediated by phytochrome in Sinapis alba and Arabidopsis thaliana seedlings.

In chloroplasts, carotenoids are essential pigments involved in photosynthesis. During-photomorphogenesis, a coordinated increase in the amounts of chlorophylls and carotenoids, in conjugation with other components, leads to the formation of a functional photosynthetic apparatus. To investigate the regulation of carotenoid biosynthesis during this process at the molecular level, GGPS, PSY and PDS cDNAs have been cloned from white mustard (Sinapis alba L). GGPS encodes a key enzyme in plastid isoprenoid metabolism, while the products of PSY and PDS catalyse the subsequent steps in carotenoid biosynthesis. Due to the low mRNA levels of the genes involved, the use of a RT-PCR protocol was necessary to measure gene expression during photomorphogenesis. With light, there is an up-regulation of PSY expression, the first gene within the carotenoid biosynthetic pathway, while PDS and GGPS expression levels remain constant. Treatment with different light qualities reveals a phytochrome-mediated regulation of PSY expression in developing white mustard seedlings. To obtain more detailed information on the light-regulation, Arabidopsis thaliana wild-type and phytochrome mutants were utilized. Continuous far-red and red light both increase the expression of PSY in wild-type seedlings, demonstrating that both light-labile and light-stable phytochromes are involved in PSY regulation. The response to far-red light is completely abolished in the phyA mutant, showing that PHYA mediates the increase in PSY transcript levels under these light conditions. In the phyB mutant, the red light response is normal, indicating that PSY expression is not controlled by PHYB but by other light-stable phytochromes. Measurement of chlorophylls and carotenoids under the same light regimes shows that the up-regulation of PSY expression does not necessarily result in an increase of the carotenoid content. Only those light conditions which allow chlorophyll biosynthesis lead to a significant increase of the carotenoid content. Therefore, it is proposed that up-regulation of PSY mRNA levels leads to an increased capacity for the formation of carotenoids. However, this only takes place under light conditions leading to protochlorophyllide photoconversion.

Alkyl and Aryl Transferases↗
PubMed1996

Equipment configuration and procedures: preferences for interventional microtherapy.

Magnetic resonance imaging (MRI), computed tomography, and electron beam tomography scanners are built for radiologic diagnosis. With increasing frequency they are being used in the field of interventional Microtherapy to permit transparent visualization of the therapeutic field. Each of these scanners can be combined with endoscopy, fluoroscopy/digital subtraction angiography, and ultrasound units for hybrid imaging techniques as well as with therapeutic systems like lasers or radiofrequency. MRI affords 3D localization without x-ray exposure. Open access and keyhole imaging allow nearly real time guidance of instruments. Minimally invasive techniques using endoscopes and hybrid tomographic guidance result in improved tip tracking of microinstruments and reduced complications. This safer access into the body will lead to interdisciplinary cooperation with the potential for large cost reductions. This report summarizes our experience regarding which of the hybrid imaging suites is best suited for procedures including among others drug instillations, prosthesis (stent) implantation, or microoperations (endoscopic diskectomy/sequestrectomy), and physiological measurements simultaneously.

Diagnostic Imaging↗
PubMed1985

Stability and self-assembly of the S-layer protein of the cell wall of Bacillus stearothermophilus.

The surface layer of the cell envelope of Bacillus stearothermophilus consists of a regular array of protein subunits. As shown by dodecyl sulfate polyacrylamide gel-electrophoresis and ultracentrifugation, the fully solubilized S-layer protein represents a homogeneous entity with a subunit molecular mass of 115 +/- 5 kDa. Solubilization of the protein may be accomplished at acid pH, or using high concentrations of urea or guanidine X HCl. It is accompanied by (partial) denaturation, thus interfering with the characterization of the protein in its unperturbed native state. Removal of the solubilizing agent by dialysis or dilution allows the S-layer to be reassembled into two-dimensional crystalline lattices identical to those observed in intact cells. To determine the kinetics of association, optimum conditions are found to be rapid mixing with 0.1 M sodium phosphate pH 7.0, 20 degrees C, final protein concentration greater than 10 micrograms/ml. If the time course of the self-assembly is monitored by light scattering, as well as by chemical cross-linking with glutardialdehyde, multiphasic kinetics with a rapid initial phase and slow consecutive processes of higher than second-order are observed. The rapid phase may be attributed to the formation of oligomeric precursors (Mr greater than 10(6) ). Concentration-dependent light scattering measurements give evidence for a "critical concentration" of association, suggesting that patches of 12-16 protein subunits fuse and recrystallize into the final (native) S-layer structure. Recrystallization tends to be complete.

Bacterial Proteins↗