Nanopatterning of biomolecules with microscale beads.
Explore the source record for details and available documents.
Biophysics↗
Biomedical subjects
Otmar Höglinger
Publications and source records attributed to Otmar Höglinger.
Single-molecule reader for high-throughput bioanalysis.
We report here the development of a device for single-molecule imaging on large surface areas. A CCD camera operated in time delay and integration mode is synchronized with the movement of a sample scanning stage, enabling continuous data acquisition. Experiments on single fluorescent lipid molecules in supported lipid bilayers and on stained living cells demonstrate the capabilities of the method. Areas of up to 5 x 5 mm(2) were recorded within 11 min at a pixel size of 129 nm.
Biological Assay↗
Co-localization of CD3 and prion protein in Jurkat lymphocytes after hypothermal stimulation.
While long-term effects of temperature treatment in respect of, e.g., gene-expression and cellular function have already been studied in some detail, nothing is known on the physiological responses of lymphocytes during short-term hypothermal shifts. In this report, we characterized the effects of such a stimulation using the human lymphocyte cell line Jurkat E6.1 and present evidence that warming from 4 to 37 degrees C for only 2 min is sufficient to cause co-localization of CD3, prion protein and the lipid-raft ganglioside GM1 paralleling lymphocyte activation as observed by Ca(2+) mobilization and mitogen-activated protein kinase-phosphorylation.
Actins↗
The physiological functions of prion protein.
Prion proteins are mentioned predominantly as unprecedented infectious pathogens in the context of transmissible spongiform encephalopathies. Since prions are devoid of nucleic acids, disease transmission must be mediated by an entirely novel mechanism. The general accepted theory proposes the conversion of cellular prion protein (PrP(C)) into the pathological isoform solely through conformational changes. This process favors the development of insoluble protein aggregates in the central nervous system typical for prion diseases. However, progress to elucidate the physiological functions of PrP(C) is still slow besides recent indications of a multifaceted network, in which PrP(C) seems to play a fundamental role. Possible contributions of interrupted or disturbed physiological signaling events due to the pathological prion protein isoform are presented in terms of recent findings.
Animals↗