PubMed Health⌕ Search

Biomedical subjects

J H Hoffmann

Publications and source records attributed to J H Hoffmann.

6 recordsLinked to original sources
PubMed2002

[Magnetoneurographic registration of evoked summation action fields over lumbar vertebrae following transcutaneous tibial nerve stimulation].

Goal of this study was the development of a protocol for the registration of evoked magnetic fields over the lumbar spine using off-the-shelf equipment. Three subjects in a sitting position with their torso bent slightly forward were stimulated at the tibial nerve with a commercially available stimulator. Neuromagnetic fields were registered over a circular, 800 cm2 area of the lumbosacral spine using a 61-channel 4D-Neuroimaging biomagnetometer. After appropriate signal processing, dipolar magnetic fields with a field strength 5-17 fT peak-to-peak amplitude were detected in three out of four registrations. Location and orientation of these fields concurred with the expected evoked compound action currents along the course of the nerve fibers.

Adult↗
PubMed2001

Activation of the redox-regulated molecular chaperone Hsp33--a two-step mechanism.

BACKGROUND: Hsp33 is a novel redox-regulated molecular chaperone. Hsp33 is present in the reducing environment of the cytosol and is, under normal conditions, inactive. The four highly conserved cysteines found in Hsp33 constitute a novel zinc binding motif. Upon exposure to oxidative stress, Hsp33's chaperone activity is turned on. This activation process is initiated by the formation of two intramolecular disulfide bonds. Recently, the 2.2 A crystal structure of Hsp33 has been solved, revealing that Hsp33 is present as a dimer in the structure (Vijayalakshmi et al., this issue, 367-375 [1]). RESULTS: We show here that oxidized, highly active Hsp33 is a dimer in solution. In contrast, reduced and inactive Hsp33 is monomeric. The incubation of reduced Hsp33 in H(2)O(2) leads to the simultaneous formation of two intramolecular disulfide bonds and the concomitant release of zinc. This concentration-independent step is followed by a concentration-dependent association reaction. The dimerization of Hsp33 requires highly temperature-sensitive structural rearrangements. This allows Hsp33's activation process to be greatly accelerated at heat shock temperatures. CONCLUSIONS: The regulation of Hsp33's chaperone function is highly sophisticated. On a transcriptional level, Hsp33 is under heat shock control. This increases the concentration of Hsp33 under heat and oxidative stress, a process that favors dimerization, a critical step in Hsp33's activation reaction. On a posttranslational level, Hsp33 is redox regulated. Dimerization of disulfide-bonded Hsp33 monomers leads to the formation of two extended, putative substrate binding sites. These sites might explain Hsp33's high and promiscuous affinity for unstructured protein folding intermediates.

Bacterial Proteins↗