NR ABSZ
AU Brown,D.R.; Schmidt,B.; Groschup,M.H.; Kretzschmar,H.A.
TI Prion protein expression in muscle cells and toxicity of a prion protein fragment
QU European Journal of Cell Biology 1998 Jan; 75(1): 29-37
PT journal article
AB The prion protein (PrP) is a cell surface glycoprotein normally associated with neurones. Expression of the prion protein in cultured mouse myoblasts and myotubes suggests that the prion protein may play a physiological role in skeletal muscle. When myotubes differentiate from myoblasts prion protein expression is upregulated. Accompanying this increase is an upregulation of Cu/Zn superoxide dismutase (SOD-1) in myotubes. Muscle cells derived from mice deficient in cellular PrP (PrPc) show little increase in SOD-1 after differentiation from myoblasts to myotubes. Myoblasts and myotubes are resistant to the toxicity of a neurotoxic prion protein peptide (PrP106-126). However, in the presence of murine microglia, PrP106-126 causes a reduction in cell number. This effect is greater on myotubes than myoblasts. Even in the presence of microglia PrP106-126 is not toxic to muscle cells derived from PrP-deficient mice. Our results suggest that PrPc expression is associated with regulation of cellular resistance to oxidative stress in skeletal muscle.
MH Animal; Antioxidants/metabolism; Cell Differentiation/drug effects; Cell Line; Mice; Muscle, Skeletal/cytology/enzymology/*metabolism; Oxidative Stress/drug effects; Peptide Fragments/*biosynthesis/*toxicity; Prions/*biosynthesis/*toxicity; Rats; Superoxide Dismutase/metabolism; Support, Non-U.S. Gov't
AD Prof. Dr. Hans A Kretzschmar, Institut für Neuropathologie, Georg-August University Göttingen, Robert-Koch-Str. 40, D-37075 Göttingen
SP englisch
PO Deutschland
OR Prion-Krankheiten 2