NR AUBP
AU Massimino,M.L.; Ferrari,J.; Sorgato,M.C.; Bertoli,A.
TI Heterogeneous PrPc metabolism in skeletal muscle cells
QU FEBS Letters 2006 Feb 6; 580(3): 878-84
PT journal article
AB Recent reports have shown that prions, the causative agent of transmissible spongiform encephalopathies, accumulate in the skeletal muscle of diseased animals and man. In an attempt to characterise in this tissue the prion protein (PrPc), whose conformational rearrangement governs the generation of prions, we have analysed the protein in primary cultured murine myocytes and in different skeletal muscle types. Our results indicate that the expression and cellular processing of PrPc change during myogenesis, and in muscle fibres with different contractile properties. These findings imply a potential role for PrPc in the skeletal muscle physiology, but may also explain the different capability of muscles to sustain prion replication.
MH Animals; Animals, Newborn; Humans; Mice; *Muscle Development; Muscle Fibers/*metabolism/pathology; Muscle, Skeletal/*metabolism/pathology; Organ Specificity; PrPc Proteins/*metabolism; Prion Diseases/*metabolism/pathology; Research Support, Non-U.S. Gov't
AD Department of Biological Chemistry, University of Padova, viale G. Colombo 3, 35121 Padova, Italy.
SP englisch
PO Niederlande