The infectious prion protein (PrP Sc ) is the etiologic agent of transmissible neurodegenerative conditions such as scrapie or Creutzfeldt-Jakob disease. Its fragment 106-126 (PrP106-126) has been reported to maintain most of the pathological features of PrP Sc . We report here the intracellular mechanisms mediating the proliferative effects of PrP106-126 on rat cortical type I astrocytes. The proliferative effects of PrP106-126 started after 24h of treatment and lasted up to 9 days and was antagonized by the L-type voltage-sensitive calcium channel blocker nicardipine. Microfluorimetric studies showed that PrP106-126 caused a rapid increase in the (Ca ++ ) i . This effect was prevented by nicardipine, or by Ca ++ -free conditions, showing that the PrP106-126 enhances (Ca ++ ) i mobilizing Ca ++ from the extracellular environment. Moreover, binding studies demonstrated a direct interference of PrP106-126 with the dihydropyridine binding site. This is the first evidence that a prion protein fragment directly stimulates the proliferation of astrocytes via an increase in (Ca ++ ) i through the L-type voltage-sensitive calcium channels.
Biochemical and Biophysical Research Communications – Elsevier
Published: Nov 12, 1996
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