Intracellular Calcium Rise through L-Type Calcium Channels, as Molecular Mechanism for Prion Protein Fragment 106-126-Induced Astroglial Proliferation

Intracellular Calcium Rise through L-Type Calcium Channels, as Molecular Mechanism for Prion... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biochemical and Biophysical Research Communications Elsevier

Intracellular Calcium Rise through L-Type Calcium Channels, as Molecular Mechanism for Prion Protein Fragment 106-126-Induced Astroglial Proliferation

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Publisher
Elsevier
Copyright
Copyright © 1996 Academic Press
ISSN
0006-291x
DOI
10.1006/bbrc.1996.1673
pmid
8920926
Publisher site
See Article on Publisher Site

Abstract

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.

Journal

Biochemical and Biophysical Research CommunicationsElsevier

Published: Nov 12, 1996

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