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J. Biol. Chem., Vol. 276, Issue 42, 39145-39149, October 19, 2001
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From the Departments of The function of the cellular prion protein (PrP)
is still poorly understood. We present here an unprecedented role for
PrP against Bax-mediated neuronal apoptosis and show that PrP
potently inhibits Bax-induced cell death in human primary
neurons. Deletion of four octapeptide repeats of PrP (PrP
Prion Protein Protects Human Neurons against
Bax-mediated Apoptosis*
§,§,
**
Neurology and Neurosurgery,
and ¶ Pediatrics, McGill University, Montréal, PQ,
H3A 2T5 Canada and the Bloomfield Center for Research in
Aging, The Lady Davis Institute for Medical Research, Sir Mortimer B. Davis, Jewish General Hospital, Montreal, Quebec, H3T 1E2 Canada
OR)
and familial D178N and T183A PrP mutations completely or partially
eliminate the neuroprotective effect of PrP. PrP remains
anti-apoptotic despite truncation of the
glycosylphosphatidylinositol (GPI) anchor signal peptide,
indicating that the neuroprotective form of PrP does not require the
abundant cell surface GPI-anchored PrP. Our results implicate PrP as a
potent and novel anti-apoptotic protein against Bax-mediated cell death.
*
This work was supported by Grant MT-13464 from the Medical
Research Council of Canada and Fonds de Recherche en Santé du Québec (to A. L. B.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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