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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Cellular prion protein transduces neuroprotective signals

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Chiarini, Luciana B. ; Freitas, Adriana R. O. ; Zanata, Silvio M. ; Brentani, Ricardo R. ; Martins, Vilma R. [5] ; Linden, Rafael
Total Authors: 6
Document type: Journal article
Source: EMBO Journal; v. 21, n. 13, p. 3317-3326, July 2002.
Field of knowledge: Biological Sciences - Biochemistry

To test for a role for the cellular prion protein (PrPc) in cell death, we used a PrPc-binding peptide. Retinal explants from neonatal rats or mice were kept in vitro for 24 h, and anisomycin (ANI) was used to induce apoptosis. The peptide activated both cAMP/protein kinase A (PKA) and Erk pathways, and partially prevented cell death induced by ANI in explants from wild-type rodents, but not from PrPc-null mice. Neuroprotection was abolished by treatment with phosphatidylinositol-specific phospholipase C, with human peptide 106-126, with certain antibodies to PrPc or with a PKA inhibitor, but not with a MEK/Erk inhibitor. In contrast, antibodies to PrPc that increased cAMP also induced neuroprotection. Thus, engagement of PrPc transduces neuroprotective signals through a cAMP/PKA-dependent pathway. PrPc may function as a trophic receptor, the activation of which leads to a neuroprotective state. (AU)

FAPESP's process: 99/07124-8 - The role of celular prion protein in physiological and pathological processes
Grantee:Vilma Regina Martins
Support Opportunities: Research Projects - Thematic Grants