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Axonal transport of the cellular prion protein is increased during axon regeneration
Author(s) -
Moya Kenneth L.,
Hässig Raymonde,
Breen Kieran C.,
Volland Hervé,
Di Giamberardino Luigi
Publication year - 2005
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2004.02940.x
Subject(s) - axon , regeneration (biology) , microbiology and biotechnology , glycoprotein , biology , axoplasmic transport , hamster , prion protein , growth cone , schwann cell , extracellular , sciatic nerve , in vitro , biochemistry , anatomy , pathology , medicine , disease
The cellular prion protein, PrP c , is a glycosylphosphatidylinositol‐anchored cell surface glycoprotein and a protease‐resistant conformer of the protein may be the infectious agent in transmissible spongiform encephalopathies. PrP c is localized on growing axons in vitro and along fibre bundles that contain elongating axons in developing and adult brain. To determine whether the growth state of axons influenced the expression and axonal transport of PrP c , we examined changes in the protein following post‐traumatic regeneration in the hamster sciatic nerve. Our results show (1) that PrP c in nerve is significantly increased during nerve regeneration; (2) that this increase involves an increase in axonally transported PrP c ; and (3) that the PrP c preferentially targeted for the newly formed portions of the regenerating axons consists of higher molecular weight glycoforms. These results raise the possibility that PrP c may play a role in the growth of axons in vivo , perhaps as an adhesion molecule interacting with the extracellular environment through specialized glycosylation.