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Anterograde axonal transport of chicken cellular prion protein (PrP c ) in vivo requires its N‐terminal part
Author(s) -
Butowt Rafal,
Davies Paul,
Brown David R.
Publication year - 2007
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.21229
Subject(s) - axoplasmic transport , internalization , microbiology and biotechnology , biology , soma , dynein , biophysics , gene isoform , extracellular , microtubule , chemistry , biochemistry , cell , neuroscience , gene
The cellular isoform of prion protein (PrP c ) can exist in membrane‐bound and secreted forms. Both forms of PrP c can be transported by retinal ganglion cell (RGC) axons along the optic nerve in the anterograde direction. In this study we determined which part of chicken PrP c is required for its anterograde axonal transport within the optic nerve of embryonic chicken. We intraocularly injected radio‐iodinated fragments of recombinant chicken PrP c and then examined their anterograde axonal transport from retina into optic tectum. Using gamma‐counting and different autoradiographic techniques we quantified anterograde axonal transport of the N‐terminal part of chicken PrP c (amino acid residues 1–116) in this model system. The transport of the N‐terminal part has similar properties as the anterograde transport of full‐length chicken PrP c (Butowt et al., 2006) described previously (e.g., has similar efficiency, is microtubule‐dependent, and is saturable). Moreover, the pattern of ultrastructural distribution of the N‐terminal fragment within RGCs is similar to the distribution of full‐length PrP c . The C‐terminal fragment of chicken PrP c (residues 118–246) and different PrP‐derived peptides were not transported. Moreover, PrP c ‐derived peptides were sorted into different endocytotic pathways in neurons, indicating that they cannot substitute for full‐length PrP c to study its internalization and trafficking. These data indicate that the N‐terminal half of chicken PrP c contains the necessary information to drive the internalization and subsequent sorting of extracellular PrP c in RGCs soma into the anterograde axonal transport pathway. © 2007 Wiley‐Liss, Inc.