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. 1993 May 1;90(9):4309–4313. doi: 10.1073/pnas.90.9.4309

Localization of the mRNA for a chicken prion protein by in situ hybridization.

D A Harris 1, P Lele 1, W D Snider 1
PMCID: PMC46496  PMID: 8483948

Abstract

The infectious agent (prion) responsible for transmissible spongiform encephalopathies in humans and animals is composed primarily of a 33- to 35-kDa glycoprotein called PrPSc (scrapie isoform of prion protein), which is a posttranslationally modified form of the normal cell-surface protein PrPC. Little is known about the function of PrPC. Interestingly, chPrP, the chicken homologue of PrPC, copurifies with a factor from brain that stimulates synthesis of acetylcholine receptors on skeletal muscle cells. Using in situ hybridization, we report here that chPrP mRNA is widely distributed in cholinergic and noncholinergic neurons throughout the adult central nervous system, including those in the telencephalic striata, thalamus and hypothalamus, optic tectum, medulla, cerebellum, and spinal cord. The mRNA is present in the brain and spinal cord as early as embryonic day 6 and is also found in dorsal root ganglia, retina, intestine, and heart. Our data suggest that if chPrP serves to regulate acetylcholine receptor number on postsynaptic targets, this is not its only function. It is likely that the protein plays a more widespread role in the central nervous system and perhaps elsewhere, possibly one related to intercellular communication, adhesion, or recognition. The chicken embryo represents an attractive experimental system in which to investigate the normal developmental function of PrPC.

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