期刊
NEUROBIOLOGY OF DISEASE
卷 16, 期 3, 页码 527-537出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.nbd.2004.05.005
关键词
prion; Golgi apparatus; brain
资金
- NIA NIH HHS [P30 AG10133] Funding Source: Medline
- NIGMS NIH HHS [T32GM07200] Funding Source: Medline
- NINDS NIH HHS [NS40975] Funding Source: Medline
Prion diseases result from conversion of PrPC, a neuronal membrane glycoprotein of unknown function, into PrPSc, an abnormal conformer that is thought to be infectious. To facilitate analysis of PrP distribution in the brain, we have generated transgenic mice in which a PrP promoter drives expression of PrP-EGFP, a fusion protein consisting of enhanced green fluorescent protein inserted adjacent to the glycolipid attachment site of PrP. We find that PrP-EGFP in the brain is glycosylated and glycolipid-anchored and is localized to the surface membrane and the Golgi apparatus of neurons. Like endogenous PrP, PrP-EGFP is concentrated in synapse-rich regions and along axon tracts. PrP-EGFP is functional in vivo, since it ameliorates the cerebellar neurodegeneration induced by a truncated form of PrP. These observations clarify uncertainties in the cellular localization of PrPC in brain, and they establish PrP-EGFP transgenic mice as useful models for further studies of prion biology. (C) 2004 Elsevier Inc. All rights reserved.
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