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Identification of candidate proteins binding to prion protein.

Abstract：

:Prion diseases are disorders of protein conformation that produce neurodegeneration in humans and animals. Studies of transgenic (Tg) mice indicate that a factor designated protein X is involved in the conversion of the normal cellular prion protein (PrPC) into the scrapie isoform (PrPSc); protein X appears to interact with PrPC but not with PrPSc. To search for PrPC binding proteins, we fused PrP with alkaline phosphatase (AP) to produce a soluble, secreted probe. PrP-AP was used to screen a lambdagt11 mouse brain cDNA library, and six clones were isolated. Four cDNAs are novel while two clones are fragments of Nrf2 (NF-E2 related factor 2) transcription factor and Aplp1 (amyloid precursor-like protein 1). The observation that PrP binds to a member of the APP (amyloid precursor protein) gene family is intriguing, in light of possible relevance to Alzheimer's disease. Four of the isolated clones are expressed preferentially in the mouse brain and encode a similar motif.

journal_name

Neurobiol Dis

journal_title

Neurobiology of disease

authors

Yehiely F,Bamborough P,Da Costa M,Perry BJ,Thinakaran G,Cohen FE,Carlson GA,Prusiner SB

doi

10.1006/nbdi.1997.0130

subject

Has Abstract

pub_date

1997-01-01 00:00:00

pages

339-55

issue

4

eissn

0969-9961

issn

1095-953X

pii

S0969-9961(97)90130-3

journal_volume

3

pub_type

杂志文章

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