Roles of endoproteolytic α-cleavage and shedding of the prion protein in neurodegeneration

被引：47

作者：

Altmeppen, Hermann C. ^{[1
]}

Prox, Johannes ^{[2
]}

Puig, Berta ^{[1
]}

Dohler, Frank ^{[1
]}

Falker, Clemens ^{[1
]}

Krasemann, Susanne ^{[1
]}

Glatzel, Markus ^{[1
]}

机构：

[1] Univ Med Ctr HH Eppendorf, Inst Neuropathol, D-20246 Hamburg, Germany

[2] Univ Kiel, Inst Biochem, Kiel, Germany

来源：

FEBS JOURNAL | 2013年 / 280卷 / 18期

关键词：

ADAM10; Alzheimer's disease; neurodegeneration; neurotoxic oligomers; prion disease; prion protein; shedding; -cleavage; -amyloid; AMYLOID PRECURSOR PROTEIN; CELLULAR PRION; A-BETA; SECRETASE CLEAVAGE; AMINO-TERMINUS; IN-VIVO; ADAM10; DISEASE; PRPC; DISINTEGRIN;

D O I：

10.1111/febs.12196

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The cellular prion protein (PrPC) plays important roles in neurodegenerative diseases. First, it is the well-established substrate for the conformational conversion into its pathogenic isoform (PrPSc) giving rise to progressive and fatal prion diseases. Moreover, several recent reports highlight important roles of PrPC in other neurodegenerative conditions such as Alzheimer's disease. Since PrPC is subject to proteolytic processing, here we discuss the two main cleavage events under physiological conditions, -cleavage and shedding. We focus on how these cleavages and the resulting fragments may impact prion diseases as well as other neurodegenerative proteinopathies. Finally, we discuss the recently identified sheddase of PrPC, namely the metalloprotease ADAM10, with regard to therapeutic potential against neurodegenerative diseases.

引用

页码：4338 / 4347

页数：10

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