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朊病毒蛋白：生理与疾病的交汇点。

Prion protein at the crossroads of physiology and disease.

机构信息

Department of Biochemistry, Boston University School of Medicine, Boston, MA 02118, USA.

出版信息

Trends Neurosci. 2012 Feb;35(2):92-103. doi: 10.1016/j.tins.2011.10.002. Epub 2011 Dec 1.

DOI:10.1016/j.tins.2011.10.002
PMID:22137337
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3273588/
Abstract

The presence of the cellular prion protein (PrP(C)) on the cell surface is critical for the neurotoxicity of prions. Although several biological activities have been attributed to PrP(C), a definitive demonstration of its physiological function remains elusive. In this review, we discuss some of the proposed functions of PrP(C), focusing on recently suggested roles in cell adhesion, regulation of ionic currents at the cell membrane and neuroprotection. We also discuss recent evidence supporting the idea that PrP(C) may function as a receptor for soluble oligomers of the amyloid β peptide and possibly other toxic protein aggregates. These data suggest surprising new connections between the physiological function of PrP(C) and its role in neurodegenerative diseases beyond those caused by prions.

摘要

细胞朊病毒蛋白（PrP(C)）存在于细胞膜表面对于朊病毒的神经毒性至关重要。尽管已经赋予了 PrP(C) 几种生物学活性，但它的生理功能仍然难以确定。在这篇综述中，我们讨论了 PrP(C) 的一些拟议功能，重点是最近提出的在细胞黏附、调节细胞膜离子流和神经保护方面的作用。我们还讨论了最近支持 PrP(C) 可能作为淀粉样β肽可溶性寡聚物和可能其他毒性蛋白聚集体的受体这一观点的证据。这些数据表明，PrP(C) 的生理功能与其在朊病毒以外的神经退行性疾病中的作用之间存在惊人的新联系。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fd9/3273588/2e0bfa1f79c4/nihms334829f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fd9/3273588/249696312a9f/nihms334829f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fd9/3273588/e77c589aec30/nihms334829f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fd9/3273588/d136414fb75e/nihms334829f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fd9/3273588/8f30d0ca5c14/nihms334829f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fd9/3273588/8c2585614c03/nihms334829f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fd9/3273588/2e0bfa1f79c4/nihms334829f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fd9/3273588/249696312a9f/nihms334829f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fd9/3273588/e77c589aec30/nihms334829f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fd9/3273588/d136414fb75e/nihms334829f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fd9/3273588/8f30d0ca5c14/nihms334829f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fd9/3273588/8c2585614c03/nihms334829f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5fd9/3273588/2e0bfa1f79c4/nihms334829f6.jpg

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本文引用的文献

1
The N-terminal, polybasic region is critical for prion protein neuroprotective activity.N 端多碱性区域对于朊病毒蛋白的神经保护活性至关重要。
PLoS One. 2011;6(9):e25675. doi: 10.1371/journal.pone.0025675. Epub 2011 Sep 29.
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A nine amino acid domain is essential for mutant prion protein toxicity.一个九氨基酸结构域是突变朊病毒蛋白毒性所必需的。
J Neurosci. 2011 Sep 28;31(39):14005-17. doi: 10.1523/JNEUROSCI.1243-11.2011.
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Amyloid-β-induced synapse damage is mediated via cross-linkage of cellular prion proteins.淀粉样β诱导的突触损伤是通过细胞朊病毒蛋白的交联介导的。
J Biol Chem. 2011 Nov 4;286(44):37955-37963. doi: 10.1074/jbc.M111.248724. Epub 2011 Sep 7.
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Prion protein interacts with BACE1 protein and differentially regulates its activity toward wild type and Swedish mutant amyloid precursor protein.朊蛋白与 BACE1 蛋白相互作用，并对其针对野生型和瑞典突变型淀粉样前体蛋白的活性进行差异调节。
J Biol Chem. 2011 Sep 23;286(38):33489-500. doi: 10.1074/jbc.M111.278556. Epub 2011 Jul 27.
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Ablation of cellular prion protein does not ameliorate abnormal neural network activity or cognitive dysfunction in the J20 line of human amyloid precursor protein transgenic mice.敲除细胞朊病毒蛋白不能改善人淀粉样前体蛋白转基因小鼠 J20 品系中异常的神经网络活动或认知功能障碍。
J Neurosci. 2011 Jul 20;31(29):10427-31. doi: 10.1523/JNEUROSCI.1459-11.2011.
6
Interaction between prion protein and toxic amyloid β assemblies can be therapeutically targeted at multiple sites.朊病毒蛋白与毒性淀粉样 β 聚合体之间的相互作用可以在多个靶点进行治疗性靶向。
Nat Commun. 2011 Jun 7;2:336. doi: 10.1038/ncomms1341.
7
Enhanced neural progenitor/stem cells self-renewal via the interaction of stress-inducible protein 1 with the prion protein.应激诱导蛋白 1 与朊病毒蛋白相互作用增强神经祖细胞/干细胞自我更新。
Stem Cells. 2011 Jul;29(7):1126-36. doi: 10.1002/stem.664.
8
Alzheimer's disease brain-derived amyloid-β-mediated inhibition of LTP in vivo is prevented by immunotargeting cellular prion protein.阿尔茨海默病脑源性淀粉样蛋白-β在体内介导的 LTP 抑制可被针对细胞朊病毒蛋白的免疫靶向所预防。
J Neurosci. 2011 May 18;31(20):7259-63. doi: 10.1523/JNEUROSCI.6500-10.2011.
9
The cellular prion protein mediates neurotoxic signalling of β-sheet-rich conformers independent of prion replication.细胞朊病毒蛋白介导富含β-折叠构象的神经毒性信号，而不依赖于朊病毒复制。
EMBO J. 2011 May 18;30(10):2057-70. doi: 10.1038/emboj.2011.86. Epub 2011 Mar 25.
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An N-terminal polybasic domain and cell surface localization are required for mutant prion protein toxicity.N 端多碱性结构域和细胞表面定位是突变型朊病毒蛋白毒性所必需的。
J Biol Chem. 2011 Apr 22;286(16):14724-36. doi: 10.1074/jbc.M110.214973. Epub 2011 Mar 8.