Prion protein (PrPc) interacts with histone H3 confirmed by affinity chromatography

Cai, Hanning; Xie, Ying; Hu, Lingyin; Fan, Jie; Li, Renqiang

doi:10.1016/j.jchromb.2013.04.003

Cited by 4 publications

(3 citation statements)

References 17 publications

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“…In addition to truncated forms, PrP C can localize in the nucleus of different cell types including neural cells, and it interacts with structural chromatin components, principally histone H3; the interaction of PrP C with histone H3 suggests that PrP is involved in transcriptional regulation in the nucleus . Nuclear PrP interacts with distinct proteins involved in cell proliferation and cell junction in several cell types, and PrP participates in the process of DNA repair after genotoxic stress …”

Section: Discussionmentioning

confidence: 99%

Sporadic Creutzfeldt–Jakob disease with glial PrP^Res nuclear and perinuclear immunoreactivity

et al. 2018

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Proteinase K-resistant prion protein (PrP ) nuclear and perinuclear immunoreactivity in oligodendrocytes of the frontal cortex is found in one case of otherwise typical sporadic Creutzfeldt-Jakob disease (sCJD) type VV2a. The PrP nature of the inclusions is validated with several anti-PrP antibodies directed to amino acids 130-160 (12F10), 109-112 (3F4), 97-102 (8G8) and the octarepeat region (amino acids 59-89: SAF32). Cellular identification and subcellular localization were evaluated with double- and triple-labeling immunofluorescence and confocal microscopy using antibodies against PrP, glial markers, and histone H3. Based on review of the literature and our own experience, this is a very odd situation that deserves further validation in other cases.

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Section: Discussionmentioning

confidence: 99%

Sporadic Creutzfeldt–Jakob disease with glial PrP^Res nuclear and perinuclear immunoreactivity

et al. 2018

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“…The idea of a role for PrP in DNA repair is further supported by its affinity for nucleic acids ( 44 ) and its capacity to bend and unwind DNA ( 45 , 46 ). Moreover, it was recently demonstrated that it interacts with chromatin histones ( 33 , 47 ). Our results raise the question of how PrP, a protein normally going through the glycosylation pathway, can, in response to a genotoxic stress, be directed to the cell nucleus.…”

Section: Discussionmentioning

confidence: 99%

The prion protein is critical for DNA repair and cell survival after genotoxic stress

Bravard¹,

Auvré²,

Fantini³

et al. 2014

Nucleic Acids Research

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The prion protein (PrP) is highly conserved and ubiquitously expressed, suggesting that it plays an important physiological function. However, despite decades of investigation, this role remains elusive. Here, by using animal and cellular models, we unveil a key role of PrP in the DNA damage response. Exposure of neurons to a genotoxic stress activates PRNP transcription leading to an increased amount of PrP in the nucleus where it interacts with APE1, the major mammalian endonuclease essential for base excision repair, and stimulates its activity. Preventing the induction of PRNP results in accumulation of abasic sites in DNA and impairs cell survival after genotoxic treatment. Brains from Prnp−/− mice display a reduced APE1 activity and a defect in the repair of induced DNA damage in vivo. Thus, PrP is required to maintain genomic stability in response to genotoxic stresses.

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“…Many studies have identified PrP-interacting and -binding partners, such as Cu 2+ , Ni 2+ , glycosaminoglycans, DNA, RNA, a number of signaling proteins, histone H3, and thiamine etc. [51]- [54]. In addition to classical function in glycolysis, aldolase has been implicated in insulin-dependent glucose transport mediated by GLUT4, and appears to be a major calmodulin-dependent protein kinase phosphatase-binding protein in the brain [55] [56].…”

Section: Discussionmentioning

confidence: 99%

Prion Protein Binds to Aldolase A Produced by Bovine Intestinal M Cells

Nagasawa¹,

Takahashi²,

Itani³

et al. 2015

OJVM

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Microfold (M) cells are a kind of intestinal epithelial cell in the follicle-associated epithelium (FAE) of Peyer's patches. They can transport antigens and microorganisms to lymphoid tissues. Bovine spongiform encephalopathy (BSE) is a fatal neurodegenerative disorder in cattle. It is linked to variant Creutzfeldt-Jakob disease in humans. Although it is thought that M cells transport the BSE agent, the exact mechanism by which it crosses the intestinal barrier is not clear. We have bovine intestinal epithelial cell line (BIE cells), which can differentiate into the M cell type in vitro after stimulation, and which is able to transport the BSE agent. We show here that M cells are able to incorporate large numbers of PrP coated magnetic particles into intracellular vesicles, which we collected. The results of 2-DE show a specific protein associated with the PrP-coated particles, compared with non-coated particles. This protein was identified as aldolase A, a glycolytic pathway enzyme, using LC-MS/MS analysis. Aldolase A was synthesized and secreted by BIE cells, and increased during M cell differentiation. In the villi of the bovine intestine, aldolase A was detected on the surface of the epithelium and in the mucus droplet of goblet cells. In the FAE of bovine jejunal and ileal Peyer's patches, aldolase A was localized on the surface and the apical part of the M cells. The binding of rbPrP to aldolase A was clearly detected and inhibited by pre-treatment of anti-aldolase A antibody. Aldolase A was co-stained with incorporated PrP Sc in M-BIE cells. These results suggest that bovine M cells and goblet cells synthesize aldolase A, and that aldolase A may * Corresponding author. have the ability to bind PrP and associate with PrP in cellular vesicles. Therefore, aldolase A-positive M cells may play a key role in the invasion of BSE into the body.

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Prion protein (PrPc) interacts with histone H3 confirmed by affinity chromatography

Cited by 4 publications

References 17 publications

Sporadic Creutzfeldt–Jakob disease with glial PrP^Res nuclear and perinuclear immunoreactivity

Sporadic Creutzfeldt–Jakob disease with glial PrP^Res nuclear and perinuclear immunoreactivity

The prion protein is critical for DNA repair and cell survival after genotoxic stress

Prion Protein Binds to Aldolase A Produced by Bovine Intestinal M Cells

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Prion protein (PrPc) interacts with histone H3 confirmed by affinity chromatography

Cited by 4 publications

References 17 publications

Sporadic Creutzfeldt–Jakob disease with glial PrPRes nuclear and perinuclear immunoreactivity

Sporadic Creutzfeldt–Jakob disease with glial PrPRes nuclear and perinuclear immunoreactivity

The prion protein is critical for DNA repair and cell survival after genotoxic stress

Prion Protein Binds to Aldolase A Produced by Bovine Intestinal M Cells

Contact Info

Product

Resources

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Sporadic Creutzfeldt–Jakob disease with glial PrP^Res nuclear and perinuclear immunoreactivity

Sporadic Creutzfeldt–Jakob disease with glial PrP^Res nuclear and perinuclear immunoreactivity