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Prion Disease Related Research Tools

Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of fatal neurodegenerative disorders that include Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler-Scheinker syndrome, kuru and fatal familial insomnia. Prion diseases are thought to be caused by the misfolding of native cellular prion protein (PrP^C) into the aggregation prone form (PrP^Sc). PrP^Sc refers to the misfolded infectious form that differs from PrP^C because it has a higher content of β-sheet structure and it aggregates to form medium and large size polymers. The conversion of PrP^C into PrP^Sc is the main event in prion disease.

Structure of PrPC and PrPSc. Fig.1 Structure of PrP^C and PrP^Sc.

The Central Role of PrP^Sc

There is no doubt that the formation and accumulation of PrP^Sc in the brain is the triggering factor of prion disease. PrP^Sc accumulates in different brain regions as distinct types of deposits depending on the animal species and strains of the agent. The loss of the critical biological function of PrP^C is one possible mechanism by which PrP^Sc formation might result in neurodegeneration. Studies have proposed various functions of PrP^C, such as the roles in apoptosis, oxidative stress, neuroprotection, transmembrane signaling, myelination, cell adhesion, and trafficking of metal ions. Another possible mechanism by which PrP^Sc formation might be linked to the disease is by direct toxicity of the misfolded protein.

Therapeutic Development

Currently, no therapeutic or prophylactic regimens exist for prion diseases. A variety of therapeutic strategies have been proposed but most of them directed at preventing prion conversion. The targets include inhibition of PrP^C expression, enhancement of PrP^C degradation, inhibition of PrP^C-PrP^Sc interaction, inhibition of PrP^Sc oligomer formation, and enhancement of PrP^Sc degradation. PrP^C and PrP^Sc have been widely studied to understand the enigmatic nature of prions. Additionally, some cellular factors have been implicated as possible targets in PrP^C-mediated or PrP^Sc-induced neurodegenerative processes. One example is the growth arrest and DNA-damage-inducible protein GADD34. GADD34 promotes dephosphorylation of the α-subunit of eukaryotic translation initiation factor 2 and reverses translational suppression caused by the prion infection-induced unfolded protein response in the endoplasmic reticulum.

Therapeutic targets in PrPSc degradation pathways. Fig.1 Therapeutic targets in PrP^Sc degradation pathways. (Goold, 2015)

Targets and Canditaes Related to Prion Disease

Beclin VPS34 Complex	P150; Vps34; Beclin 1; mAtg14
mTROC complex	Raptor; PRAS40; mTOR; Deptor; mLST8
Others	Sirt 1; Heat shock proteins; Cytosolic PrP^Sc; Membrane associated PrP^Sc; Lysomal proteases; USP 14; p38 MAPK; DNA-damage-inducible protein GADD34
Small molecules	Prion receptor laminin (LPR/LR); Pentosan polysulfate (PPS); Quinacrine; Compound B; IND series; Anle138b; Amphotericin B

Creative Biolabs aims to provide biological products to help promote your prion diseases project research. These reagents include but are not limited to site-specific modified peptides, conjugated peptides, monoclonal antibodies (mAbs), polyclonal antibodies (pAbs), labeled antibodies, proteins, analytical kits, and small molecule activators and inhibitors.

Reference

Goold, R.; et al. Prion degradation pathways: potential for therapeutic intervention. Molecular and Cellular Neuroscience. 2015, 66: 12-20.

For Research Use Only. Not For Clinical Use.

Target

CASPR

67LR

Neurofilament L

SORT1

PRNP

KCNIP3

Adracalin

S100 Beta

eNOS

HIP1R

SMNDC1

Plexin A1

Ubiquitin

GAPDH

PFKFB3

FGF13

Mint-1

YY1

RTR

DNAJC5

SOD3

ANTXR2/CMG-2

Synaptogyrin 3

Neuroglycan C

UNC5C

IRS1

PMP22

Prostate Specific Antigen

ATOH1

Norbin

NDRG2

EAAT2

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Host Species:: Mouse

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Prion Disease Related Research Tools

The Central Role of PrPSc

Therapeutic Development

Targets and Canditaes Related to Prion Disease

Target

The Central Role of PrP^Sc