Prion Protein

Cellular prion protein (PrPC) is a cell surface glycoprotein encoded by the gene PRNP. The physiological roles of PrPC are poorly understood, however its misfolded form (PrPSc) plays a critical role in neurogenerative transmissible spongiform encephalopathies (TSEs).

Products
Background
Literature
Pathways
Cat No Product Name / Activity
6250 Filipin III
Polyene antibiotic; inhibits formation of PrPSc
3491 Prion Protein 106-126 (human)
Prion protein fragment
3238 TCS PrP Inhibitor 13
Antiprion agent; inhibits PrPSc accumulation

Cellular prion protein (PrPC) is a cell surface glycoprotein encoded by the PRNP gene in humans. It is highly expressed in the CNS and PNS, where it is found on neurons, astrocytes, oligodendrocytes and microglia; it is also found in multiple peripheral organs and on immune cells. PrPC is an evolutionarily conserved protein indicating a critical physiological function, however it is also a cause of pathogenesis in neurodegenerative prion diseases.

The physiological roles of PrPC are poorly understood. There is evidence that PrPC can interact with other cell surface proteins, including neurotransmitter receptors such as metabotropic and ionotropic glutamate receptors, α7 nicotinic acetylcholine receptors; laminin receptors and neural cell adhesion molecule 1 (NCAM1). Additionally PrPC has been linked to many intracellular signaling pathways which exhibit crosstalk with each other; namely the cAMP/PKA, ERK1/2, PKC, RhoA/ROCK and Src kinase family pathways. This indicates that PrPC is involved in a wide range of cellular processes, including cell survival and proliferation, autophagy, protein synthesis, cellular glucose uptake, myelin maintenance and changes to cell shape, particularly neurite outgrowth.

PrPC is expressed both pre- and post-synaptically and interacts with several neurotransmitter receptors, implying a role in neuronal excitability. PrPC knockout mice have increased susceptibility to NMDA mediated excitotoxicity suggesting a neuroprotective function for PrPC. Knockout mice also show disrupted synaptic plasticity associated with abnormal behavior in nest building tasks, novel open field exploration, and more pronounced age related cognitive decline in short term memory tasks.

PrPC can undergo conversion to a pathogenic, partially protease resistant, misfolded form (PrPSc) which is highly prone to aggregation. The aggregation of this form, particularly the formation of soluble oligomers, causes cell death and neurodegeneration in prion diseases. Also known as transmissible spongiform encephalopathies (TSEs), these are infectious diseases characterized by rapidly progressing neurodegeneration following a long, preclinical incubation period. Examples include scrapie in sheep and goats, bovine spongiform encephalopathy in cattle and Creutzfeldt-Jakob disease in humans.

Literature for Prion Protein

Tocris offers the following scientific literature for Prion Protein to showcase our products. We invite you to request* or download your copy today!

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Kinases

Kinases Product Listing

A collection of over 400 products for kinase research, the listing includes inhibitors of:

  • Receptor Tyrosine Kinases
  • Protein Kinases A, C, D and G
  • PI-3 Kinase, Akt and mTOR
  • MAPK Signaling
  • Receptor Serine/Threonine Kinases
Neurodegeneration

Neurodegeneration Product Guide

A collection of over 275 products for neurodegeneration research, the guide includes research tools for the study of:

  • Alzheimer's disease
  • Parkinson's disease
  • Huntington's disease

Pathways for Prion Protein

MAPK

MAPK Signaling Pathway

The mitogen-activated protein kinase pathway evokes an intracellular signaling cascade in response to extracellular stimuli such as heat and stress. It can influence cell division, metabolism and survival.