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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).
|Cat. No.||Product Name / Activity|
|Oligomeric aggregation inhibitor; inhibits prion protein and α-synuclein aggregate formation|
|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.
Tocris offers the following scientific literature for Prion Protein to showcase our products. We invite you to request* your copy today!
*Please note that Tocris will only send literature to established scientific business / institute addresses.