Numerous studies have investigated the cellular prion protein (PrP) since its discovery. These investigations have explained that its structure is predominantly composed of alpha helices and short beta sheet segments, and when its abnormal scrapie isoform (PrP) is infected, PrP transforms the PrP, leading to prion diseases, including Creutzfeldt-Jakob disease in humans and bovine spongiform encephalopathy in cattle. Given its ubiquitous distribution across a variety of cellular types, the PrP manifests a diverse range of biological functions, including cell-cell adhesion, neuroprotection, signalings, and oxidative stress response.
View Article and Find Full Text PDFThe immune system is one of the most important parts of the human body and immunomodulation is the major function of the immune system. In response to outside pathogens or high inflammation, the immune system is stimulated or suppressed. Thus, identifying effective and potent immunostimulants or immunosuppressants is critical.
View Article and Find Full Text PDFThe cellular prion protein (PrP) is a cell surface glycoprotein expressed in many cell types that plays an important role in normal cellular processes. However, an increase in PrP expression has been associated with a variety of human cancers, where it may be involved in resistance to the proliferation and metastasis of cancer cells. PrP-deficient () and PrP-overexpressing (Tga20) mice were studied to evaluate the role of PrP in the invasion and metastasis of cancer.
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