Major prion protein in the context of Protein folding

Major prion protein in the context of Protein folding

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⭐ Core Definition: Major prion protein

The major prion protein (PrP) is encoded in the human body by the PRNP gene also known as CD230 (cluster of differentiation 230). Expression of the protein is most prominent in the nervous system but occurs in many other tissues throughout the body.

The protein can exist in multiple isoforms: the normal PrP form, and the protease-resistant form designated PrP such as the disease-causing PrP (scrapie) and an isoform located in mitochondria. The misfolded version PrP is associated with a variety of uniformly fatal neurodegenerative diseases in humans and nonhuman species. In nonhuman species these include ovine scrapie, bovine spongiform encephalopathy (BSE, mad cow disease), feline spongiform encephalopathy, transmissible mink encephalopathy (TME), exotic ungulate encephalopathy, chronic wasting disease (CWD) which affects deer; human prion diseases include Creutzfeldt–Jakob disease (CJD), fatal familial insomnia (FFI), Gerstmann–Sträussler–Scheinker syndrome (GSS), kuru, and variant Creutzfeldt–Jakob disease (vCJD). Similarities exist between kuru, thought to be due to human ingestion of diseased individuals, and vCJD, thought to be due to human ingestion of BSE-tainted cattle products.

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Major prion protein in the context of Prions

A prion (/ˈpriːɒn/ ) is a misfolded protein that induces misfolding in normal variants of the same protein, leading to cellular death. Prions are responsible for prion diseases, known as transmissible spongiform encephalopathy (TSEs), which are fatal and transmissible neurodegenerative diseases affecting both humans and animals. These proteins can misfold sporadically, due to genetic mutations, or by exposure to an already misfolded protein, leading to an abnormal three-dimensional structure that can propagate misfolding in other proteins.

The term prion comes from "proteinaceous infectious particle". Unlike other infectious agents such as viruses, bacteria, and fungi, prions do not contain nucleic acids (DNA or RNA). Prions are mainly twisted isoforms of the major prion protein (PrP), a naturally occurring protein with an uncertain function. They are the hypothesized cause of various TSEs, including scrapie in sheep, chronic wasting disease (CWD) in deer, bovine spongiform encephalopathy (BSE) in cattle (mad cow disease), and Creutzfeldt–Jakob disease (CJD) in humans.

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LINKED FROM (PARENTS)
← Prions ← Prion
LINKS TO (CHILDREN)
Gene → Cluster of differentiation → Protein → Nervous system → Isoforms → Protease → Mitochondria → Protein folding → Neurodegeneration → Ovine → Scrapie → Bovine spongiform encephalopathy → Feline spongiform encephalopathy → Transmissible mink encephalopathy → Exotic ungulate encephalopathy → Chronic wasting disease → Deer → Creutzfeldt–Jakob disease → Fatal familial insomnia → Gerstmann–Sträussler–Scheinker syndrome → Kuru (disease) → Variant Creutzfeldt–Jakob disease →