PRND Human
Description
Introduction to PRND Human
PRND (Prion Protein 2, Dublet) is a gene encoding the doppel protein (Dpl), a glycosylphosphatidylinositol (GPI)-anchored glycoprotein structurally and biochemically analogous to the cellular prion protein (PrP). Located approximately 20 kbp downstream of the PRNP gene on chromosome 20, PRND is expressed predominantly in the testis and minimally in the central nervous system during embryogenesis . While its precise physiological role remains under investigation, PRND is implicated in blood vessel morphogenesis, endothelial cell function, and neurological disorders . Recombinant PRND Human refers to the engineered form of this protein, commonly used in laboratory research to study its biochemical properties and disease associations .
Biological Functions
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Neurological and Vascular Development: PRND regulates endothelial tip cell polarity and sprouting during CNS blood vessel morphogenesis. Genetic ablation in mice causes defective angiogenesis and impaired blood-brain barrier integrity .
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Reproductive System: Highly expressed in testis, PRND is critical for male fertility, with knockout models showing sterility .
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Disease Associations:
Mechanistic Insights
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PRND interacts with receptor tyrosine kinases (RTKs) to activate pathways involved in endothelial cell survival and migration .
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Structural studies reveal its antagonistic relationship with PrP: PRND’s neurotoxic effects are counteracted by PrP’s N-terminal domain .
Expression in Human Cancers
A study of 22 astrocytomas revealed differential PRND expression:
| Tumor Type | PRND Expression (Relative to Controls) |
|---|---|
| Glioblastoma (GBM) | 8.36±2.38 (highest) |
| Anaplastic Astrocytoma | 0.20±0.09 (70-fold lower than GBM) |
| Low-Grade Astrocytoma | 0.06±0.01 (140-fold lower) |
PRND is also elevated in gastric adenocarcinoma and anaplastic meningioma .
Polymorphisms and Disease Risk
| Polymorphism | Population | Association | Source |
|---|---|---|---|
| T174M | European | No strong link to sporadic CJD | |
| P56L | Korean | Potential marker for sporadic CJD | |
| T26M | Global | Neutral in prion diseases but under study |
Therapeutic Targets
Product Specs
Product Science Overview
Prion proteins are a unique class of proteins that have garnered significant attention due to their role in neurodegenerative diseases. The term “prion” was first coined by Stanley Prusiner in 1982 to describe “proteinaceous infectious particles” responsible for diseases such as scrapie, Creutzfeldt-Jakob disease (CJD), and kuru . Prion Protein 2 (Human Recombinant) is a synthetic version of the human prion protein, produced using recombinant DNA technology.
The prion protein (PrP) is encoded by the PRNP gene located on chromosome 20 in humans . The normal cellular form of the prion protein, known as PrP^C, is predominantly α-helical and is anchored to the cell membrane by a glycosylphosphatidylinositol (GPI) anchor . PrP^C is expressed at high levels in the brain and is involved in various cellular processes, including cell signaling and protection against oxidative stress .
Prion diseases are caused by the conformational conversion of the normal cellular prion protein (PrP^C) into its misfolded, pathogenic isoform, known as scrapie prion protein (PrP^Sc) . This misfolded form is rich in β-sheets and has the ability to self-replicate by templating the conversion of PrP^C into PrP^Sc . The accumulation of PrP^Sc in the brain leads to neurodegeneration and the characteristic symptoms of prion diseases .
Recombinant prion proteins are produced using recombinant DNA technology, which involves inserting the gene encoding the prion protein into a suitable expression system, such as bacteria or yeast . This allows for the production of large quantities of the protein for research purposes. Recombinant prion proteins are used to study the structure, function, and pathogenic mechanisms of prion proteins, as well as to develop potential therapeutic strategies .
Research on prion proteins has provided valuable insights into the mechanisms of protein misfolding and aggregation, which are also relevant to other neurodegenerative diseases such as Alzheimer’s and Parkinson’s disease . Understanding the structure and function of prion proteins has led to the development of novel therapeutic strategies aimed at preventing or reversing the misfolding of prion proteins .
