CD230 or major prion protein (PrP)
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Function
- neuroprotective adaptive cellular response to hypoxia[6]
- prion protein PrPc (CD230) may be receptor for A4 oligomers; PrPc may bind & internalize A4 oligomers[8]
Structure
- glypiated cell-surface glycoprotein
- can occur in 2 structural conformations:
- PrPc (normal, of unknown function) C-terminal domain folded mostly in alpha-helical conformaion (3 alpha helices & a short antiparallel beta-sheet), stabilized by single disulfide bond linking helices 2 & 3
- PrPSc (abnormal protein resulting in disease) PrPSc has high beta-sheet content
Compartment
- associated with synaptic membranes
Expression
- present in most mammalian tissues
- highest levels in CNS
- widely expressed in cells of immune system
Pathology
- the PrPSc protein is extremely stable, resistant to proteolysis, organic solvents & high temperatures
- once formed, it can initiate a chain reaction converting PrPc to the more stable PrPSc
Polymorphism
- polymorphism at codon 129 in coding region of PrP gene (MM, VV, MV) & size of PrP fragment resistant to proteinase K digestion serves as classification for prion diseases
Laboratory
Analysis:[2]
- protein misfolding cyclic amplification (PMCA)
- assay based upon selective binding to plasminogen
- CSF real time quaking-induced conversion assay is the most sensitive & specific test for prion proteins in CSF[9]
More general terms
Additional terms
- bovine spongiform encephalopathy; mad cow disease; BSE
- Creutzfeldt-Jakob [CJ] disease
- fatal familial insomnia
- Gerstmann-Straussler-Scheinker disease
- kuru
- prion
- protein misfolding cyclic amplification (PMCA)
- scrapie
References
- ↑ Stedman's Medical Dictionary 27th ed, Williams & Wilkins, Baltimore, 1999
- ↑ 2.0 2.1 Journal Watch 21(15):125, 2001 Saborio et al Nature 411:810, 2001 Maissen et al Lancet 357:2026, 2001
- ↑ Johnson & Gibbs NEJM 339:1994, 1998
- ↑ Coughey B. Trends in the Biochemical Sciences 26:235, 2001
- ↑ Entrez Gene http://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Retrieve&dopt=Graphics&list_uids=5621
- ↑ 6.0 6.1 McLennan NF et al, Prion protein accumulation and neuroprotection in hypoxic brain damage Am J Pathol 2004, 165:227 PMID: https://www.ncbi.nlm.nih.gov/pubmed/15215178
- ↑ Sanchez-Juan P et al, CSF tests in the differential diagnosis of Creutzfeldt-Jakob disease. Neurology 2006, 67:637 PMID: https://www.ncbi.nlm.nih.gov/pubmed/16924018
Collins SJ et al, Determinants of diagnostice investigation sensitivities across the clinical spectrum of sporadic Creutzfeldt-Jakob disease Brain 2006, 129:2278 PMID: https://www.ncbi.nlm.nih.gov/pubmed/16816392
Cali I et al, Classification of sporadic Creutzfeldt-Jakob disease revisited. Brain 2006, 129:2266 PMID: https://www.ncbi.nlm.nih.gov/pubmed/16923954 - ↑ 8.0 8.1 Lauren J et al. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-oligomers. Nature 2009 Feb 26; 457:1128 PMID: https://www.ncbi.nlm.nih.gov/pubmed/19242475
Cisse M and Mucke L. Alzheimer's disease: A prion protein connection. Nature 2009 Feb 26; 457:1090. PMID: https://www.ncbi.nlm.nih.gov/pubmed/19242462 - ↑ 9.0 9.1 Medical Knowledge Self Assessment Program (MKSAP) 19. American College of Physicians, Philadelphia 2021