PrPC Proteins

Normal cellular isoform of prion proteins (PRIONS) encoded by a chromosomal gene and found in normal and scrapie-infected brain tissue, and other normal tissue. PrPC are protease-sensitive proteins whose function is unknown. Posttranslational modification of PrPC into PrPSC leads to infectivity.
Also Known As:
Cp 33-35; Cp33-35, Scrapie; PrP-sen; PrP sen; Scrapie Amyloid Precursor Protein
Networked: 38 relevant articles (0 outcomes, 4 trials/studies)

Bio-Agent Context: Research Results


1. Priola, Suzette A: 7 articles (05/2009 - 09/2002)
2. Caughey, B: 6 articles (08/2002 - 05/2000)
3. Caughey, Byron: 5 articles (04/2012 - 03/2002)
4. Priola, S A: 5 articles (12/2001 - 05/2000)
5. Vorberg, Ina: 3 articles (07/2004 - 09/2002)
6. Xiong, L W: 3 articles (11/2001 - 02/2001)
7. Horiuchi, M: 3 articles (05/2001 - 05/2000)
8. Hughson, Andrew G: 2 articles (04/2012 - 08/2007)
9. Ward, Anne E: 2 articles (05/2009 - 09/2008)
10. Moore, Roger A: 2 articles (08/2007 - 03/2006)

Related Diseases

1. Scrapie
2. Prion Diseases (Transmissible Spongiform Encephalopathies)
3. Neuroblastoma
4. Conversion Disorder (Astasia Abasia)
10/13/1998 - "The inhibition observed in the cell-free conversion reaction suggests that the mechanism involved direct interactions of the tetrapyrrole with PrP-res and/or PrP-sen. "
05/04/2001 - "Mechanistic analyses indicated that Ha166-179, Ha200-223, and peptides containing residues 119-136 inhibit primarily by binding to PrP-sen and blocking its binding to PrP-res. Circular dichroism analyses indicated that Ha117-141 and Ha200-223, but not non-inhibitory peptides, readily formed high beta-sheet structures when placed under the conditions of the conversion reaction. "
06/15/1999 - "Here we describe new, more physiological cell-free systems for analyzing the initial binding and subsequent conversion reactions between PrP-sen and PrP-res. These systems allowed the use of antibodies to map the sites of interaction between PrP-sen and PrP-res. Binding of antibodies (alpha219-232) to hamster PrP-sen residues 219-232 inhibited the binding of PrP-sen to PrP-res and the subsequent generation of PK-resistant PrP. "
08/03/1998 - "The addition of the disulfide reducing agent dithiothreitol inhibited the cell-free conversion reaction with an IC50 of 2-2.5 mM. Separate pretreatment of either PrP-sen or PrP-res with dithiothreitol and an alkylating agent also inhibited the conversion reaction. "
03/01/2002 - "A cell-free conversion reaction approximating physiological conditions was used, which contained purified DRMs as a source of PrP-sen and brain microsomes from scrapie-infected mice as a source of PrP-res. Interestingly, DRM-associated PrP-sen was not converted to PrP-res until the PrP-sen was either released from DRMs by treatment with phosphatidylinositol-specific phospholipase C (PI-PLC), or the combined membrane fractions were treated with the membrane-fusing agent polyethylene glycol (PEG). "
5. Infection

Related Drugs and Biologics

1. PrPSc Proteins
2. Endopeptidase K (Proteinase K)
3. Glycoproteins (Glycoprotein)
4. Phosphoinositide Phospholipase C
5. Small Interfering RNA (siRNA)
6. Porphyrins
7. Polyethylene Glycols (Polyethylene Glycol)
8. Peptides
9. Dithiothreitol (Cleland's Reagent)
10. Detergents (Detergent)