Disease relevance of prnp

• The mechanism governing the alternative fates of nascent PrP remains to be elucidated but may have significance for understanding the pathogenesis of scrapie and other prion diseases [1].

High impact information on prnp

• These results identify an unexpected functional domain for stop transfer in the prion protein and have implications for the mechanism of membrane protein biogenesis [2].
• The amino acid sequences of these prion proteins show approximately 30% identity with mammalian prion proteins [3].
• SP6 PrP RNA microinjected into Xenopus oocytes produced two forms of PrP: one that remained in the cell and another that was secreted into the medium [1].
• Earlier studies in the wheat germ cell-free system showed that one form of PrP is a transmembrane protein that spans the bilayer at least twice [Hay, B., Barry, R. A., Lieberburg, I., Prusiner, S. B., & Lingappa, V. R. (1987) Mol. Cell. Biol. 7, 914-920] [1].
• Cell-free translation studies in rabbit reticulocyte lysates supplemented with microsomal membranes gave similar results: while one form of PrP was found as an integral membrane protein spanning the membrane at least twice, another form of PrP was found to be completely translocated to the microsomal membrane vesicle lumen [1].

Biological context of prnp

• PrP transcripts were maternally expressed and detected throughout embryonic development, most strongly from neurulation onwards and including the tadpole stage [4].
• Cell type-specific transgene expression of the prion protein in Xenopus intermediate pituitary cells [5].

Anatomical context of prnp

• In adult frogs, PrP mRNA expression was observed in all tissues examined, with high expression in brain, pituitary and testis [4].
• The cellular form of prion protein (PrPC) is anchored to the plasma membrane of the cell and expressed in most tissues, but predominantly in the brain, including in the pituitary gland [5].

Associations of prnp with chemical compounds

• Other features worth noting are the presence of not perfectly conserved hydrophobic stretch, which is considered the prion signature, as well as the complete absence of histidine residues [6].
• This glutamine-rich region behaves in a similar manner as TIA-1 and prion protein, two molecules with known roles in protein aggregation [7].

Analytical, diagnostic and therapeutic context of prnp

• Molecular cloning of the cDNA coding for Xenopus laevis prion protein [6].
• Microinjection of PrP mRNA into fertilized Xenopus eggs did not affect early embryonic development [4].

References