Properties of the cellular prion protein expressed in Xenopus oocytes

Neuroreport. 2002 Jul 2;13(9):1229-33. doi: 10.1097/00001756-200207020-00032.

Abstract

The cellular prion protein (PrPC) from different species can be reproducibly expressed in Xenopus oocytes following injection of in vitro transcribed mRNAs. The level of PrPC accumulation increases with the amount of RNA injected and with the duration of incubation. PrPC expressed in oocytes is similar in size and abundance to PrPC protein in mouse brain and >100 ng of PrPC is expressed per oocyte allowing complete experiments to be carried out in single living cells. The protein is glycosylated, fully protease sensitive and expressed on the cell surface. Xenopus oocytes therefore provide a useful model system for the study of prion proteins and their associated disease processes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cricetinae
  • Dose-Response Relationship, Drug
  • Endopeptidases / metabolism
  • Female
  • Gene Expression Regulation / drug effects
  • Gene Expression Regulation / physiology
  • Glycosylation / drug effects
  • Membrane Glycoproteins / drug effects
  • Membrane Glycoproteins / genetics
  • Membrane Glycoproteins / metabolism
  • Mice
  • Models, Animal
  • Molecular Weight
  • Oocytes / cytology
  • Oocytes / drug effects*
  • Oocytes / metabolism
  • PrPC Proteins / biosynthesis*
  • PrPC Proteins / genetics
  • Protein Transport / drug effects
  • Protein Transport / physiology
  • RNA, Messenger / genetics
  • RNA, Messenger / pharmacology*
  • Temperature
  • Xenopus laevis / anatomy & histology
  • Xenopus laevis / genetics
  • Xenopus laevis / metabolism*

Substances

  • Membrane Glycoproteins
  • PrPC Proteins
  • RNA, Messenger
  • Endopeptidases