NDLI: Isolation of a cDNA clone encoding the leader peptide of prion protein and expression of the homologous gene in various tissues.

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Isolation of a cDNA clone encoding the leader peptide of prion protein and expression of the homologous gene in various tissues.

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Isolation of a cDNA clone encoding the leader peptide of prion protein and expression of the homologous gene in various tissues.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Carp, R. I. Innis, M. A. Robakis, N. K. Rubenstein, R. Sawh, P. R. Wolfe, G. C.
Abstract	We have isolated a hamster cDNA clone representing the coding sequences for the entire precursor of prion protein (PrP) 27-30. This clone encodes a protein of 254 residues and contains an in-frame ATG codon 42 bases upstream from the one previously reported. Analysis of the predicted amino acid sequence suggests that the PrP precursor protein contains an amino-terminal signal sequence, and a membrane-spanning domain in the carboxyl terminus. Cleavage of the signal peptide would produce a mature protein of 232 amino acids. Sequences homologous to the hamster PrP cDNA were detected in hamster, mouse, sheep, human, and rabbit genomes. A related 2.5-kilobase transcript was present in the brain of normal and scrapie-infected rodents. Two homologous transcripts, 2.5 and 1.1 kilobases, were detected in the lung and heart of normal animals. No PrP mRNA was detected in spleen stroma, a tissue known to contain high titers of scrapie. Antisera raised to the 27- to 30-kDa polypeptide detected the PrP in both normal and infected brains but failed to detect this protein in either normal or infected spleens. Homologous mRNA species were detected in human, sheep, and rabbit brain, even though the latter is resistant to scrapie infection. Our data suggest that PrP is not a necessary component of the infectious agent.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	17
Volume Number	83
Language	English
Publisher	National Academy of Sciences
Publisher Date	1986-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Prions Genetics Amino Acid Sequence Animals Cloning, Molecular Cricetinae DNA Gene Expression Regulation Immunosorbent Techniques Immunology Protein Conformation Protein Precursors RNA, Messenger Solubility Species Specificity Tissue Distribution Comparative Study Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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