Advertisement

The sequence within the two polyadenylation sites of the A4 amyloid peptide precursor stimulates the translation

  • F. de Sauvage
  • V. Kruys
  • J. N. Octave
Part of the Key Topics in Brain Research book series (KEYTOPICS)

Summary

cDNA probes specific for the A4 amyloid peptide precursor hybridize with a 3.2–3.4 kb mRNA doublet which can be attributed to the use of two polyadenylation sites. Different chimeric mRNAs were synthesized by in vitro transcription of the coding region of the chicken lysozyme or the chloramphenicol acetyl transferase followed by two 3′ untranslated regions of the A4 amyloid peptide precursor mRNA using the two possible polyadenylation sites. In vivo translation of these mRNA constructs in Xenopus oocytes indicates that the long mRNAs using the second polyadenylation site produce higher amounts of proteins as compared to the short mRNAs. This effect on the translation is not related to a higher stability of the long mRNA in oocytes.

Keywords

Down Syndrome Northern Blot Analysis Polyadenylation Site Chimeric RNAs Chicken Lysozyme 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Bahmanyar S, Higgins GA, Godgaber D, Lewis DA, Morrison JH, Wilson MC, Shankar SK, Gajdusek DC (1987) Localization of amyloid ß protein messenger RNA in brains from patients with Alzheimer’s disease. Science 237: 77–80PubMedCrossRefGoogle Scholar
  2. Chirgwin JM, Przybyla AE, MacDonald RJ, Rutter WJ (1979) Isolation of biological active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18: 5294–5299PubMedCrossRefGoogle Scholar
  3. Cohen ML, Golde TE, Usiak MF, Younkin LH, Younkin SG (1988) In situ hybridization of nucleus basalis neurons shows increased ß-amyloid mRNA in Alzheimer disease. Proc Natl Acad Sci USA 85: 1227–1231PubMedCrossRefGoogle Scholar
  4. Goedert M (1988) Neuronal localization of amyloid beta protein precursor mRNA in normal human brain and in Alzheimer’s disease. EMBO J 6: 3627–3632Google Scholar
  5. Gorman CM, Moffat LF, Howards BH (1982) Recombinant genomes which express chloramphenicol acetyl transferase in mammalian cells. Mol Cell Biol 2: 1044–1051PubMedGoogle Scholar
  6. Huez G, Cleuter Y, Bruck C, Van Vloten-Doting L, Goldbach R, Verdiun B (1983) Translational stability of plant viral RNAs microinjected into living cells; influence of a 3’-poly(A) segment. Eur J Biochem 130: 205–209PubMedCrossRefGoogle Scholar
  7. Kang J, Lemaire HG, Unterbeck A, Salbaum MJ, Masters CL, Grzeschik KH, Multhaup G, Beyreuther K, Muller-Hill B (1987) The precursor of Alzheimer’s disease amyloid A4 protein resembles a cell surface receptor. Nature 325: 733–736PubMedCrossRefGoogle Scholar
  8. Lewis DA, Higgins GA, Young WG, Goldgaber D, Gajdusek DC, Wilson MC, Morrison JH (1988) Distribution of precursor amyloid-ß-protein messenger RNA in human cerebral cortex: relationship to neurofibrillary tangles and neuritic plaques. Proc Natl Acad Sci USA 85: 1691–1695PubMedCrossRefGoogle Scholar
  9. Masters CL, Simms G, Weinman NA, Multhaup G, McDonald BL, Beyreuther K (1985) Amyloid plaque core protein in Alzheimer’s disease and Down syndrome. Proc Natl Acad Sci USA 82: 4242–4249CrossRefGoogle Scholar
  10. Palmert MR, Golde TE, Cohen ML, Kovacs DM, Tanzi RE, Gusella JF, Usiak MF, Younkin LH, Younkin SG (1988) Amyloid protein precursor messenger RNAs: differential expression in Alzheimer’s disease. Science 241: 1080–1084PubMedCrossRefGoogle Scholar
  11. Strickland S, Huarte J, Belin D, Vassalli A, Rickles RJ, Vassalli JD (1988) Antisense RNA directed against the 3’ noncoding region prevents dormant mRNA activation in mouse oocytes. Science 241: 680–684PubMedCrossRefGoogle Scholar
  12. Thomas PS (1980) Hybridization of denaturated RNA and small DNA fragments transferred to nitrocellulose. Proc Natl Acad Sci USA 77: 5201–5205PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Wien 1990

Authors and Affiliations

  • F. de Sauvage
    • 1
  • V. Kruys
    • 2
  • J. N. Octave
    • 1
  1. 1.Laboratoire de NeurochimieUniversité Catholique de LouvainBelgium
  2. 2.Université Libre de BruxellesBelgium

Personalised recommendations