Structure and expression of the alternatively-spliced forms of mRNA for the mouse homolog of Alzheimer's disease amyloid beta protein precursor

Takeshi Yamada, Hiroyuki Sasaki, Katsumi Dohura, Ikuo Goto, Yoshiyuki Sakaki

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Abstract

The human amyloid β protein (BP) is a major constitutent of the amyloid deposited in the brain of patients with Alzheimer's disease and is derived from a larger precursor protein (BPP). In human three alternatively-spliced forms of BPP mRNA were found and two of them were shown to encode a protease inhibitory activity. We have isolated the corresponding species of cDNA in mice and found that the inhibitor domain is highly conserved through mammalian evolution. The homology between human and mouse was 94.6%. Northern blot using specific probes showed that the mRNA for BPP with inhibitor domain was present in every tissue, particularly at a higher level in the kidney. On the other hand, that without inhibitor domain was found most abundantly in the brain but much less in the kidney and the intestine. These data suggest that the individual BPP mRNA species were produced in a tissue-specific manner in mouse as in the case of human.

Original languageEnglish
Pages (from-to)906-912
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume158
Issue number3
DOIs
Publication statusPublished - Feb 15 1989
Externally publishedYes

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All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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