Abstract:
:The human amyloid beta protein (BP) is a major constituent 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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Yamada T,Sasaki H,Dohura K,Goto I,Sakaki Ydoi
10.1016/0006-291x(89)92808-8subject
Has Abstractpub_date
1989-02-15 00:00:00pages
906-12issue
3eissn
0006-291Xissn
1090-2104pii
0006-291X(89)92808-8journal_volume
158pub_type
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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