Isolation and expression of multiple forms of beta amyloid protein precursor cDNAs.

R. J. Donnelly, J. S. Jacobsen, C. G. Rasool, A. J. Blume, M. P. Vitek

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Alzheimer's disease (AD) is associated with the extra-normal accumulation of a 42 amino acid (aa) beta-amyloid peptide (BAP) in amyloid plaques and cerebrovascular deposits. Though BAP is deposited exclusively in brains of AD and Down syndrome patients, the mRNA encoding the putative precursor to BAP is found in the brain and in peripheral tissues. Using an HL 60 cDNA library, we have isolated two Amyloid Peptide Precursor (APP) cDNAs with sequences that code for proteins containing 751 and 770 aa (APP 751 and APP 770). These longer forms of APP encode a novel region of 56 aa which is homologous to the Kunitz domain of serine protease inhibitors which is not found in the 695 aa form (APP 695) isolated from brain (1). We have examined APP expression at the RNA level using Northern blots and S1 nuclease protection studies in which the lengths, distributions and relative abundances of APP RNAs were assayed. We find that brain, WA 17 cells and NG 108-15 cells contain all three forms of APP RNAs while HL 60 cells, TMT3 cells and AB-1 cells contain predominantly the APP 751 and APP 770 RNAs.

Original languageEnglish (US)
Pages (from-to)925-937
Number of pages13
JournalProgress in clinical and biological research
Volume317
StatePublished - 1989
Externally publishedYes

ASJC Scopus subject areas

  • Medicine(all)

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