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Neurochem Int. 1989;14(2):163-6. doi: 10.1016/0197-0186(89)90117-4.

Identification of different ? amyloid cDNAs cloned from the brain of a patient with sporadic alzheimer's disease.

Neurochemistry international

J N Octave, F De Sauvage, A F Macq, J M Maloteaux, E C Laterre

Affiliations

  1. Université Catholique de Louvain, Laboratoire de Neurochimie, Avenue Hippocrate 10, B-1200 Brussels, Belgium.

PMID: 20504413 DOI: 10.1016/0197-0186(89)90117-4

Abstract

Neurofibrillary tangles and senile plaques, two neuropathological markers of Alzheimer's disease, may both contain peptide fragments derived from the ? amyloid protein. Human ? amyloid peptide precursor cDNAs have been isolated from normal foetal and adult brain libraries. In peripheral tissue and cultured cells, a novel precursor containing a protease inhibitor domain has been cloned. A cDNA library from the cerebral cortex of a patient with sporadic Alzheimer's disease was constructed and several clones coding for the ? amyloid peptide precursor were isolated cDNAs containing two types of insertion coding for a serine protease inhibitor domain were identified. The use of another polyadenylation site available in the 3?-untranslated region of the mRNA was observed. These results indicate that, in one patient with Alzheimer's disease, different RNA species coding for the ? amyloid peptide precursor arise by alternative splicing of a single transcriptional unit, and use different polyadenylation sites.

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