The PreA4695precursor protein of Alzheimer's disease A4 amyloid is encoded by 16 exons
- 1 January 1989
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 17 (2) , 517-522
- https://doi.org/10.1093/nar/17.2.517
Abstract
Alzheimer''s disease (AD) is characterized by the cerebral deposition of fibrillar aggregates of the amyloid A4 protein. Complementary DNA''s coding for the precursor of the amyloid A4 protein have been described. In order to identify the structure of the precursor gene relevant clones from several human genomic libraries were isolated. Sequence analysis of the various clones revealed 16 exons to encode the 695 residue precursor protein (PreA4695) of Alzheimer''s disease amyloid A4 protein. The DNA sequence coding for the amyloid A4 protein is interrupted by an intron. This finding supports the idea that amyloid A4 protein arises by incomplete proteolysis of a larger precursor, and not by aberrant splicing.Keywords
This publication has 19 references indexed in Scilit:
- Amyloid β Protein Precursor Is Possibly a Heparan Sulfate Proteoglycan Core ProteinScience, 1988
- Novel precursor of Alzheimer's disease amyloid protein shows protease inhibitory activityNature, 1988
- Protease inhibitor domain encoded by an amyloid protein precursor mRNA associated with Alzheimer's diseaseNature, 1988
- A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitorsNature, 1988
- Primer-Directed Enzymatic Amplification of DNA with a Thermostable DNA PolymeraseScience, 1988
- A cDNA specifying the human amyloid β precursor protein (ABPP) encodes a 95-kDa polypeptideNucleic Acids Research, 1988
- The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptorNature, 1987
- Alzheimer's DiseaseNew England Journal of Medicine, 1986
- DNA sequencing with chain-terminating inhibitorsProceedings of the National Academy of Sciences, 1977
- Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components.The Journal of cell biology, 1975