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cDNA isolation of Alzheimer's amyloid precursor protein from cholinergic nerve terminals of the electric organ of the electric ray.
- Source :
-
The Biochemical journal [Biochem J] 1998 Feb 15; Vol. 330 ( Pt 1), pp. 29-33. - Publication Year :
- 1998
-
Abstract
- Alzheimer's amyloid precursor protein (APP) is a transmembrane protein containing three phosphorylation sites in its cytoplasmic domain. In the present study, we isolated cDNA of APP from electric ray electric lobe (elAPP). This APP (elAPP699) consists of 699 amino acids, contains the beta-amyloid domain and has 80.7% similarity with the human APP695 isoform. The cytoplasmic domain, including three phosphorylation sites, was completely conserved. In the nerve terminals of the cholinergic neuron from the electric ray electric organ, we found elAPP699 existed exclusively in the mature form. We found the phosphorylated form of mature elAPP699 in the nerve terminal as well as in cell body. Immature elAPP699 was not subject to phosphorylation. Our findings indicate that, in neurons, the phosphorylation of APP occurs after maturation.
- Subjects :
- Amino Acid Sequence
Animals
Base Sequence
Cell Compartmentation
Cholinergic Fibers chemistry
Cloning, Molecular
DNA, Complementary isolation & purification
Glycosylation
Humans
Molecular Sequence Data
Phosphorylation
Sequence Alignment
Sequence Homology, Amino Acid
Amyloid beta-Protein Precursor genetics
Electric Organ chemistry
Torpedo genetics
Subjects
Details
- Language :
- English
- ISSN :
- 0264-6021
- Volume :
- 330 ( Pt 1)
- Database :
- MEDLINE
- Journal :
- The Biochemical journal
- Publication Type :
- Academic Journal
- Accession number :
- 9461486
- Full Text :
- https://doi.org/10.1042/bj3300029