Literature DB >> 9461486

cDNA isolation of Alzheimer's amyloid precursor protein from cholinergic nerve terminals of the electric organ of the electric ray.

K Iijima1, D S Lee, J Okutsu, S Tomita, N Hirashima, Y Kirino, T Suzuki.   

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.

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Year:  1998        PMID: 9461486      PMCID: PMC1219103          DOI: 10.1042/bj3300029

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  34 in total

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  4 in total

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3.  Alternative Selection of β-Site APP-Cleaving Enzyme 1 (BACE1) Cleavage Sites in Amyloid β-Protein Precursor (APP) Harboring Protective and Pathogenic Mutations within the Aβ Sequence.

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  4 in total

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