| Autor: |
T V, Ramabhadran, S E, Gandy, J, Ghiso, A J, Czernik, D, Ferris, R, Bhasin, D, Goldgaber, B, Frangione, P, Greengard |
| Rok vydání: |
1993 |
| Předmět: |
|
| Zdroj: |
The Journal of biological chemistry. 268(3) |
| ISSN: |
0021-9258 |
| Popis: |
The predominant component of amyloid plaques of Alzheimer's disease is the amyloid beta protein (A beta), a 39-42-amino-acid peptide derived by proteolysis of a family of precursors known as amyloid precursor proteins (APP). In mammalian brain and in cultured mammalian cells, the release of APP amino-terminal fragments into the extracellular medium occurs by a proteolytic cleavage within the A beta domain, thereby precluding amyloidogenesis. Infection of Sf9 insect cells with baculovirus vectors containing APP cDNAs results in high levels of APP expression. The concomitant release of amino-terminal fragments of APP and the production of carboxyl-terminal, cell-associated cleavage products are observed. Here we demonstrate by direct protein microsequencing that the proteolytic processing of APP in the Sf9 cells generates a prominent carboxyl-terminal species that is identical to that produced in human cells, suggesting that the major pathway for proteolytic processing of APP is conserved among metazoans. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
|
