| Autor: |
Pasternack JM; Division of Neuropathology, Case Western Reserve University, Cleveland, Ohio 44106., Palmert MR, Usiak M, Wang R, Zurcher-Neely H, Gonzalez-De Whitt PA, Fairbanks MB, Cheung T, Blades D, Heinrikson RL, et. al. |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemistry [Biochemistry] 1992 Nov 10; Vol. 31 (44), pp. 10936-40. |
| DOI: |
10.1021/bi00159a038 |
| Abstrakt: |
The 39-43 amino acid beta amyloid protein (A beta) that deposits as amyloid in the brains of patients with Alzheimer's disease (AD) is encoded as an internal sequence within a larger membrane-associated protein known as the amyloid protein precursor (APP). In cultured cells, the APP is normally cleaved within the A beta to generate a large secreted derivative and a small membrane-associated fragment. Neither of these derivatives can produce amyloid because neither contains the entire A beta. Our study was designed to determine whether the soluble APP derivatives in human brain end within the A beta as described in cell culture or whether AD brain produces potentially amyloidogenic soluble derivatives that contain the entire A beta. We find that both AD and control brain contain nonamyloidogenic soluble derivatives that end at position 15 of the A beta. We have been unable to detect any soluble derivatives that contain the entire A beta in either the AD or control brain. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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