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- W2029374989 abstract "The phosphorylation status of fill-length APP (FL-APP) and secreted APP (s-APP) was investigated in stably transfected cells. 32P incorporation was detected in the mature full-length APP both in the absence and presence of phorbol ester. Surprisingly, 32P-phosphate was incorporated in the secreted ectodomain, and this was stable to treatment of the [32P]-phospho-s-APP with a large excess of PNGase F, suggesting that N-linked oligosaccharide sites do not account for phosphate incorporation. Phosphoamino acid analysis of the [32P]-phospho-s-APP resulted in the recovery of [32P]-phosphoserine as the preponderant species. Brefeldin A completely inhibited the release of [32P]-phospho-s-APP, but did not inhibit the incorporation of 32P into the FL-APP, suggesting that phosphorylation occurs early in the central vacuolar pathway. It is possible that ectodomain phosphorylation by a novel luminal or extracellular protein kinase may play a role in regulating the metabolic fate of APP." @default.
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- W2029374989 date "1993-12-01" @default.
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- W2029374989 title "Serine Phosphorylation of the Secreted Extracellular Domain of APP" @default.
- W2029374989 doi "https://doi.org/10.1006/bbrc.1993.2490" @default.
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