2026-07-16T12:49:14Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/272552026-02-21T18:03:57Zcom_20.500.12105_2273com_20.500.12105_2202col_20.500.12105_19571
Repisalud
author
Villa, Ana
author
Santiago, Jorge
author
García-Silva, Susana
author
Ruiz-León, Yolanda
author
Pascual, Angel
2026-02-21T18:03:57Z
2026-02-21T18:03:57Z
2002-10
Neurochem Int . 2002 Oct;41(4):261-9
Neurochem Int
12106777
https://hdl.handle.net/20.500.12105/27255
The beta-amyloid peptide, the major component of the senile plaques that characterize Alzheimer's disease, is generated from a set of alternatively spliced beta-amyloid precursor proteins (APPs), which are proteolytically cleaved by the action of a set of enzymes referred to generically as secretases. The major processing pathway involves the proteolytic cleavage of APP by alpha-secretase and results in the release of soluble non-amyloidogenic full-length amino terminal fragments (sAPP), which appear to be involved in neurotrophic events. A reduced production of these neuroprotective sAPP would contribute, together with deposition of the beta-amyloid peptide, to the neurodegenerative processes that lead to the cellular death in Alzheimer's disease. In the present work, we describe a dramatic reduction of sAPP content in medium conditioned by neuronal cells grown under low-serum conditions, when compared with the levels released in the presence of 10% serum. The inhibitory effect on sAPP release appears to be quite specific since that reduction occurs without major changes in cell proliferation, expression of APP-mRNA or intracellular APP levels. Under low-serum conditions, cells showed a more differentiated morphology and no apoptotic signs were observed. Since the alpha-secretase has been described as a membrane anchored protein, our results suggest that the serum contains an essential factor(s) involved in the alpha-secretase activity.
eng
serum concentration
sAPP release
amyloid precursor protein (APP)
neuroblastoma cells
Serum is required for release of Alzheimer's amyloid precursor protein in neuroblastoma cells.
research article
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