Serum is required for release of Alzheimer’s amyloid precursor protein in neuroblastoma cells

In the present study, the release of secreted β-amyloid precursor protein (AβPPs) in response to thrombin stimulation in platelets has been investigated. Incubation of platelets with thrombin produced a concentration-dependent release of AβPPs with a concomitant reduction in the AβPP remaining in the lysates. The response to thrombin was not affected by pretreatment for 15 min with the phospholipase C inhibitor U-73122, with the protein kinase C inhibitor staurosporine, or with hydrogen peroxide (which at the concentrations used affects the phosphoinositide signalling system in human platelets). In contrast, pretreatment with wortmannin and sodium azide reduced the responses to thrombin. These data would suggest that thrombin may cause the release of AβPPs from human platelets via an activation of a phospholipase C-independent pathway. Thrombin-stimulated AβPPs release was also reduced by 4-hydroxynonenal. This finding, if it is a phenomenon also found for CNS cells, could be of relevance to the pathogenesis of Alzheimer's disease, given that an accumulation of 4-hydroxynonenal is found in this disease.

Effects of staurosporine, U-73122, wortmannin, 4-hydroxynonenal and sodium azide upon the release of secreted beta-amyloid precursor protein from human platelets in response to thrombin stimulation.

Effects of sodium azide on the secretion of soluble amyloid-β precursor protein and the accumulation of β-amyloid(1–40) in cultured chick neurons

Serum-dependent effects of tamoxifen and cannabinoids upon C6 glioma cell viability.

The metabolism of amyloid precursor protein (A beta PP) in chick neurons cultured in serum-free medium is described. A beta PP immunoreactivity, detected with the 22C11 antibody, was seen at approximately 135 and approximately 120 kDa. A beta PPs (approximately 120 kDa) was released from the cells and could be detected in the culture medium without the need of a purification step. The content of A beta PPs increased with time after medium change, but was not affected by either carbachol (100 microM), glutamate (50 microM), veratrine (20 microM), oleic acid (200 microM), A23187 (5 microM), phorbol 12, 13-dibutyrate (PDBu, 1 microM), staurosporine (1 microM), Go 6976 (1 microM) or okadaic acid (50 nM) although the combination of PDBu and okadaic acid reduced the secretion. Addition of the muscarinic receptor agonist carbachol to the neurons increased the rate of phosphoinositide breakdown. In Western blot experiments using antibodies to the alpha, beta II and epsilon isoforms of protein kinase C and conditions whereby robust signals could be seen with rat brain lysates, no immunoreactive bands that could be inhibited by appropriate positive control peptides were seen. It is concluded A beta PPs production by chick neurons in culture is mainly constitutive in nature.

The secretion of soluble amyloid beta precursor protein (A beta PPs) by chick neurons in serum-free primary culture is not regulated by protein kinase C.

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The secretion of soluble amyloid beta precursor protein (A beta PPs) by chick neurons in serum-free primary culture is not regulated by protein kinase C.