R. Fukuyama et al., INDUCTION OF GENE-EXPRESSION OF AMYLOID PRECURSOR PROTEIN (APP) IN ACTIVATED HUMAN LYMPHOBLASTOID-CELLS AND LYMPHOCYTES, Molecular and chemical neuropathology, 23(2-3), 1994, pp. 93-101
To understand the possible role of amyloid precursor protein (APP) in
human lymphocytes, and the regulation of APP gene expression in this c
ell type, we determined levels of cellular APP protein and of mRNA in
human T-cell-derived Jurkat cells that were treated with lectin, phorb
ol ester, and calcium ionophore. We also related these levels to cell
aggregation and adhesion. Cell-cell aggregation and cell-plastic adhes
ion were observed over a 24-h period after incubating cells for 2 h wi
th phytohemagglutinin or phorbol myristate acetate. Cells treated with
a calcium ionophore showed no aggregation or adhesion. Western blots
indicated no obvious alteration in the level of cellular APP with diff
erent treatments. Northern blots showed a significant transient increa
se of APP mRNA after incubation with the calcium ionophore, whereas ph
orbol ester treatment showed a slight increase of APP mRNA. We analyze
d the level of APP mRNA in human peripheral T cells which had been sep
arated from peripheral lymphocytes. The level increased transiently by
up to threefold after treatment with calcium ionophore plus phorbol e
sters. These data suggest that cell-cell aggregation and cell-matrix a
dhesion by human lymphocytes are not associated with an increased leve
l of cellular APP protein or of mRNA.