Divergent changes of chromogranin A/secretogranin II levels in differentiating human neuroblastoma cells

Abstract

Human neuroblastoma cells were cultured either in the absence or presence of 12-O-tetradecanoylphorbol-13-acetate (TPA) known to induce neuronal differentiation. This treatment led to a marked increase in the concentration of secretogranin II but to a decrease of chromogranin A. Analogous changes were observed for the respective mRNAs. Thus during differentiation of these cells the biosynthesis of two vesicle constituents of large dense core vesicles is differentially regulated as determined both at the mRNA and the protein level. Levels of both synaptin/synaptophysin and SV2 were also elevated but to a smaller degree than that of secretogranin II.

Mutual relationships between chromogranins A and B and gastrin in individual gastrin cells.

“…As a consequence, the intercellular differences of immunoreactivities ascertained are related to differences in the relative amounts of gastrin, CgA, and CgB among G-cells. With respect to the remarkable correlations ofimmunoreactivities, it is obvious that under in situ conditions the storage of gastrin, CgA, and CgB in G-cells is regulated in a sophisticated way (38) Moreover, the conclusions to be drawn from available in vitro studies on Cg biosynthesis depend largely on the properties of the secretagogues (12,23), the type of cultured cells (13,14,40,42), or the duration ofculture time ofa given cell culture (12,43).…”

Insulin-like growth factor I shifts from promoting cell division to potentiating maturation during neuronal differentiation.

“…SH-SY5Y cells are adrenergic, and the concentrations of noradrenalin and secretogranin II and the number of large dense-core vesicles increase dramatically following PMAinduced differentiation (7,23). NPY is expressed in a large population of sympathetic ganglion cells (24) and is stored in large dense-core vesicles, mainly together with noradrenalin (25).…”

Chromogranin A: current status as a precursor for bioactive peptides and a granulogenic/sorting factor in the regulated secretory pathway

“…a Rat adrenal medulla, [37]; b rat anterior pituitary, [38,154] c rat adrenal medulla, [50]; a AtT20, [45]; e bovine chromaffin cells [25]; f PC12 cells, [155]; g parathyroid cells [47]; h rat pituitary and pituitary cells in culture (decrease in CGA and SglI mRNA), [33,34]; i rat pituitary (decrease in CGA, slight increase in CGB and SglI mRNA), [35]; J rat pituitary, increases with estrogen, decrease with dexamethasone in CGB mRNA, [156]; k parathyroid [40]; i rat adrenal, [37]; m rat adrenal, [50]; n bovine chromaffin cells (slight increase in CGA mRNA with forskolin treatment after 48 h, decrease with PMA alone and block of dexamethasone increase by PMA), [25]; o bovine chromaffin cells (no change in CGA mRNA after potassium or nicotine depolarizationi slight but not significant increase in CGA mRNA after 24 h with forskolin; increased SglI mRNA after 24 h with forskolin and potassium) [50]; p PC12 cells, no change in CGA or SglI mRNA with forskolin or PMA and increased CGB mRNA after both forskolin and PMA, [55]; q bovine chromaffin cells, CGB mRNA: occasional slight increase with K ÷, slight increase forskolin, no change after PMA treatment, C.-M. Hsu, L. Eiden, unpublished observations; r PC12 cells, increase in CGB mRNA and decrease in SglI mRNA after treatment with forskolin or 8-Br-cAMP, [157,158]; s rat insulinoma (RIN cells), CGA mRNA: no change after forskolin, blockade of dexamethasone induction with PMA but no effect of PMA alone, [25]; t SK-N-SH human neuroblastoma cells, decreased CGA mRNA after PMA, S.-H. Hahm, L. Eiden and A. lacangelo, unpublished observations; u SY-5Y human neuroblastoma cells, decreased CGA mRNA and increased SgII mRNA after PMA, [52]; v bovine chromaffin cells, no significant change in CGB or CGA mRNA after K ÷, [41].…”

“…Also in contrast to CGA and CGB, SglI is up-regulated by stimulation of the protein kinase C pathway in bovine chromaffin and human neuroblastoma cells [50,52]. Regulation by protein kinase C may be either cell-or species-specific, since Laslop and co-workers [55] reported that PMA stimulation of PC12 cells did not result in the up-regulation of SglI mRNA (Table 1).…”