Erythroid differentiation and growth inhibition of K562 cells by XXXX : synergism with interferon-alpha.

@entity1 @entity268 @entity5393 @entity2353 @entity10766 @entity13327 @entity6618 @entity517 @entity22818 @entity5536 @entity1919 @entity291 @entity3027 @entity16748
We found that @entity10766 ( @entity22818 ), a P-site specific adenylate cyclase inhibitor, inhibited the growth of K562 cells and caused them to become @entity16748 positive. The continuous exposure of cells to @entity22818 was needed to recruit cells for growth inhibition and differentiation. Fetal @entity291 or @entity1 sera were also necessary for @entity22818 to induce differentiation. @entity22818 at a concentration of 1.5 mM with serum induced 98% of the cells to produce hemoglobin and inhibited their growth to 15% of that of the control. An increase of @entity6618 mRNA and a decrease of @entity517 and @entity13327 mRNA occurred only during differentiation in the presence of fetal calf serum (FCS). An incubation with @entity22818 and interferon-alpha ( @entity3027 ) or hemin synergistically induced more benzidine-positive cells than in the presence of @entity22818 alone, although @entity3027 did not trigger differentiation by itself. The erythroid differentiation and growth inhibition were, however, not related to a decreased intracellular @entity1919 ( @entity268 ) concentration induced by @entity22818 . The simultaneous incubation with @entity5393 ( @entity5393 ) and @entity22818 enhanced the effects of @entity22818 . @entity5536 , a possible metabolite of @entity22818 digestion by purine @entity2353 phosphorylase (PNP), also induced erythroid differentiation in K562 cells. However, it did not act synergistically with @entity3027 .
