c Abl, which is constitutively active because of the lack of Gly2 needed for myristoylation, firmly stimulated tyrosine phosphorylation weighed against c Abl. While apoptosis was evidently noticed upon adriamycin therapy, immunostaining of cleaved caspase 3, the active kind of caspase 3, showed that neither expression of NLS c Abl natural product library caused apoptosis or did that of c Abl. These results suggest that d Abl caused chromatin structural changes are not related to apoptosis induction. To evaluate the effect of nuclear c Abl with those of the other tyrosine kinases Lyn and Syk on chromatin structural changes, cells were transfected with NLS c Abl, NLS Lyn or NLS Syk. Like NLS cAbl, NLS Syk and both NLS Lyn were local to the nucleus. Intriguingly, nuclear tyrosine phosphorylation mediated by NLS cAbl and NLS Lyn was plainly visualized within the nucleus upon methanol fixation, while NLS Syk mediated nuclear tyrosine phosphorylation was detected only upon paraformaldehyde fixation. Let’s assume that nuclear proteins phosphorylated by NLS Syk are different from these phosphorylated by NLS Lyn and NLS d Abl, the different Metastasis fixation homes, i. e. Coagulates and methanol dehydrates biomacromolecules but paraformaldehyde crosslinks them, might explain why the 2 fixation methods gave different results. More over, unlike NLS Syk, NLS c Abl and NLS Lyn induced a similar group pattern of tyrosine phosphorylation, but NLS Lyn and NLS Syk mediated tyrosine phosphorylations were not inhibited by therapy. Quantitative analyses showed that NLS Lyn and NLS c Abl similarly induced powerful chromatin structural changes but NLS Syk did not and imatinib treatment particularly restricted NLS c Abl induced chromatin structural changes. These results claim that induction of chromatin structural changes is a prominent feature of nuclear tyrosine potent FAAH inhibitor phosphorylation mediated by nuclear c Abl besides nuclear Lyn. Histone modifications by nuclear h Abl It is known that regulation of chromatin structure requires histone modifications, such as methylation and acetylation. To look at the connection between nuclear c Abl mediated chromatin structural adjustments and histone modifications, cells were transfected with NLS c Abl and stained for H3K9Me3, which really is a heterochromatic histone modification. Immunostaining confirmed that H3K9Me3 was localized to hypercondensed heterochromatic parts, and that appearance of NLS d Abl increased the degrees of fluorescence intensity of anti H3K9Me3 antibody. 2D piece analyses showed that the degrees of H3K9Me3 definitely correlated with those of chromatin structural changes. Then, cells were stained for H4Ac, H3K14Ac, H3K4Me3 and H4K16Ac, the majority of which were known as euchromatic histone marks.