Tyrosine Kinase Activity Modulates Catalysis and Translocation of Cellular 5-Lipoxygenase (∗)
RA Lepley, DT Muskardin, FA Fitzpatrick - Journal of Biological Chemistry, 1996 - ASBMB
Tyrosine kinase activity, a determinant of Src homology domain interactions, has a
prominent effect on cellular localization and catalysis by 5-lipoxygenase. Six separate
inhibitors of tyrosine kinase each inhibited 5 (S)-hydroxyeicosatetraenoic acid formation by
HL-60 cells stimulated with calcium ionophore, in the presence or absence of exogenous
arachidonic acid substrate, indicating that they modulated cellular 5-lipoxygenase activity.
The tyrosine kinase inhibitors also blocked the translocation of 5-lipoxygenase from cytosol …
prominent effect on cellular localization and catalysis by 5-lipoxygenase. Six separate
inhibitors of tyrosine kinase each inhibited 5 (S)-hydroxyeicosatetraenoic acid formation by
HL-60 cells stimulated with calcium ionophore, in the presence or absence of exogenous
arachidonic acid substrate, indicating that they modulated cellular 5-lipoxygenase activity.
The tyrosine kinase inhibitors also blocked the translocation of 5-lipoxygenase from cytosol …
