Protein kinase inhibitor H-7

The protein kinase inhibitor H-7 potently and directly inhibits rabbit brain protein kinase C (K_i = 6.0 μM) and rabbit skeletal muscle cAMP-dependent protein kinase (K_i = 3.0 μM), but exhibits weak activity against other purified protein kinases and ATPases from multiple species and tissues^[1].
Protein kinase inhibitor H-7 (10-50 μM; 2 min preincubation) dose-dependently inhibits protein kinase C-mediated phosphorylation of the 40K protein in intact washed rabbit platelets, but does not inhibit Ca²⁺-calmodulin-mediated phosphorylation of the 20K protein in the same cellular system even at a concentration of 50 μM^[2].
The protein kinase inhibitor H-7 (100-300 μM) enhances lamellipodial protrusive activity and reduces cell polarity in Swiss 3T3 fibroblasts and SVT2 transformed fibroblasts, which is manifested by a significant increase in dispersion value and a significant decrease in elongation value^[3].
The protein kinase inhibitor H-7 (300 μM; 10-30 min) disrupts stress fibers and focal adhesion-related proteins (myosin, vinculin, talin) in chicken lens cells, while preserving intercellular adherens junctions, and these cytoskeletal changes are fully reversible after removal of H-7^[3].
When used as a pretreatment, the protein kinase inhibitor H-7 (300 μM; 10-15 min pretreatment, or added during permeabilization/contraction) potently inhibits ATP-induced contraction in Saponin (HY-100597)-permeabilized Swiss 3T3 fibroblasts, chicken lens cells and chicken embryo fibroblasts, but only weakly inhibits contraction when added to permeabilized cells^[3].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.