The kinase dead mutant retains the ability to induce P210^BCR-ABL–mediated elevated adhesion.

(A) The profile of a typical spin using K1176R () expressing 32D cells is depicted along with pK1 control cells for comparison (●). (–●–) represents a curve fitted to the experimental points for K1176R while (–○–) represent a curve fitted to the experimental points for pK1 cells. (B) The critical shear stress was calculated for a series of spins using 2 independent populations of cells (left, right) expressing pK1 (n = 12 from Figure 2B, n = 8) or K1176R (n = 18, n = 9) and shows that adhesion is increased in the absence of kinase activity (P < .001,P = .003). Nonspecific binding between K1176R 32D cells to BSA matrices was minimal and similar to pK1 32D control cells (data not shown). (C) Measurement of α₄β₁- and α₅β₁-integrin expression in transduced cells 32D. Surface expression of α₄- and α₅-integrin subunits (corresponding to the α₄β₁ and α₅β₁integrins that bind fibronectin) in pK1-, P210^BCR-ABL–, or K1176R-transduced cells 32D are displayed. Cells stained with the secondary phycoerythrin-conjugated antibody alone are shown as negative controls. The studies were performed in triplicate, and the MFI and SDs are shown. Representative histograms showing the level of integrin expression are presented.