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1 Department of Surgery, Yale University School of Medicine, New Haven, Connecticut 06510; and 2 First Department of Surgery, Asahikawa Medical College, Asahikawa, Japan 078-8510
The p38/mitogen-activated protein (MAP)
kinase-activated protein kinase 2 (MAPKAP kinase 2)/heat shock protein
(HSP)25/27 pathway is thought to play a critical role in actin
dynamics. In the present study, we examined whether p38 was involved in the morphological changes seen in endothelial cells (EC) exposed to
shear stress. Cultured bovine aortic EC were subjected to 14 dyn/cm2 laminar steady shear stress. Peak activation of
p38, MAPKAP kinase 2, and HSP25 were sixfold at 5 min, sixfold at 5 min, and threefold at 30 min compared with static control,
respectively. SB-203580 (1 µM), a specific inhibitor of p38,
abolished the activation of MAPKAP kinase 2 and HSP25 as well as EC
elongation and alignment in the direction of flow elicited by shear
stress. The mean orientation angle of cells subjected to shear without
SB-203580, with SB-203580, or static control were 17, 50, and 43°,
respectively (P < 0.05). EC transfected with the
dominant negative mutant of p38-
aligned randomly with no stress
fiber formation despite exposure to shear stress. These data suggests
that the pathway of p38/MAPKAP kinase 2/HSP25/27 is activated in
response to shear stress, and this pathway plays an important role in
morphological changes induced by shear stress.
mitogen-activated protein kinase; heat shock protein; actin; reorientation
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