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Am J Physiol Cell Physiol 281: C1165-C1172, 2001;
0363-6143/01 $5.00
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Vol. 281, Issue 4, C1165-C1172, October 2001

Essential role for extracellular Ca2+ in JNK activation by mechanical stretch in bladder smooth muscle cells

Nobuhiro Kushida, Yukihito Kabuyama, Osamu Yamaguchi, and Yoshimi Homma

Department of Biomolecular Science and Department of Urology, Fukushima Medical University School of Medicine, Fukushima 960-1295, Japan

Mechanical stretch has been implicated in phenotypic changes as an adaptive response to stretch stress physically loaded in bladder smooth muscle cells (BSMCs). To investigate stretch-induced signaling, we examined the mitogen-activated protein kinase (MAPK) family using rat primary BSMCs. When BSMCs were subjected to sustained mechanical stretch using collagen-coated silicon membranes, activation of c-Jun NH2-terminal kinase (JNK) was most relevant among three subsets of MAPK family members: the activity was elevated from 5 min after stretch and peaked at 10 min with an 11-fold increase. Activation of p38 was weak compared with that of JNK, and ERK was not activated at all. JNK activation by mechanical stretch was totally dependent on extracellular Ca2+ and inhibited by Gd3+, a blocker of stretch-activated (SA) ion channels. Nifedipine and verapamil, inhibitors for voltage-dependent Ca2+ channels, had no effect on this JNK activation. Moreover, none of the inhibitors pertussis toxin, genistein, wortmannin, or calphostin C affected stretch-induced JNK activation, indicating that G protein-coupled and tyrosine kinase receptors are unlikely to be involved in this JNK activation. On the other hand, W-7, a calmodulin inhibitor, and cyclosporin A, a calcineurin inhibitor, prevented JNK activation by stretch. These results suggest a novel pathway for stretch-induced activation of JNK in BSMCs: mechanical stretch evokes Ca2+ influx via Gd3+-sensitive SA Ca2+ channels, resulting in JNK activation under regulation in part by calmodulin and calcineurin.

stretch-activated ion channel; calmodulin; cyclosporin A; c-Jun NH2-terminal kinase


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