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Am J Physiol Renal Physiol (July 8, 2003). doi:10.1152/ajprenal.00378.2002
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Submitted on October 21, 2002
Accepted on June 30, 2003

Obstruction-induced changes in urinary bladder smooth muscle contractility: A role for Rho-kinase

Wu Bing1, Shaohua Chang1, Joseph A. Hypolite2, Michael E. DiSanto2, Stephen A. Zderic3, Lester Rolf4, Alan J. Wein2, and Samuel Chacko5*

1 Department of Pathobiology, University of Pennsylvania, Philadelphia, Pennsylvania, USA
2 Division of Urology, University of Pennsylvania, Philadelphia, Pennsylvania, USA
3 Children's Hospital of Philadelphia, philadelphia, Pennsylvania, USA
4 University Laboratory Animal Resources, University of Pennsylvania, Philadelphia, Pennsylvania, USA
5 Department of Pathobiology, University of Pennsylvania, Philadelphia, Pennsylvania, USA; Division of Urology, University of Pennsylvania, Philadelphia, Pennsylvania, USA

* To whom correspondence should be addressed. E-mail: chackosk{at}mail.med.upenn.edu.

Detrusor smooth muscle (DSM) undergoes hypertrophy following partial bladder outlet obstruction (PBOO) in male rabbits, as it does in men with PBOO induced by benign prostatic hyperplasia. Despite detrusor hypertrophy, some bladders are severely dysfunctional (decompensated). This study used the rabbit model for PBOO to determine the biochemical regulation of the contractile apparatus and force maintenance by the detrusor from decompensated bladders (DB). Bladders from sham-operated rabbits served as a control. Upon stimulation with 125 mM KCl, the DSM from sham-operated (SB) rabbits showed phasic contractions, whereas the detrusor from DB was tonic, exhibiting slow development of force, a longer duration of force maintenance, and slow relaxation. Rho-kinase (ROK) inhibitor Y-27632 enhanced the relaxation of pre-contracted DSM strips from DB. The enhancement of relaxation of the KCl-induced contraction of DB by Y-27632 was associated with dephosphorylation of myosin light chain (MLC20). The DSM extract from DB showed low phosphatase activity compared to that of SB. The DB also showed more Ca2+-independent MLC20 phosphorylation, and this was partially inhibited by Y-27632. RT-PCR and Western blotting revealed similar expression levels of myosin light chain kinase and ROK {alpha} isoform in SB and DB, but ROK-{beta} was over-expressed in the DB. These results suggest that the ROK-mediated pathway is partly responsible for the high degree of force maintenance and slow relaxation seen in the detrusor from DB.




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