1415 RHO KINASE-SIGNALING IN THE HUMAN PROSTATE DOES NOT INVOLVE EZRIN/RADIXIN/MOESIN, ADDUCIN, OR LIM KINASE

Abstract

You have accessJournal of UrologyBenign Prostatic Hyperplasia: Basic Research1 Apr 20101415 RHO KINASE-SIGNALING IN THE HUMAN PROSTATE DOES NOT INVOLVE EZRIN/RADIXIN/MOESIN, ADDUCIN, OR LIM KINASE Frank Strittmatter, Christian Gratzke, Boris Schlenker, Philipp Weinhold, Christian G. Stief, and Martin Hennenberg Frank StrittmatterFrank Strittmatter More articles by this author , Christian GratzkeChristian Gratzke More articles by this author , Boris SchlenkerBoris Schlenker More articles by this author , Philipp WeinholdPhilipp Weinhold More articles by this author , Christian G. StiefChristian G. Stief More articles by this author , and Martin HennenbergMartin Hennenberg More articles by this author View All Author Informationhttps://doi.org/10.1016/j.juro.2010.02.1107AboutPDF ToolsAdd to favoritesDownload CitationsTrack CitationsPermissionsReprints ShareFacebookTwitterLinked InEmail INTRODUCTION AND OBJECTIVES Rho kinase is an important mediator of contraction and proliferation in prostatic smooth muscle cells. Here, we investigated, whether ezrin/radixin/moesin (“ERM proteins”), adducin or LIM kinase are substrates and suitable markers of Rho kinase in the human prostate. METHODS Human prostate tissue was obtained from 5 patients underoing radical prostatectomies. The effect of the Rho kinase inhibitor Y27632 on prostate tone was tested in myographic measurements (n=5). The effect of Y27632 on the phosphorylation state of putative Rho kinase substrates was investigated by Western blot analysis with phospho-specific antibodies after incubation (45 minutes) of prostate tissue with Y27632 (10 or 30 μM) and solvent (n=5). RESULTS In myographic measurements, the resting tone of prostate strips was reduced by Y27632 (from 0.503+/-0.004 g to 0.315+/-0.061 g, p<0.02), indicating the presence and constitutive activity of Rho kinase, the effectiveness of Y27632, and substantial regulation of prostate tone by Rho kinase. The phosphorlyation state of the ERM proteins ezrin (threonine 567), radixin (threonine 564), and moesin (threonine 558) remained unaltered by Y27632 (phospho-ERM was 157+/-32% after 10 μM Y27632 and 262+/-91% after 30 μM Y27632 compared to solvent, phospho-moesin was 100+/-22% after 10 μM Y27632 and 119+/-29% after 30 μM Y27632 compared to solvent). Likewise, Y27632 did not change the state of adducin phosphorylation at threonine 448, or of LIM kinase-1/2 phosphorylation at threonines 508/505 (phospho-adducin was 184+/-23% after 10 μM Y27632 and 181+/-31% after 30 μM Y27632 compared to solvent, phospho-LIM kinase-1/2 was 118+/-56% after 10 μM Y27632 and 116+/-28% after 30 μM Y27632 compared to solvent). CONCLUSIONS Rho kinase is an important regulator of human prostatic smooth muscle, raising the need for suitable markers of prostatic Rho kinase activity. Futher studies are required to evaluate the prostate-specific regulation of Rho kinase, which differs from Rho kinase regulation in other smooth muscle types. Munich, Germany© 2010 by American Urological Association Education and Research, Inc.FiguresReferencesRelatedDetails Volume 183Issue 4SApril 2010Page: e546 Peer Review Report Advertisement Copyright & Permissions© 2010 by American Urological Association Education and Research, Inc.MetricsAuthor Information Frank Strittmatter More articles by this author Christian Gratzke More articles by this author Boris Schlenker More articles by this author Philipp Weinhold More articles by this author Christian G. Stief More articles by this author Martin Hennenberg More articles by this author Expand All Advertisement Advertisement PDF downloadLoading ...