{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T08:20:49Z","timestamp":1790065249466,"version":"4.0.1"},"reference-count":50,"publisher":"Oxford University Press (OUP)","issue":"6","license":[{"start":{"date-parts":[[2013,6,1]],"date-time":"2013-06-01T00:00:00Z","timestamp":1370044800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2013,6,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:sec><jats:title>Introduction<\/jats:title><jats:p>Activated RhoA\/Rho kinase (ROCK) has been implicated in diabetes-induced erectile dysfunction. Earlier studies have demonstrated involvement of ROCK pathway in the activation of arginase in endothelial cells. However, signaling pathways activated by ROCK in the penis remain unclear.<\/jats:p><\/jats:sec><jats:sec><jats:title>Aim<\/jats:title><jats:p>We tested whether ROCK and p38 MAPK are involved in the elevation of arginase activity and subsequent impairment of corpora cavernosal (CC) relaxation in diabetes.<\/jats:p><\/jats:sec><jats:sec><jats:title>Methods<\/jats:title><jats:p>Eight weeks after streptozotocin-induced diabetes, vascular functional studies, arginase activity assay, and protein expression of RhoA, ROCK, phospho-p38 MAPK, p38 MAPK, phospho-MYPT-1Thr850, MYPT-1 and arginase levels were assessed in CC tissues from nondiabetic wild type (WT), diabetic (D) WT (WT\u2009+\u2009D), partial ROCK 2+\/\u2212 knockout (KO), and ROCK 2+\/\u2212 KO\u2009+\u2009D mice.<\/jats:p><\/jats:sec><jats:sec><jats:title>Main Outcome Measures<\/jats:title><jats:p>The expression of RhoA, ROCK 1 and 2, phosphorylation of MYPT-1Thr850 and p38 MAPK, arginase activity\/expression, endothelial- and nitrergic-dependent relaxation of CC was assayed.<\/jats:p><\/jats:sec><jats:sec><jats:title>Results<\/jats:title><jats:p>Diabetes significantly reduced maximum relaxation (Emax) to both endothelium-dependent acetylcholine (WT\u2009+\u2009D: Emax; 61\u2009\u00b1\u20094% vs. WT: Emax; 75\u2009\u00b1\u20092%) and nitrergic nerve stimulation. These effects were associated with increased expression of active RhoA, ROCK 2, phospho-MYPT-1Thr850, phospho-p38 MAPK, arginase II, and activity of corporal arginase (1.6-fold) in WT diabetic CC. However, this impairment in CC of WT\u2009+\u2009D mice was absent in heterozygous ROCK 2+\/\u2212 KO\u2009+\u2009D mice for acetylcholine (Emax: 80\u2009\u00b1\u20095%) and attenuated for nitrergic nerve-induced relaxation. CC of ROCK 2+\/\u2212 KO\u2009+\u2009D mice showed much less ROCK activity, did not exhibit p38 MAPK activation, and had reduced arginase activity and arginase II expression. These findings indicate that ROCK 2 mediates diabetes-induced elevation of arginase activity. Additionally, pretreatment of WT diabetic CC with inhibitors of arginase (ABH) or p38 MAPK (SB203580) partially prevented impairment of ACh- and nitrergic nerve-induced relaxation and elevation of arginase activity.<\/jats:p><\/jats:sec><jats:sec><jats:title>Conclusion<\/jats:title><jats:p>ROCK 2, p38 MAPK and arginase play key roles in diabetes-induced impairment of CC relaxation.<\/jats:p><\/jats:sec>","DOI":"10.1111\/jsm.12134","type":"journal-article","created":{"date-parts":[[2013,4,8]],"date-time":"2013-04-08T16:51:11Z","timestamp":1365439871000},"page":"1502-1515","source":"Crossref","is-referenced-by-count":50,"title":["Activated Rho Kinase Mediates Diabetes-Induced Elevation of Vascular Arginase Activation and Contributes to Impaired Corpora Cavernosa Relaxation: Possible Involvement of p38 MAPK Activation"],"prefix":"10.1093","volume":"10","author":[{"given":"Haroldo A.","family":"Toque","sequence":"first","affiliation":[{"name":"Department of Pharmacology & Toxicology \u00a0 , Augusta, GA , USA"},{"name":"Georgia Health Sciences University \u00a0 , Augusta, GA , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kenia P.","family":"Nunes","sequence":"additional","affiliation":[{"name":"Department of Physiology \u00a0 , Augusta, GA , USA"},{"name":"Georgia Health Sciences University \u00a0 , Augusta, GA , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lin","family":"Yao","sequence":"additional","affiliation":[{"name":"Department of Pharmacology & Toxicology \u00a0 , Augusta, GA , USA"},{"name":"Georgia Health Sciences University \u00a0 , Augusta, GA , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James K.","family":"Liao","sequence":"additional","affiliation":[{"name":"Department of Cardiology \u00a0 , Chicago, IL , USA"},{"name":"University of Chicago Medicine \u00a0 , Chicago, IL , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R. Clinton","family":"Webb","sequence":"additional","affiliation":[{"name":"Department of Pharmacology & Toxicology \u00a0 , Augusta, GA , USA"},{"name":"Georgia Health Sciences University \u00a0 , Augusta, GA , USA"},{"name":"Department of Physiology \u00a0 , Augusta, GA , USA"},{"name":"Georgia Health Sciences University \u00a0 , Augusta, GA , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ruth B.","family":"Caldwell","sequence":"additional","affiliation":[{"name":"Department of Cell Biology and Anatomy \u00a0 , Augusta, GA , USA"},{"name":"Georgia Health Sciences University \u00a0 , Augusta, GA , USA"},{"name":"Vascular Biology Center \u00a0 , Augusta, GA , USA"},{"name":"Georgia Health Sciences University \u00a0 , Augusta, GA , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R. 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