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To elucidate the mechanism responsible for this effect we have examined the morphology, dynamics, and cytoskeletal organization of various cultured cells following H\u20107\u2010treatment. We show here that drug treated cells display an enhanced protrusive activity. Focal contact\u2010attached stress fibers and the associated myosin, vinculin, and talin deteriorated in such cells while actin, vinculin, and N\u2010cadherin associated with cell\u2010cell junctions were retained. Furthermore, we demonstrate that even before these cytoskeletal changes become apparent, H\u20107 suppresses cellular contractility. Thus, short pretreatment with H\u20107 leads to strong inhibition of the ATP\u2010induced contraction of saponin permeabilized cells. Comparison of H\u20107 effects with those of other kinase inhibitors revealed that H\u20107\u2010induced changes in cell shape, protrusional activity, and actin cytoskeleton structure are very similar to those induced by selective inhibitor of myosin light chain kinase, KT5926. Specific inhibitors of protein kinase C (Ro31\u20108220 and GF109203X), on the other hand, did not induce similar alterations. These results suggest that the primary effect of H\u20107 on cell morphology, motility, and junctional interactions may be attributed to the inhibition of actomyosin contraction. This effect may have multiple effects on cell behavior, including general reduction in cellular contractility, destruction of stress fibers, and an increase in lamellipodial activity. It is proposed that this reduction in tension also leads to the apparent stability of cell\u2010cell junctions in low\u2010calcium medium. \u00a9 1994 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/cm.970290405","type":"journal-article","created":{"date-parts":[[2005,2,24]],"date-time":"2005-02-24T01:54:11Z","timestamp":1109210051000},"page":"321-338","source":"Crossref","is-referenced-by-count":93,"title":["Effect of protein kinase inhibitor H\u20107 on the contractility, integrity, and membrane anchorage of the microfilament system"],"prefix":"10.1002","volume":"29","author":[{"given":"Tova","family":"Volberg","sequence":"first","affiliation":[]},{"given":"Benjamin","family":"Geiger","sequence":"additional","affiliation":[]},{"given":"Sandra","family":"Citi","sequence":"additional","affiliation":[]},{"given":"Alexander D.","family":"Bershadsky","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2005,2,4]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/0896-6273(93)90226-H"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.117.2.357"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1007\/978-1-4684-5278-5"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.87.5.1884"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1002\/jcp.1041410112"},{"key":"e_1_2_1_7_1","doi-asserted-by":"crossref","first-page":"14565","DOI":"10.1016\/S0021-9258(18)82365-1","article-title":"Cell spreading on extracellular matrix proteins induces tyrosine phosphorylation of tensin","volume":"268","author":"Bockholt S. 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