{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,11]],"date-time":"2026-04-11T18:46:49Z","timestamp":1775933209590,"version":"3.50.1"},"reference-count":42,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2005,2,4]],"date-time":"2005-02-04T00:00:00Z","timestamp":1107475200000},"content-version":"vor","delay-in-days":5878,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cell Motil. Cytoskeleton"],"published-print":{"date-parts":[[1989,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The latrunculins are architecturally novel marine compounds isolated from the Red Sea sponge <jats:italic>Latrunculia magnifica<\/jats:italic>. In vivo, they alter cell shape, disrupt microfilament organization, and inhibit the microfilament\u2010mediated processes of fertilization and early development. In vitro, latrunculin A was recently found to affect the polymerization of pure actin in a manner consistent with the formation of a 1:1 molar complex with G\u2010actin. These in vitro effects as well as previous indications that the latrunculins are more potent than the cytochalasins suggest differences in the in vivo mode of action of the two clases of drugs. To elucidate these differences we have compared the short\u2010 and long\u2010term effects of latrunculins on cell shape and actin organization to those of cytochalasin D. Exposure of hamster fibroblast NIL8 cells for 1\u20133 hr to latrunculin A, latrunculin B, and cytochalasin D causes concentration\u2010dependent changes in cell shape and actin organization. However, the latrunculin\u2010induced changes were strikingly different from those induced by cytochalasin D. Furthermore, while initial effects were manifest with both latrunculin A and cytochalasin D already at concentrations of about 0.03 \u03bcg\/ml, latrunculin A caused complete rounding up of all cells at 0.2 \u03bcg\/ml, whereas with cytochalasin D maximum contraction was reached at concentrations 10\u201320 times higher. The short\u2010term effects of latrunculin B were similar to those of latrunculin A although latrunculin B was slightly less potent. All three drugs inhibited cytokinesis in synchronized cells, but their long\u2010term effects were markedly different. NIL8 cells treated with latrunculin A maintained their altered state for extended periods. In contrast, the effects of cytochalasin D progressed with time in culture, and the latrunculin B\u2010induced changes were transient in the continued presence of the drug. These transient effects were found to be due to a gradual inactivation of latrunculin B by serum and were used to compare recovery patterns of cell shape and actin organization in two different cell lines. This comparison showed that the transient effects of latrunculin B were fully reversible for the NIL8 cells and not for the mouse neuroblastoma N1E\u2010115 cells.<\/jats:p>","DOI":"10.1002\/cm.970130302","type":"journal-article","created":{"date-parts":[[2005,2,24]],"date-time":"2005-02-24T03:36:58Z","timestamp":1109216218000},"page":"127-144","source":"Crossref","is-referenced-by-count":485,"title":["Latrunculins\u2014novel marine macrolides that disrupt microfilament organization and affect cell growth: I. Comparison with cytochalasin D"],"prefix":"10.1002","volume":"13","author":[{"given":"Ilan","family":"Spector","sequence":"first","affiliation":[]},{"given":"Nava R.","family":"Shochet","sequence":"additional","affiliation":[]},{"given":"Dina","family":"Blasberger","sequence":"additional","affiliation":[]},{"given":"Yoel","family":"Kashman","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":"10.1083\/jcb.76.2.360"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-4827(81)90038-0"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(76)90233-3"},{"key":"e_1_2_1_5_1","doi-asserted-by":"crossref","first-page":"9982","DOI":"10.1016\/S0021-9258(19)86660-7","article-title":"Substoichiometric concentrations of cytochalasin D inhibit actin polymerization","volume":"254","author":"Brenner S. 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