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The formation of E-lams was inhibited by the proteintyrosine kinase inhibitors herbimycin A and genistein and augmented by the protein-tyrosine phosphatase inhibitor sodium orthovanadate. Staurosporine treatment induced relocation of tyrosine phosphorylated phospholipase C-\u03b31 (PLC-\u03b31) to the tips of lamellipodia where actin assembly was initiated. Consistent with an involvement of PLC-\u03b31 in E-lam formation, intracellular free calcium (Ca2+) was elevated during the formation of E-lams and conversely, E-lam formation was blocked by intracellular Ca2+ chelation with BAPTA\/AM, but not by extracellular reduction of Ca2+ by EGTA. Notably, glycogen synthase kinase-3\u03b1\/\u03b2 (GSK-3\u03b1\/\u03b2) was activated by staurosporine as evidenced by reduced phosphorylation on Ser-21\/9. Suppression of GSK-3 activity by LiCl2 or by a specific chemical inhibitor, SB-415286, blocked E-lam formation but without altering cell spreading. Furthermore, GSK-3 inhibitors blocked both staurosporine- and EGF-induced keratinocyte migration in scratch-wounded cultures. We propose that GSK-3 plays a crucial role in the formation of long lamellipodia in human keratinocytes and is potentially a central regulatory molecule in epithelial cell migration during wound healing.<\/jats:p>","DOI":"10.1242\/jcs.00693","type":"journal-article","created":{"date-parts":[[2003,8,5]],"date-time":"2003-08-05T00:29:31Z","timestamp":1060043371000},"page":"3749-3760","source":"Crossref","is-referenced-by-count":46,"title":["Glycogen synthase kinase-3 regulates formation of long lamellipodia in human keratinocytes"],"prefix":"10.1242","volume":"116","author":[{"given":"Leeni","family":"Koivisto","sequence":"first","affiliation":[{"name":"University of British Columbia, Faculty of Dentistry, Department of Oral Biological and Medical Sciences, 2199 Wesbrook Mall, Vancouver, BC V6T 1Z3, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Keyhan","family":"Alavian","sequence":"additional","affiliation":[{"name":"University of British Columbia, Faculty of Dentistry, Department of Oral Biological and Medical Sciences, 2199 Wesbrook Mall, Vancouver, BC V6T 1Z3, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lari","family":"Ha\u0308kkinen","sequence":"additional","affiliation":[{"name":"University of British Columbia, Faculty of Dentistry, Department of Oral Biological and Medical Sciences, 2199 Wesbrook Mall, Vancouver, BC V6T 1Z3, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Steven","family":"Pelech","sequence":"additional","affiliation":[{"name":"Kinexus Bioinformatics Corporation, Suite 401, 2389 Health Sciences Mall, Vancouver, BC V6T 1Z4, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christopher A.","family":"McCulloch","sequence":"additional","affiliation":[{"name":"University of Toronto, Faculty of Dentistry, Department of Biological and Diagnostic Sciences, 150 College Street, Toronto, ON M5S 3E2, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hannu","family":"Larjava","sequence":"additional","affiliation":[{"name":"University of British Columbia, Faculty of Dentistry, Department of Oral Biological and Medical Sciences, 2199 Wesbrook Mall, Vancouver, BC V6T 1Z3, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"237","reference":[{"key":"2021042517375276700_REF1","doi-asserted-by":"crossref","unstructured":"Aoki, M. and Tavassoli, M. 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