{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,3]],"date-time":"2026-06-03T16:20:36Z","timestamp":1780503636224,"version":"3.54.1"},"reference-count":41,"publisher":"Wiley","issue":"s1","license":[{"start":{"date-parts":[[2012,1,13]],"date-time":"2012-01-13T00:00:00Z","timestamp":1326412800000},"content-version":"vor","delay-in-days":43,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["European J Oral Sciences"],"published-print":{"date-parts":[[2011,12]]},"abstract":"<jats:p><jats:italic>Huang Z, Kim J, Lacruz RS, Bringas P Jr, Glogauer M, Bromage TG, Kaartinen VM, Snead ML. Epithelial\u2010specific knockout of the<\/jats:italic> Rac1 <jats:italic>gene leads to enamel defects. \u2028Eur J Oral Sci 2011; 119 (Suppl. 1): 168\u2013176. \u00a9 2011 Eur J Oral Sci<\/jats:italic><\/jats:p><jats:p>The Ras\u2010related C3 botulinum toxin substrate 1 (<jats:italic>Rac1<\/jats:italic>) gene encodes a 21\u2010kDa GTP\u2010binding protein belonging to the RAS superfamily. RAS members play important roles in controlling focal adhesion complex formation and cytoskeleton contraction, activities with consequences for cell growth, adhesion, migration, and differentiation. To examine the role(s) played by RAC1 protein in cell\u2013matrix interactions and enamel matrix biomineralization, we used the <jats:italic>Cre<\/jats:italic>\/<jats:italic>loxP<\/jats:italic> binary recombination system to characterize the expression of enamel matrix proteins and enamel formation in <jats:italic>Rac1<\/jats:italic> knockout mice (<jats:italic>Rac1<\/jats:italic><jats:sup><jats:italic>\u2212\/\u2212<\/jats:italic><\/jats:sup>). Mating between mice bearing the floxed <jats:italic>Rac1<\/jats:italic> allele and mice bearing a cytokeratin 14\u2010<jats:italic>Cre<\/jats:italic> transgene generated mice in which <jats:italic>Rac1<\/jats:italic> was absent from epithelial organs. Enamel of the <jats:italic>Rac1<\/jats:italic> conditional knockout mouse was characterized by light microscopy, backscattered electron imaging in the scanning electron microscope, microcomputed tomography, and histochemistry. Enamel matrix protein expression was analyzed by western blotting. Major findings showed that the Tomes\u2019 processes of <jats:italic>Rac1<\/jats:italic><jats:sup><jats:italic>\u2212\/\u2212<\/jats:italic><\/jats:sup> ameloblasts lose contact with the forming enamel matrix in unerupted teeth, the amounts of amelogenin and ameloblastin are reduced in <jats:italic>Rac1<\/jats:italic><jats:sup><jats:italic>\u2212\/\u2212<\/jats:italic><\/jats:sup> ameloblasts, and after eruption, the enamel from <jats:italic>Rac1<\/jats:italic><jats:sup><jats:italic>\u2212\/\u2212<\/jats:italic><\/jats:sup> mice displays severe structural defects with a complete loss of enamel. These results support an essential role for RAC1 in the dental epithelium involving cell\u2013matrix interactions and matrix biomineralization.<\/jats:p>","DOI":"10.1111\/j.1600-0722.2011.00904.x","type":"journal-article","created":{"date-parts":[[2012,1,13]],"date-time":"2012-01-13T18:56:16Z","timestamp":1326480976000},"page":"168-176","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["Epithelial\u2010specific knockout of the <i>Rac1<\/i> gene leads to enamel defects"],"prefix":"10.1111","volume":"119","author":[{"given":"Zhan","family":"Huang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jieun","family":"Kim","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rodrigo 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