Cooperation of two ADAMTS metalloproteases in closure of the mouse palate identifies a requirement for versican proteolysis in regulating palatal mesenchyme proliferation

• Published in: Development (Cambridge) Vol. 137; no. 23; pp. 4029 - 4038
• Main Authors: Enomoto, Hiroyuki, Nelson, Courtney M., Somerville, Robert P. T., Mielke, Katrina, Dixon, Laura J., Powell, Kimerly, Apte, Suneel S.
• Format: Journal Article
• Language: English
• Published: England Company of Biologists 01.12.2010
• Subjects: ADAM Proteins - deficiency; ADAM Proteins - genetics; ADAM Proteins - metabolism; ADAMTS Proteins; ADAMTS9 Protein; Animals; Animals, Newborn; Cell Count; Cell Lineage - genetics; Cell Proliferation; Cleft Palate - enzymology; Cleft Palate - pathology; Gene Expression Regulation, Developmental; Gene Expression Regulation, Enzymologic; Mesoderm - enzymology; Mesoderm - pathology; Mesoderm - ultrastructure; Mice; Mice, Inbred C57BL; Mutation - genetics; Organogenesis - genetics; Palate - enzymology; Palate - pathology; Palate - ultrastructure; Protein Processing, Post-Translational; RNA, Messenger - genetics; RNA, Messenger - metabolism; Versicans - metabolism

We have identified a role for two evolutionarily related, secreted metalloproteases of the ADAMTS family, ADAMTS20 and ADAMTS9, in palatogenesis. Adamts20 mutations cause the mouse white-spotting mutant belted (bt), whereas Adamts9 is essential for survival beyond 7.5 days gestation (E7.5). Function...