An extracellular matrix infrastructure provides support for murine secondary palatal shelf remodelling.
A crucial part of secondary palate morphogenesis is the movement of the palatal shelves from an initial vertical position on either side of the tongue to a final horizontal one above it to achieve palate closure. The immunocytochemical localization of extracellular matrix (ECM) molecules in the palatal shelf during this remodelling and reorientation revealed the existence of an ECM infrastructure within the mesenchyme. The major components of this infrastructure were collagen III, fibronectin, and hyaluronate (HA). With remodelling, HA's domain within the mesenchyme was expanded, whereas those of fibronectin and collagen III became more circumscribed. The expansion of an HA-rich matrix within the mesenchyme is thought to be crucial for palatal reorientation. The results of this study suggest that, as this expansion occurs, it is modulated by collagen and fibronectin components of the ECM infrastructure. Prior to shelf remodelling, this infrastructure may be anchored by a specialized region of the midoral epithelial-mesenchymal interface and the subjacent mesenchyme which is characterized by the unique distribution of collagen III, fibronectin, and tenascin. The midoral palatal epithelium also may play a role in directing shelf expansion. This epithelial region undergoes changes in cell packing and epithelial cell layering that correlate with shelf remodelling. These changes occur concomitantly with changes in the expression of collagen III, collagen IV, and laminin within the underlying basement membrane. The localization and patterning of tenascin within the developing palate suggests that it not only contributes to the postulated anchoring structure of the midoral epithelial-mesenchymal region, but also plays a role in the determining the fate of the medial edge epithelial cells during the final stage of palate closure.
D000818:Animals; D016723:Bone Remodeling; D015816:Cell Adhesion Molecules, Neuronal / Q000032:analysis*; D003094:Collagen / Q000032:analysis*; D005109:Extracellular Matrix / Q000737:chemistry* / Q000648:ultrastructure; D016326:Extracellular Matrix Proteins / Q000032:analysis*; D005353:Fibronectins / Q000032:analysis*; D006820:Hyaluronic Acid / Q000032:analysis*; D007150:Immunohistochemistry; D007797:Laminin / Q000032:analysis; D051379:Mice; D010159:Palate / Q000737:chemistry* / Q000196:embryology* / Q000502:physiology; D019063:Tenascin
D015816:Cell Adhesion Molecules, Neuronal; D016326:Extracellular Matrix Proteins; D005353:Fibronectins; D007797:Laminin; D019063:Tenascin; D006820:Hyaluronic Acid; D003094:Collagen