title: Heparanase localization during palatogenesis in mice.
abstract: Palatogenesis is directed by epithelial-mesenchymal interactions and results partly from remodeling of the extracellular matrix (ECM) of the palatal shelves. Here, we assessed heparanase distribution in developing mouse palates. No heparanase was observed in the vertically oriented palatal shelves in early stages of palate formation. As palate formation progressed, the palatal shelves were reorganized and arranged horizontally above the tongue, and heparanase localized to the epithelial cells of these shelves. When the palatal bilateral shelves first made contact, the heparanase localized to epithelial cells at the tips of shelves. Later in fusing palatal shelves, the cells of the medial epithelial seam (MES) were labeled with intense heparanase signal. In contrast, the basement membrane heparan sulfate (HS) was scarcely observed in the palatal shelves in contact. Moreover, perlecan labeling was sparse in the basement membrane of the MES, on which laminin and type IV collagen were observed. Moreover, we assessed the distribution of matrix metalloproteinase- (MMP-) 9, MMP-2, and MMP-3 in developing mouse palates and these MMPs were observed in the MES. Our findings indicated that heparanase was important for palate formation because it mediated degradation of the ECM of palatal shelves. Heparanase may, in concert with other proteases, participate in the regression of the MES.
authors.affiliation: Department of Anatomy and Cell Biology, Faculty of Medicine, Osaka Medical College, Takatsuki 569-8686, Japan. an1026@art.osaka-med.ac.jp
authors.forename: Azumi
authors.initials: A
authors.lastname: Hirata
authors.forename: Kentaro
authors.initials: K
authors.lastname: Katayama
authors.forename: Takehito
authors.initials: T
authors.lastname: Tsuji
authors.forename: Nagato
authors.initials: N
authors.lastname: Natsume
authors.forename: Toshio
authors.initials: T
authors.lastname: Sugahara
authors.forename: Yuichi
authors.initials: Y
authors.lastname: Koga
authors.forename: Kazufumi
authors.initials: K
authors.lastname: Takano
authors.forename: Yoshinori
authors.initials: Y
authors.lastname: Otsuki
authors.forename: Hiroaki
authors.initials: H
authors.lastname: Nakamura
mesh_terms: D000818:Animals; D001485:Basement Membrane / Q000378:metabolism; D024141:Collagen Type IV / Q000378:metabolism; D005109:Extracellular Matrix / Q000378:metabolism; D005260:Female; D018507:Gene Expression Regulation, Developmental; D015971:Gene Expression Regulation, Enzymologic; D005966:Glucuronidase / Q000096:biosynthesis*; D019812:Heparan Sulfate Proteoglycans / Q000378:metabolism; D006497:Heparan Sulfate / Q000378:metabolism; D007797:Laminin / Q000378:metabolism; D008297:Male; D051379:Mice; D008810:Mice, Inbred C57BL; D008856:Microscopy, Fluorescence; D010159:Palate / Q000196:embryology*; D013997:Time Factors; D000099175:Heparanase
chemical_list: D024141:Collagen Type IV; D005966:Glucuronidase; D019812:Heparan Sulfate Proteoglycans; D006497:Heparan Sulfate; D007797:Laminin; D000099175:Heparanase; C071927:perlecan