Maturation stage enamel defects in Odontogenesis-associated phosphoprotein (Odaph) deficient mice. 2021

Yikang Ji, and Cong Li, and Yuan Tian, and Yan Gao, and Zhiheng Dong, and Lili Xiang, and Zhenzhen Xu, and Yuguang Gao, and Li Zhang
Department of Stomatology, Yantai Affiliated Hospital of Binzhou Medical University, Yantai, Shandong, China.

Mutation in Odontogenesis-associated phosphoprotein (ODAPH) has been reported to cause recessive hypomineralized amelogenesis imperfecta (AI) in human. However, the exact role of ODAPH in amelogenesis is still unknown. ODAPH was identified as a novel constituent of the atypical basal lamina located at the interface between maturation ameloblasts and the enamel by dual immunofluorescence staining of ODAPH and LAMC2. Odaph knockout mice were generated to explore the function of ODAPH in amelogenesis. Odaph-/- mice teeth showed severely attrition and reduced enamel mineralization. Histological analysis showed from transition or early-maturation stage, ameloblasts were rapidly shortened, lost cell polarity, and exhibited cell pathology. Abundant enamel matrix marked by amelogenin was retained. Temporary cyst-like structures were formed between flattened epithelial cells and the enamel from maturation stage to eruption. The integrity of the atypical basal lamina was impaired indicated by the reduced diffuse expression of LAMC2 and AMTN. The expression of maturation stage related genes of Amtn, Klk4, Integrinβ6 and Slc24a4 were significantly decreased. Our results suggested Odaph played vital roles during amelogenesis by maintaining the integrity of the atypical basal lamina in maturation stage, which may contribute to a better understanding of the pathophysiology of human AI.

UI MeSH Term Description Entries
D007797 Laminin Large, noncollagenous glycoprotein with antigenic properties. It is localized in the basement membrane lamina lucida and functions to bind epithelial cells to the basement membrane. Evidence suggests that the protein plays a role in tumor invasion. Merosin,Glycoprotein GP-2,Laminin M,Laminin M Chain,Chain, Laminin M,Glycoprotein GP 2,M Chain, Laminin
D010750 Phosphoproteins Phosphoprotein
D003743 Dental Enamel A hard thin translucent layer of calcified substance which envelops and protects the dentin of the crown of the tooth. It is the hardest substance in the body and is almost entirely composed of calcium salts. Under the microscope, it is composed of thin rods (enamel prisms) held together by cementing substance, and surrounded by an enamel sheath. (From Jablonski, Dictionary of Dentistry, 1992, p286) Enamel,Enamel Cuticle,Dental Enamels,Enamel, Dental,Enamels, Dental,Cuticle, Enamel,Cuticles, Enamel,Enamel Cuticles,Enamels
D000565 Ameloblasts Cylindrical epithelial cells in the innermost layer of the ENAMEL ORGAN. Their functions include contribution to the development of the dentinoenamel junction by the deposition of a layer of the matrix, thus producing the foundation for the prisms (the structural units of the DENTAL ENAMEL), and production of the matrix for the enamel prisms and interprismatic substance. (From Jablonski's Dictionary of Dentistry, 1992) Ameloblast
D000566 Amelogenesis The elaboration of dental enamel by ameloblasts, beginning with its participation in the formation of the dentino-enamel junction to the production of the matrix for the enamel prisms and interprismatic substance. (Jablonski, Dictionary of Dentistry, 1992). Amelogeneses
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D016326 Extracellular Matrix Proteins Macromolecular organic compounds that contain carbon, hydrogen, oxygen, nitrogen, and usually, sulfur. These macromolecules (proteins) form an intricate meshwork in which cells are embedded to construct tissues. Variations in the relative types of macromolecules and their organization determine the type of extracellular matrix, each adapted to the functional requirements of the tissue. The two main classes of macromolecules that form the extracellular matrix are: glycosaminoglycans, usually linked to proteins (proteoglycans), and fibrous proteins (e.g., COLLAGEN; ELASTIN; FIBRONECTINS; and LAMININ). Extracellular Matrix Protein,Matrix Protein, Extracellular,Matrix Proteins, Extracellular,Protein, Extracellular Matrix,Proteins, Extracellular Matrix
D051379 Mice The common name for the genus Mus. Mice, House,Mus,Mus musculus,Mice, Laboratory,Mouse,Mouse, House,Mouse, Laboratory,Mouse, Swiss,Mus domesticus,Mus musculus domesticus,Swiss Mice,House Mice,House Mouse,Laboratory Mice,Laboratory Mouse,Mice, Swiss,Swiss Mouse,domesticus, Mus musculus
D018345 Mice, Knockout Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes. Knockout Mice,Mice, Knock-out,Mouse, Knockout,Knock-out Mice,Knockout Mouse,Mice, Knock out

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