Development, Function and Evolution of Teeth by MF Teaford, MM Smith, MWJ Ferguson

By MF Teaford, MM Smith, MWJ Ferguson

Advances in genetics, histology, microstructure, biomechanics, and morphometrics have allowed researchers to view tooth and dental tissue from new views. Written through major specialists within the box, this booklet brings jointly overviews on quite a lot of dental subject matters. The members speak about the newest examine linking genes, molecules, and developmental mechanisms inside an evolutionary framework. This publication will stimulate cooperative examine in fields as assorted as paleontology, molecular biology, developmental biology, and sensible morphology.

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Growth factors as inductive signals regulating tooth morphogenesis. Seminars in Cell and Developmental Biology, 7, 185±193. , Vaahtokari, A. -M. (1995). Regulation of organogenesis. Common molecular mechanisms regulating the development of teeth and other organs. International Journal of Developmental Biology, 39, 35±50. Tims, H. W. M. (1901). Tooth genesis in the Caviidae. Journal of the Linnean Society (Zoology), 28, 261±290. Ê berg, T. and Thesleff, I. (1996a). , A developing tooth: association with an embryonic signalling center and suppression by EGF and FGF-4.

Developmental Biology, 155, 172±179. , Gallo, R. and Lose, E. (1992). Biology of the syndecans. Annual Review of Cell Biology, 8, 333±364. Berteretche, M. L. and Forest, N. (1993). Abnormal incisor-tooth differentiation in transgenic mice expressing the muscle-speci®c desmin gene. European Journal of Cell Biology, 62, 183±193. Bishop, M. A. (1985). Evidence for tight junctions between odontoblasts in the rat incisor. Cell Tissue Research, 239, 137±140. Bishop, M. A. and Yoshida, S. (1992). A permeability barrier to lanthanum and the presence of collagen between odontoblasts in pig molars.

Schematic representation of micro®laments-membrane (Mb) ± ®bronectin interaction. Fibronectin interacts with integrin by means of the GRGDS sequence and with the 165 kDa membrane protein by means of a N-terminal 62 kDa peptide including the collagen-binding domain and the ®rst type III repeated unit. Neither the collagen-binding domain alone (47 kDa) nor the large 175 kDa protein interacted with the 165 kDa protein. Although ®bronectin ± 165 kDa interaction interferes with micro®lament organization neither, actin, nor a-actinin nor vinculin directly interacted with the 165 kDa protein.

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