Download Ciba Foundation Symposium 136 - Cell and Molecular Biology PDF

Brings jointly the newest study within the mobile and molecular biology of bones and the teeth, together with purposes to clinical and dental perform. An interdisciplinary workforce of participants addresses regulate of bone formation, resorption and remodelling, osteoblast differentiation and osteoclast job, elements influencing dental extracellular matrix biomineralization, non-collagen proteins in bone and their functionality, hormonal law of bone progress, and extra.


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Extra info for Ciba Foundation Symposium 136 - Cell and Molecular Biology of Vertebrate Hard Tissues

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04). Electron diffraction patterns with a 210" reflection present as a strong meridional pattern of short arc which is indicative of calcium hydroxyapatite crystalites (Fig. 5 ) . The mechanisms by which embryonic tooth organs cultured in serumless and chemically-defined medium regulate tissue-specific biomineralization are not known. Because serum or serum-derived factors were not employed in 32 n Slavkin et al CHROMOSOMES I I J, e m RNAa prot e i ns transmembrane plasma membrane \ , I I , I I I the culture medium, exogenous hormonal regulation was excluded as a possibility for regulation of this in vifro model system.

Slavkin: The polyclonal antibodies that we are using cross-react unequivocally with all three of the phosphoproteins found in rat, rabbit, mouse and man. Factors influencing dental biornineralization 39 Veis: Do they react with the same affinity? Sluvkin: We use the same concentration of IgG antibodies and the same conditions for each of these mammalian species. The avidity of the antibody for the epitopes seems comparable in each species. Veis: The point is that you don’t know which phosphoprotein you are looking at at any given time.

Several mammalian amelogenin cDNAs have been produced, sequenced and used to predict the complete primary structure of bovine and mouse amelogenin (Shimokawa et a1 1987, Snead et a1 1983, 1985). Both amelogenin cDNA probes hybridize with human genomic DNA (Fig. 2). Enamelins, in contrast, are relatively hydrophilic proteins of higher molecular mass (about 68-72 kDa), constitute 1-3% of the total enamel matrix protein, and are characterized by a high content of glycine, aspartic acid, serine and glutamic acid (Termine et a1 1980).

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