Dataset Information

Distribution of Cathepsin K in Late Stage of Tooth Germ Development and Its Function in Degrading Enamel Matrix Proteins in Mouse.

ABSTRACT: Cathepsin K (CTSK) is a member of cysteine proteinase family, and is predominantly expressed in osteoclastsfor degradationof bone matrix proteins. Given the similarity in physical properties of bone and dental mineralized tissues, including enamel, dentin and cementum, CTSK is likely to take part in mineralization process during odontogenesis. On the other hand, patients with pycnodysostosis caused by mutations of the CTSK gene displayedmultipledental abnormalities, such as hypoplasia of the enamel, obliterated pulp chambers, hypercementosis and periodontal disease. Thereforeitis necessary to study the metabolic role of CTSK in tooth matrix proteins. In this study, BALB/c mice at embryonic day 18 (E18), post-natal day 1 (P1), P5, P10 and P20 were used (5 mice at each time point)for systematic analyses of CTSK expression in the late stage of tooth germ development. We found that CTSK was abundantly expressed in the ameloblasts during secretory and maturation stages (P5 and P10) by immunohistochemistry stainings.During dentinogenesis, the staining was also intense in the mineralization stage (P5 and P10),but not detectable in the early stage of dentin formation (P1) and after tooth eruption (P20).Furthermore, through zymography and digestion test in vitro, CTSK was proved to be capable of hydrolyzing Emdogain and also cleaving Amelogenininto multiple products. Our resultsshed lights on revealing new functions of CTSK and pathogenesis of pycnodysostosis in oral tissues.

SUBMITTER: Jiang T

PROVIDER: S-EPMC5240959 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature

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Distribution of Cathepsin K in Late Stage of Tooth Germ Development and Its Function in Degrading Enamel Matrix Proteins in Mouse.

Jiang Tao T Liu Fen F Wang Wei-Guang WG Jiang Xin X Wen Xuan X Hu Kai-Jin KJ Xue Yang Y

PloS one 20170117 1

Cathepsin K (CTSK) is a member of cysteine proteinase family, and is predominantly expressed in osteoclastsfor degradationof bone matrix proteins. Given the similarity in physical properties of bone and dental mineralized tissues, including enamel, dentin and cementum, CTSK is likely to take part in mineralization process during odontogenesis. On the other hand, patients with pycnodysostosis caused by mutations of the CTSK gene displayedmultipledental abnormalities, such as hypoplasia of the ena ...[more]

PMID: 28095448

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Project description:1. Investigations were designed to identify the proteins which characterize the ameloblast phenotype, and to determine to what extent these extracellular-matrix proteins were degraded as a function of enamel matrix mineralization and maturation. 2. The identification of enamel proteins was based on comparisons between the electrophoretic patterns of enamel-containing and non-enamel-containing matrix extracts isolated from specific regions within 26-day embryonic New Zealand White rabbit incisor and molar tooth organs. 3. Since enamel proteins become mineralized on secretion, matrix specimens were demineralized in cold 5% (w/v) trichloroacetic acid, extracted with buffered 6M-urea and reduced with mercaptoethanol, and then the solubilized proteins were fractionated by urea/polyacrylamide-gel electrophoresis. 4. Three enamel-specific electrophoretic components were identified in newly secreted enamel-matrix specimens and this number increased as a function of mineralization and maturation. 5. Antibodies were prepared against embryonic rabbit extracellular matrix containing enamel. Comparison between immunoelectrophoretic patterns demonstrated that two of the three enamel components were antigenic. 6. Polyacrylamide-gel electrophoresis in sodium dodecyl sulphate was used to identify four enamel proteins of mol.wts. (1) 65 000 (2) 58000 (3) 22 000 and (4) 20 000, localized within enamel matrix. Enamel proteins (1) and (3) were phosphorylated, whereas (2) and (4) did not contain detectable phosphate. Labelled proline, leucine, tryptophan and glucosamine were incorporated into each of the four enamel proteins extracted from tooth explants incubated in the presence of radioactive precursors for 6 h. Whereas four proteins were identified in newly secreted enamel matrix, the concentrations of high-molecular-weight proteins (1) and (2) were found to decrease and the number (greater than 10) and concentration of low-molecular-weight polypeptides increased as a function of advanced enamel-matrix mineralization and maturation.

Dataset Information

Distribution of Cathepsin K in Late Stage of Tooth Germ Development and Its Function in Degrading Enamel Matrix Proteins in Mouse.

Publications

Distribution of Cathepsin K in Late Stage of Tooth Germ Development and Its Function in Degrading Enamel Matrix Proteins in Mouse.

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