TAILIEUCHUNG - Báo cáo khoa học: Identification of a novel matrix protein contained in a protein aggregate associated with collagen in fish otoliths

In the biomineralization processes, proteins are thought to control the polymorphism and morphology of the crystals by forming complexes of structural and mineral-associated proteins. To identify such proteins, we have searched for proteins that may form high-molecular-weight (HMW) aggregates in the matrix of fish otoliths that have aragonite and vaterite as their crystal polymorphs. | ễFEBS Journal Identification of a novel matrix protein contained in a protein aggregate associated with collagen in fish otoliths Hidekazu Tohse1 2 Yasuaki Takagi2 and Hiromichi Nagasawa1 1 Department of Applied BiologicalChemistry Graduate Schoolof Agriculturaland Life Sciences University of Tokyo Japan 2 Division of Marine Biosciences Graduate Schoolof Fisheries Science Hokkaido University Japan Keywords biomineralization calcium binding calcium carbonate collagen otolith matrix Correspondence Y. Takagi Division of Marine Bioscience Graduate School of Fisheries Science Hokkaido University 3-1-1 Minato Hakodate Hokkaido 041-8611 Japan Tel Fax 81 138 40 5550 E-mail takagi@ Database Nucleotide sequence data are available in the DDBJ EMBL GenBank databases under the accession number AB213022 Received 31 December 2007 revised 10 March 2008 accepted 13 March 2008 doi In the biomineralization processes proteins are thought to control the polymorphism and morphology of the crystals by forming complexes of structural and mineral-associated proteins. To identify such proteins we have searched for proteins that may form high-molecular-weight HMW aggregates in the matrix of fish otoliths that have aragonite and vaterite as their crystal polymorphs. By screening a cDNA library of the trout inner ear using an antiserum raised against whole otolith matrix a novel protein named otolith matrix macromolecule-64 OMM-64 was identified. The protein was found to have a molecular mass of 64 kDa and to contain two tandem repeats and a Glu-rich region. The structure of the protein and that of its DNA are similar to those of starmaker a protein involved in the polymorphism control in the zebrafish otoliths Sollner C Burghammer M Busch-Nentwich E Berger J Schwarz H Riekel C Nicolson T 2003 Science 302 282-286 . 45Ca overlay analysis revealed that the Glu-rich region has calcium-binding activity. Combined analysis by western blotting and .

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