Proteome analysis of matrix vesicles isolated from femurs of chicken embryo

被引:71
作者
Balcerzak, Marcin [1 ]
Malinowska, Agata [2 ]
Thouverey, Cyril [1 ,3 ]
Sekrecka, Anna [1 ,4 ]
Dadlez, Michal [2 ,5 ]
Buchet, Rene [3 ]
Pikula, Slawomir [1 ]
机构
[1] Polish Acad Sci, M Nencki Inst Expt Biol, Dept Biochem, PL-02093 Warsaw, Poland
[2] Polish Acad Sci, Inst Biochem & Biophys, Dept Biophys, Warsaw, Poland
[3] Univ Lyon, Univ Lyon 1, INSA Lyon,CPE Lyon, ICBMS,CNRS UMR 5246, Villeurbanne, France
[4] Univ Agr, Dept Biophys, SGGW, Warsaw, Poland
[5] Warsaw Univ, Dept Biol, Warsaw, Poland
关键词
chicken; matrix vesicles; mineralization;
D O I
10.1002/pmic.200700612
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Matrix vesicles (MVs) are extracellular organelles that initiate mineral formation, accumulating inorganic phosphate (P-i) and calcium leading to the formation of hydroxyapatite (HA) crystals, the main mineral component of bones. MVs are produced during bone formation, as well as during the endochondral calcification of cartilage. MVs are released into the extracellular matrix from osseous cells such as osteoblasts and hypertrophic chondrocytes. In this report, using 1-D SDS-PAGE, in-gel tryptic digestion and an LC-MS-MS/MS protein identification protocol, we characterized the proteome of MVs isolated from chicken embryo (Gallus gallus) bones and cartilage. We identified 126 gene products, including proteins related to the extracellular matrix and ion transport, as well as enzymes, cytoskeletal, and regulatory proteins. Among the proteins recognized for the first time in MVs were aquaporin 1, annexin A1 (AnxA1), AnxA11, glycoprotein HT7, G(i) protein alpha 2, and scavenger receptor type B. The pathways for targeting the identified proteins into MVs and their particular functions in the biomineralization process are discussed. Obtaining a knowledge of the functions and roles of these proteins during embryonic mineralization is a prerequisite for the overall understanding of the initial mineral formation mechanisms.
引用
收藏
页码:192 / 205
页数:14
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