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Proteome analysis of matrix vesicles isolated from femurs of chicken embryo
Author(s) -
Balcerzak Marcin,
Malinowska Agata,
Thouverey Cyril,
Sekrecka Anna,
Dadlez Michal,
Buchet Rene,
Pikula Slawomir
Publication year - 2007
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200700612
Subject(s) - proteome , microbiology and biotechnology , extracellular matrix , chemistry , annexin a2 , proteomics , cartilage , endochondral ossification , biochemistry , biology , annexin , gene , anatomy , cell
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 α2, 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.