TAILIEUCHUNG - Báo cáo khoa học: Identification of an osteopontin-like protein in fish associated with mineral formation

Fish has been recently recognized as a suitable vertebrate model and repre-sents a promising alternative to mammals for studying mechanisms of tis-sue mineralization and unravelling specific questions related to vertebrate bone formation. The recently developedSparus aurata(gilthead seabream) osteoblast-like cell line VSa16 was used to construct a cDNA subtractive library aimed at the identification of genes associated with fish tissue min-eralization. | ễFEBS Journal Identification of an osteopontin-like protein in fish associated with mineral formation Vera G. Fonseca Vincent Laize Marta S. Valente and M. Leonor Cancela Centro de Ciencias do Mar CCMAR Universidade do Algarve Faro Portugal Keywords bone-derived cell line gilthead seabream Sparus aurata Teleostei osteopontin subtractive library tissue mineralization Correspondence M. Leonor Cancela Centro de Ciencias do Mar CCMAR Universidade do Algarve Campus de Gambelas 8005-139 Faro Portugal Fax 351 289800069 Tel 351 289800971 E-mail lcancela@ Website http fcma edge web These authors contributed equally to this work Received 11 April2007 revised 21 June 2007 accepted 2 July 2007 doi Fish has been recently recognized as a suitable vertebrate model and represents a promising alternative to mammals for studying mechanisms of tissue mineralization and unravelling specific questions related to vertebrate bone formation. The recently developed Sparus aurata gilthead seabream osteoblast-like cell line VSa16 was used to construct a cDNA subtractive library aimed at the identification of genes associated with fish tissue mineralization. Suppression subtractive hybridization combined with mirror orientation selection identified 194 cDNA clones representing 20 different genes up-regulated during the mineralization of the VSa16 extracellular matrix. One of these genes accounted for 69 of the total number of clones obtained and was later identified as the S. aurata osteopontin-like gene. The 2138-bp full-length S. aurata osteopontin-like cDNA was shown to encode a 374 amino-acid protein containing domains and motifs characteristic of osteopontins such as an integrin receptor-binding RGD motif a negatively charged domain and numerous post-translational modifications . phosphorylations and glycosylations . The common origin of mammalian osteopontin and fish osteopontin-like proteins was indicated through an in silico .

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