Cell Biology and Toxicology

, Volume 24, Issue 3, pp 253–263 | Cite as

Impairment of mineralization by metavanadate and decavanadate solutions in a fish bone-derived cell line

  • Daniel M. Tiago
  • Vincent Laizé
  • M. Leonor Cancela
  • Manuel Aureliano
Article

Abstract

Vanadium, a trace metal known to accumulate in bone and to mimic insulin, has been shown to regulate mammalian bone formation using in vitro and in vivo systems. In the present work, short- and long-term effects of metavanadate (containing monomeric, dimeric, tetrameric and pentameric vanadate species) and decavanadate (containing decameric vanadate species) solutions on the mineralization of a fish bone-derived cell line (VSa13) were studied and compared to that of insulin. After 2 h of incubation with vanadate (10 μM in monomeric vanadate), metavanadate exhibited higher accumulation rates than decavanadate (6.85 ± 0.40 versus 3.95 ± 0.10 μg V/g of protein, respectively) in fish VSa13 cells and was also shown to be less toxic when applied for short periods. In longer treatments with both metavanadate and decavanadate solutions, similar effects were promoted: stimulation of cell proliferation and strong impairment (75%) of extracellular matrix (ECM) mineralization. The effect of both vanadate solutions (5 μM in monomeric vanadate), on ECM mineralization was increased in the presence of insulin (10 nM). It is concluded that chronic treatment with both vanadate solutions stimulated fish VSa13 cells proliferation and prevented ECM mineralization. Newly developed VSa13 fish cells appeared to be appropriate in the characterization of vanadate effects on vertebrate bone formation, representing a good alternative to mammalian systems.

Keywords

Bone-derived cell line Vanadate Decavanadate Insulin-mimetic properties Vertebrate bone formation Teleost fish Sparus aurata 

Abbreviations

DMEM

Dulbecco’s modified Eagle medium

ECM

Extracellular matrix

ERK

Extracellular signal-regulated kinase

FBS

Fetal bovine serum

MAPK

Mitogen-activated protein kinase

MTS

(3-(4,5-dimethylthiazol-2-yl)-5-(3-carboxy-methoxyphenyl)-2-(4-sulfophenyl)-2H-tetrazolium

PBS

Phosphate-buffered saline

PI3-K

Phosphatidyl inositol-3 kinase

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Copyright information

© Springer Science+Business Media B.V. 2007

Authors and Affiliations

  • Daniel M. Tiago
    • 1
  • Vincent Laizé
    • 1
  • M. Leonor Cancela
    • 1
  • Manuel Aureliano
    • 1
    • 2
  1. 1.Centre of Marine Sciences (CCMAR)University of Algarve, Campus GambelasFaroPortugal
  2. 2.Faculdade de Ciências e Tecnologia (FCT)Universidade do Algarve, Campus de GambelasFaroPortugal

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