Biological behavior of pre- osteoblasts on natural hydroxyapatite: A study of signaling molecules from attachment to differentiation

Autor(es)

Zambuzzi, Willian F. ^{[1, 2, 3]} ; Ferreira, Carmen V. ^[4] ; Granjeiro, Jose M. ^{[5, 2, 3]} ; Aoyama, Hiroshi ^[4]

Afiliação do(s) autor(es)

^[1] UNIGRANRIO, Postgrad Program Dent, Sch Hlth Sci, Rio De Janeiro - Brazil

^[2] Univ Fed Fluminense, Cell Therapy Ctr, Univ Hosp Antonio Pedro, Rio De Janeiro - Brazil

^[3] Natl Inst Metrol Standardizat & Ind Qual INMETRO, Projects Div, Rio De Janeiro - Brazil

^[4] Univ Estadual Campinas, Dept Biochem, Inst Biol, Sao Paulo - Brazil

^[5] Univ Fed Fluminense, Dept Cell & Mol Biol, Inst Biol, Niteroi, RJ - Brazil

• Tipo de documento: Artigo Científico
• Fonte: Journal of Biomedical Materials Research Part A; v. 97A, n. 2, p. 193-200, MAY 2011.
• Citações Web of Science: 18

Resumo

Several biomaterials have been widely used in bone regeneration in both orthopedic and oral surgeries. However, it is poorly understood how these biomaterials alter osteoblast phenotype. It prompted us to examine the involvement of signaling proteins during preosteoblast adhesion (attachment), proliferation, and differentiation on natural hydroxyapatite (HA) from bovine bone. Our results indicated that natural HA is able to promote osteoblast adhesion, proliferation, and differentiation. The osteoblast/HA interaction requires phosphorylation of tyrosine residues of focal adhesion kinase, Src, and Paxillin upon integrin activation, which culminates in the control of cofilin phosphorylation (at serine 03) via rac-1 activation. In part, these signaling pathways are responsible for actin-rearrangement, responsible to adapt cell-shape on HA particles. In regarding to osteoblast differentiation, we showed that natural HA favored extracellular matrix remodeling by stimulating matrix metalloproteinase activities and alkaline phosphatase activity. Overall, this study demonstrates that osteoblast response toward bovine bone HA is initially mediated by activation of focal adhesion components, culminating on actin-rearrangement executed by cofilin activation via rac-1. Moreover, bovine bone HA provided an excellent microenvironment for osteoblast activity, since adhesion to differentiation. (C) 2011 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 97A: 193-200, 2011. (AU)

• Processo FAPESP: 08/53003-9 - Investigação da função da proteína tirosina fosfatase de baixa massa molecular (LMW-PTP) na adesão de osteoblastos e formação óssea
• Beneficiário: Willian Fernando Zambuzzi
• Modalidade de apoio: Bolsas no Brasil - Pós-Doutorado