Premium
α 2 β 1 integrin‐specific collagen‐mimetic surfaces supporting osteoblastic differentiation
Author(s) -
Reyes Catherine D.,
García Andrés J.
Publication year - 2004
Publication title -
journal of biomedical materials research part a
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.849
H-Index - 150
eISSN - 1552-4965
pISSN - 1549-3296
DOI - 10.1002/jbm.a.30034
Subject(s) - materials science , integrin , biomedical engineering , nanotechnology , biophysics , biochemistry , cell , biology , medicine
The interactions of osteoblasts with their surrounding extracellular matrix (ECM) are essential for skeletal development, homeostasis, and maintenance of the mature osteoblastic phenotype. Integrins are the principal transducers of ECM signals that regulate this process of osteoblast commitment and differentiation. Several studies indicate that the α 2 β 1 integrin interaction with type I collagen is a crucial signal for the induction of osteoblastic differentiation and matrix mineralization. Integrin α 2 β 1 recognizes the Gly‐Phe‐Hyp‐Gly‐Glu‐Arg (GFOGER) motif in residues 502–507 of the α 1 [I] chain of type I collagen. This study demonstrates that an α 2 β 1 integrin‐specific GFOGER peptide triggers the activation of focal adhesion kinase and alkaline phosphatase in MC3T3‐E1 murine immature osteoblast‐like cells, two events that have been implicated in the osteoblastic differentiation pathway. These GFOGER‐peptide surfaces also support the expression of multiple osteoblast‐specific genes, including osteocalcin and bone sialoprotein, and induce matrix mineralization in a manner similar to type I collagen. This triple‐helical peptide represents a promising surface modification strategy for the design of collagen‐mimetic bioadhesive surfaces that support osteoblastic differentiation. © 2004 Wiley Periodicals, Inc. J Biomed Mater Res 69A: 591–600, 2004