Journal
BIOMATERIALS
Volume 26, Issue 22, Pages 4523-4531Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.biomaterials.2004.11.028
Keywords
cell adhesion; integrin; self-assembled monolayers; fibronectin; differentiation; myoblast
Funding
- NIBIB NIH HHS [R01-EB003364] Funding Source: Medline
- NIGMS NIH HHS [T32 GM008433] Funding Source: Medline
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Biomaterial surface properties modulate protein adsorption and cell adhesion to elicit diverse cellular responses in biomedical and biotechnological applications. We used alkanethiol self-assembled monolayers presenting well-defined chemistries (OH, CH3, NH2, and COOH) to analyze the effects of surface chemistry on myoblast proliferation and differentiation. Surfaces were pre-coated with equivalent densities of fibronectin. C2C12 skeletal myoblasts exhibited surface-dependent differences in cell proliferation (COOH = NH2 > CH3 = OH). Myogenin and troponin T gene expression levels were up-regulated on CH3 and OH surfaces compared to other chemistries. Furthermore, immunostaining for sarcomeric myosin revealed surface chemistry-dependent differences in myogenic differentiation following the pattern OH > CH3 > NH2 = COOH. Immunostaining analyses of integrin subunits demonstrated surface chemistry-dependent differences in integrin binding to adsorbed fibronectin. OH and CH3 surfaces supported selective binding Of alpha(5)beta(1) integrin while the COOH and NH2, functionalities displayed binding of both alpha(5)beta(1), and alpha(v)beta(3). Myogenic differentiation correlated with differences in integrin binding; surface chemistries that supported selective binding Of alpha(5)beta(1) displayed enhanced differentiation. Finally, blocking beta(1), but not beta(3), integrins inhibited differentiation, implicating specific integrins in the differentiation process. These results demonstrate that Surface chemistry modulates myoblast proliferation and differentiation via differences in integrin binding to adsorbed fibronectin. (c) 2004 Elsevier Ltd. All rights reserved.
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