Document Detail


Surface chemistry modulates focal adhesion composition and signaling through changes in integrin binding.
MedLine Citation:
PMID:  15183609     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Biomaterial surface properties influence protein adsorption and elicit diverse cellular responses in biomedical and biotechnological applications. However, the molecular mechanisms directing cellular activities remain poorly understood. Using a model system with well-defined chemistries (CH3, OH, COOH, NH2) and a fixed density of the single adhesive ligand fibronectin, we investigated the effects of surface chemistry on focal adhesion assembly and signaling. Surface chemistry strongly modulated integrin binding and specificity--alpha5beta1 integrin binding affinity followed the pattern OH>NH2=COOH>CH3, while integrin alphaVbeta3 displayed the relationship COOH>NH2>>OH=CH3. Immunostaining and biochemical analyses revealed that surface chemistry modulates the structure and molecular composition of cell-matrix adhesions as well as focal adhesion kinase (FAK) signaling. The neutral hydrophilic OH functionality supported the highest levels of recruitment of talin, alpha-actinin, paxillin, and tyrosine-phosphorylated proteins to adhesive structures. The positively charged NH2 and negatively charged COOH surfaces exhibited intermediate levels of recruitment of focal adhesion components, while the hydrophobic CH3 substrate displayed the lowest levels. These patterns in focal adhesion assembly correlated well with integrin alpha5beta1 binding. Phosphorylation of specific tyrosine residues in FAK also showed differential sensitivity to surface chemistry. Finally, surface chemistry-dependent differences in adhesive interactions modulated osteoblastic differentiation. These differences in focal adhesion assembly and signaling provide a potential mechanism for the diverse cellular responses elicited by different material properties.
Authors:
Benjamin G Keselowsky; David M Collard; Andrés J García
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Biomaterials     Volume:  25     ISSN:  0142-9612     ISO Abbreviation:  Biomaterials     Publication Date:  2004 Dec 
Date Detail:
Created Date:  2004-06-08     Completed Date:  2005-03-15     Revised Date:  2012-06-05    
Medline Journal Info:
Nlm Unique ID:  8100316     Medline TA:  Biomaterials     Country:  England    
Other Details:
Languages:  eng     Pagination:  5947-54     Citation Subset:  IM    
Affiliation:
Coulter School of Biomedical Engineering, Georgia Institute of Technology, Atlanta 30332, USA.
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MeSH Terms
Descriptor/Qualifier:
3T3 Cells
Animals
Cell Adhesion
Focal Adhesion Kinase 1
Focal Adhesion Protein-Tyrosine Kinases
Humans
Integrins / metabolism*
Mice
Phosphorylation
Protein Binding
Protein-Tyrosine Kinases / metabolism*
Signal Transduction*
Surface Properties
Chemical
Reg. No./Substance:
0/Integrins; EC 2.7.10.1/Focal Adhesion Kinase 1; EC 2.7.10.1/Protein-Tyrosine Kinases; EC 2.7.10.2/Focal Adhesion Protein-Tyrosine Kinases; EC 2.7.10.2/PTK2 protein, human; EC 2.7.10.2/Ptk2 protein, mouse

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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