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Journal of Dental Research
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Topographic Changes of Focal Adhesion Components and Modulation of p125FAK Activation in Stretched Human Periodontal Ligament Fibroblasts

T. Molina

Department of Orthodontics and Dentofacial Orthopedics, Dental School, University of Heidelberg, Im Neuenheimer Feld 400, 69120 Heidelberg, Germany

K. Kabsch

German Cancer Research Center, Im Neuenheimer Feld 242, 69120 Heidelberg, Germany

A. Alonso

German Cancer Research Center, Im Neuenheimer Feld 242, 69120 Heidelberg, Germany

A. Kohl

Department of Orthodontics and Dentofacial Orthopedics, Dental School, University of Heidelberg, Im Neuenheimer Feld 400, 69120 Heidelberg, Germany

G. Komposch

Department of Orthodontics and Dentofacial Orthopedics, Dental School, University of Heidelberg, Im Neuenheimer Feld 400, 69120 Heidelberg, Germany

P. Tomakidi

Department of Orthodontics and Dentofacial Orthopedics, Dental School, University of Heidelberg, Im Neuenheimer Feld 400, 69120 Heidelberg, Germany, Pascal_Tomakidi{at}med.uni-heidelberg.de

Mechanical stress has been shown in vitro to modulate integrin-β1-mediated activation of p125FAK/FAK. To test the hypothesis whether this also applies to periodontal ligament fibroblasts (PDLs), we subjected human PDLs to mechanical stretch and analyzed stress-induced changes of p125FAK activation by quantitative immunoprecipitation of p125FAK and changes in the topography of molecules localizing in focal adhesions by indirect immunofluorescence. Generally, all components of focal contacts under study-including detection of phosphotyrosine, i.e., integrin-β1, p125FAK, and paxillin-revealed a relative co-localization during stretch application. Under stretch, we observed a re-distribution of all components from the cell periphery to the cytoplasm following the main axes. Tyrosine phosphorylation of p125 FAK was monitored up to 72 hours under stretch. While the amount of p125FAK remained essentially constant, the activation of p125 FAK was clearly modulated. Tyrosine phosphorylation of p125FAK increased from 15 minutes up to 1 hour and declined after stretching periods of 24, 48, and 72 hours. The analysis of our data indicated a stretch-induced re-distribution of focal adhesion components and a modulation of p125 FAK activation, suggesting alterations in focal adhesions and their associated signal cascade.

Key Words: integrins • p125FAK/FAK • paxillin • PDL fibroblasts • stretching

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Journal of Dental Research, Vol. 80, No. 11, 1984-1989 (2001)
DOI: 10.1177/00220345010800110701


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This Article
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