This Article Full Text (PDF) References Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Add to Saved Citations Download to citation manager Request Permissions Request Reprints Add to My Marked Citations Citing Articles Citing Articles via Google Scholar Citing Articles via Scopus Google Scholar Articles by Molina, T. Articles by Tomakidi, P. Search for Related Content PubMed PubMed Citation Articles by Molina, T. Articles by Tomakidi, P. Social Bookmarking                         What's this?

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

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 p125^FAK/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 p125^FAK activation by quantitative immunoprecipitation of p125^FAK 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, p125^FAK, 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 p125^FAK remained essentially constant, the activation of p125 ^FAK was clearly modulated. Tyrosine phosphorylation of p125^FAK 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

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


CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?