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Molecular and Cellular Biology, June 2007, p. 4306-4316, Vol. 27, No. 12
0270-7306/07/$08.00+0     doi:10.1128/MCB.00041-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

{alpha}11ß1 Integrin-Dependent Regulation of Periodontal Ligament Function in the Erupting Mouse Incisor

Svetlana N. Popova,1,2 Malgorzata Barczyk,1,2,8 Carl-Fredrik Tiger,2,{dagger} Wouter Beertsen,3 Paola Zigrino,4 Attila Aszodi,5 Nicolai Miosge,6 Erik Forsberg,7 and Donald Gullberg1,2*

Department of Biomedicine,1 Department of Oral Sciences-Periodontics, University of Bergen, Jonas Lies vei 91, N-5009 Bergen, Norway,8 Department of Medical Biochemistry and Microbiology, Uppsala University, BMC, Box 582, Uppsala SE-751 23, Sweden,2 Academic Center for Dentistry, Amsterdam,The Netherlands,3 Department of Dermatology, University of Cologne, Cologne, Germany,4 Max Planck Institute for Biochemistry, Martinsried, Germany,5 Department of Prosthodontics, Georg-August-Universität, Göttingen, Germany,6 Amersham Biosciences AB, Uppsala, Sweden7

Received 9 January 2007/ Returned for modification 2 February 2007/ Accepted 28 March 2007

The fibroblast integrin {alpha}11ß1 is a key receptor for fibrillar collagens. To study the potential function of {alpha}11 in vivo, we generated a null allele of the {alpha}11 gene. Integrin {alpha}11–/– mice are viable and fertile but display dwarfism with increased mortality, most probably due to severely defective incisors. Mutant incisors are characterized by disorganized periodontal ligaments, whereas molar ligaments appear normal. The primary defect in the incisor ligament leads to halted tooth eruption. {alpha}11ß1-defective embryonic fibroblasts displayed severe defects in vitro, characterized by (i) greatly reduced cell adhesion and spreading on collagen I, (ii) reduced ability to retract collagen lattices, and (iii) reduced cell proliferation. Analysis of matrix metalloproteinase in vitro and in vivo revealed disturbed MMP13 and MMP14 synthesis in {alpha}11–/– cells. We show that {alpha}11ß1 is the major receptor for collagen I on mouse embryonic fibroblasts and suggest that {alpha}11ß1 integrin is specifically required on periodontal ligament fibroblasts for cell migration and collagen reorganization to help generate the forces needed for axial tooth movement. Our data show a unique role for {alpha}11ß1 integrin during tooth eruption.

* Corresponding author. Mailing address: Department of Biomedicine, University of Bergen, Jonas Lies vei 91, N-5009 Bergen, Norway. Phone: 47-555 86332. Fax: 47-555 86410. E-mail: donald.gullberg{at}biomed.uib.no

{dagger} Present address: Department of Microbiology, University of Gothenburg, Gothenburg, Sweden.

Molecular and Cellular Biology, June 2007, p. 4306-4316, Vol. 27, No. 12
0270-7306/07/$08.00+0     doi:10.1128/MCB.00041-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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