QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

This Article Figures Only Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Faccio, R. Articles by Zallone, A. Search for Related Content PubMed PubMed Citation Articles by Faccio, R. Articles by Zallone, A.

Localization and possible role of two different alpha v beta 3 integrin conformations in resting and resorbing osteoclasts

¹ Department of Human Anatomy and Histology, University of Bari, Italy
² M.I.A. Dibit-hsr et University of Milano Bicocca-Monza, Milan, Italy
³ Department of Internal Medicine, University of Bari, Italy
⁴ Department of Cell Biology and The Scripps Research Institute, La Jolla, USA

^* Author for correspondence (e-mail: faccio{at}pathology.wustl.edu )

Accepted 19 April 2002

Integrins are membrane receptors that mediate interactions between cells and the extracellular matrix. We recently showed that the osteoclast integrin _vß₃ exists in two different conformations, so-called `basal' and `activated', with each exhibiting a distinct function. In this study we demonstrate that, in non-resorbing osteoclasts, the `activated' form of <sub>v</sub>ß<sub>3</sub> accumulates in the motile areas of the plasma membrane. During bone resorption this conformation is prevalent in the ruffled membrane, whereas the `basal' form of _vß₃ is also present in the sealing zone. Moreover, hepatocyte growth factor (HGF) and macrophage colony stimulating factor (M-CSF), two molecules involved in osteoclastogenesis and osteoclast survival, modulate _vß₃ conformation in vitro. Preincubation with HGF or M-CSF induces a shift of conformation of _vß₃ in primary human osteoclasts (OCs) and in the osteoclast-like cell line (GCT 23). Activated integrin promotes osteoclast migration to the _vß₃ ligand osteopontin and enhances bone resorption. Thus, HGF and M-CSF modulate the _vß₃ conformational states required for osteoclast polarization and resorption. The capacity of growth factors to alter the affinity of _vß₃ toward its ligands offers a potential explanation for the diverse responses of osteoclasts to the same ligand.

Key words: Osteoclasts, Alpha v beta 3, Integrin, HGF, M-CSF

This article has been cited by other articles:

				G. N. M. Hajj, M. H. Lopes, A. F. Mercadante, S. S. Veiga, R. B. da Silveira, T. G. Santos, K. C. B. Ribeiro, M. A. Juliano, S. G. Jacchieri, S. M. Zanata, et al. Cellular prion protein interaction with vitronectin supports axonal growth and is compensated by integrins J. Cell Sci., June 1, 2007; 120(11): 1915 - 1926. [Abstract] [Full Text] [PDF]

				F. Saltel, O. Destaing, F. Bard, D. Eichert, and P. Jurdic Apatite-mediated Actin Dynamics in Resorbing Osteoclasts Mol. Biol. Cell, December 1, 2004; 15(12): 5231 - 5241. [Abstract] [Full Text] [PDF]

				Y. Calle, G. E. Jones, C. Jagger, K. Fuller, M. P. Blundell, J. Chow, T. Chambers, and A. J. Thrasher WASp deficiency in mice results in failure to form osteoclast sealing zones and defects in bone resorption Blood, May 1, 2004; 103(9): 3552 - 3561. [Abstract] [Full Text] [PDF]

				M. Rolli, E. Fransvea, J. Pilch, A. Saven, and B. Felding-Habermann Activated integrin {alpha}v{beta}3 cooperates with metalloproteinase MMP-9 in regulating migration of metastatic breast cancer cells PNAS, August 5, 2003; 100(16): 9482 - 9487. [Abstract] [Full Text] [PDF]

				R. Faccio, D. V. Novack, A. Zallone, F. P. Ross, and S. L. Teitelbaum Dynamic changes in the osteoclast cytoskeleton in response to growth factors and cell attachment are controlled by {beta}3 integrin J. Cell Biol., August 4, 2003; 162(3): 499 - 509. [Abstract] [Full Text] [PDF]