Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/6790
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Type: Journal article
Title: Integrin Expression and Function on Human Osteoblast-like Cells
Author: Gronthos, S.
Stewart, K.
Graves, S.
Hay, S.
Simmons, P.
Citation: Journal of Bone and Mineral Research, 1997; 12(8):1189-1197
Publisher: WILEY
Issue Date: 1997
ISSN: 0884-0431
1523-4681
Abstract: The integrin family of cell adhesion molecules are a series of cell surface glycoproteins that recognize a range of cell surface and extracellular matrix (ECM)-associated ligands. To date, the precise role of individual integrin molecules in bone cell-ECM interactions remains unclear. Cell binding assays were performed to examine the ability of normal human bone cells (NHBCs) to adhere to different ECM proteins in vitro. NHBCs displayed preferential adhesion to fibronectin over collagen types I, IV, and vitronectin and showed low affinity binding to laminin and collagen type V. No binding was observed to collagen type III. The integrin heterodimers alpha 1 beta 1, alpha 2 beta 1, alpha 3 beta 1, alpha 5 beta 1, alpha v beta 3, and alpha v beta 5 were found to be constitutively expressed on the cell surface of NHBCs by flow cytometric analysis. The integrins alpha 4 beta 1 and alpha 6 beta 1 were not expressed by NHBCs. Subsequent binding studies showed that NHBC adhesion to collagen and laminin was mediated by multiple integrins where cell attachment was almost completely inhibited in the presence of a combination of function-blocking monoclonal antibodies (Mabs) to alpha 1 beta 1, alpha 2 beta 1, alpha 3 beta 1, and beta 1. In contrast, the adhesion of NHBCs to fibronectin was only partially inhibited (50%) in the presence of blocking Mabs to alpha 3 beta 1, alpha 5 beta 1, and beta 1. The attachment of NHBCs to collagen, laminin, fibronectin, and vitronectin was also found to be unaffected in the presence of a function-blocking Mab to alpha v beta 3. The results of this study indicate that beta 1 integrins appear to be the predominant adhesion receptor subfamily utilized by human osteoblast-like cells to adhere to collagen and laminin and in part to fibronectin.
Keywords: Tibia
Cells, Cultured
Extracellular Matrix
Osteoblasts
Humans
Collagen
Vitronectin
Fibronectins
Laminin
Integrins
Antibodies, Monoclonal
Ligands
Fluorescent Antibody Technique, Indirect
Flow Cytometry
Analysis of Variance
Cell Adhesion
Binding Sites
Dimerization
Adult
Male
DOI: 10.1359/jbmr.1997.12.8.1189
Appears in Collections:Aurora harvest
Orthopaedics and Trauma publications

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