[Frontiers in Bioscience 2, d126-146, March 1, 1997]

	[Frontiers in Bioscience 2, d126-146, March 1, 1997] Reprints PubMed CAVEAT LECTOR
	FIBRONECTIN-INTEGRIN INTERACTIONS *Staffan Johansson, Gunbjørg Svineng, Krister Wennerberg, Annika Armulik, Lars Lohikangas* Department of Medical and Physiological Chemistry, The Biomedical Center, Box 575, S-751 23 Uppsala, Sweden Received 2/20/97; Accepted 2/27/97; On-line 3/1/97 GS and KW have made equally important and major contributions to this article. 2. INTRODUCTION* The interaction of cells with adhesion proteins in the extracellular matrix (ECM) provides signals which affect the morphology, motility, gene expression and survival of adherent cells (1-3). Many cell adhesion proteins have been identified and extensively characterized. In general, they are large, multifunctional mosaic proteins; some of them can be grouped into protein families, but otherwise they are structurally very diverse. Since each cell adhesion protein has specific effects on cells, their temporal and spatial deposition in ECMs is important for various normal and pathological processes such as formation, maintenance and remodeling of tissues, lymphocyte recirculation, thrombus formation, tumor formation and metastasis. In contrast to the ligands, most cellular receptors for adhesion proteins of the ECM belong to one protein family, the integrins (1). Additional adhesion receptors for the ECM clearly exist, e.g. dystroglycan (4, 5) and syndecans (6, 7), but the integrins have a dominating role in the anchoring of cells to the ECM. At present, 22 different integrins and several additional splice variants have been identified, a specific subset of them being expressed by each cell. Thus, the appropriate capacity for receiving information from ECMs of varying composition is available for the cells. The topic of this review is the interaction of one cell adhesion protein, fibronectin, with its various integrin receptors. The focus is on the mechanisms of ligand binding, and the importance of the interactions for fibronectin fibril formation. In addition, the in vivo effects in mouse of disruption of the genes for fibronectin and integrins subunits are discussed. For information about the intracellular responses following fibronectin-integrin interactions, other recent reviews are recommended (8-10).

[Frontiers in Bioscience 2, d126-146, March 1, 1997]
Reprints
PubMed
CAVEAT LECTOR

FIBRONECTIN-INTEGRIN INTERACTIONS

Staffan Johansson, Gunbjørg Svineng*, Krister Wennerberg*, Annika Armulik, Lars Lohikangas

Department of Medical and Physiological Chemistry, The Biomedical Center, Box 575, S-751 23 Uppsala, Sweden

Received 2/20/97; Accepted 2/27/97; On-line 3/1/97

*GS and KW have made equally important and major contributions to this article.

2. INTRODUCTION

The interaction of cells with adhesion proteins in the extracellular matrix (ECM) provides signals which affect the morphology, motility, gene expression and survival of adherent cells (1-3). Many cell adhesion proteins have been identified and extensively characterized. In general, they are large, multifunctional mosaic proteins; some of them can be grouped into protein families, but otherwise they are structurally very diverse. Since each cell adhesion protein has specific effects on cells, their temporal and spatial deposition in ECMs is important for various normal and pathological processes such as formation, maintenance and remodeling of tissues, lymphocyte recirculation, thrombus formation, tumor formation and metastasis.

In contrast to the ligands, most cellular receptors for adhesion proteins of the ECM belong to one protein family, the integrins (1). Additional adhesion receptors for the ECM clearly exist, e.g. dystroglycan (4, 5) and syndecans (6, 7), but the integrins have a dominating role in the anchoring of cells to the ECM. At present, 22 different integrins and several additional splice variants have been identified, a specific subset of them being expressed by each cell. Thus, the appropriate capacity for receiving information from ECMs of varying composition is available for the cells.

The topic of this review is the interaction of one cell adhesion protein, fibronectin, with its various integrin receptors. The focus is on the mechanisms of ligand binding, and the importance of the interactions for fibronectin fibril formation. In addition, the in vivo effects in mouse of disruption of the genes for fibronectin and integrins subunits are discussed. For information about the intracellular responses following fibronectin-integrin interactions, other recent reviews are recommended (8-10).