NDLI: Vascular Cell Adhesion Molecule (VCAM)-Ig Fusion Protein Defines Distinct Affinity States of the Very Late Antigen-4 (VLA-4) Receptor

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Vascular Cell Adhesion Molecule (VCAM)-Ig Fusion Protein Defines Distinct Affinity States of the Very Late Antigen-4 (VLA-4) Receptor

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Vascular Cell Adhesion Molecule (VCAM)-Ig Fusion Protein Defines Distinct Affinity States of the Very Late Antigen-4 (VLA-4) Receptor

Content Provider	Taylor & Francis Online
Author	Bixler, Sarah Lobb, Roy Jakubowski, Aniela Burkly, Linda C. Rosa, Margaret D.
Abstract	The Very Late Antigen-4 receptor (VLA-4) (α4β1) is constitutively expressed on leukocytes and plays a role in cell trafficking, activation and development through its interaction with two alternative ligands, Vascular Cell Adhesion Molecule (VCAM-1) and fibronectin (FN). VLA-4-dependent cell adhesion is augmented by various stimuli, such as divalent cations, certain β1-specific monoclonal antibodies (mAbs) and cell activation. However, the steps of the adhesive process which they affect are currently undefined. In order to investigate whether or not these stimuli affect the primary step, VLA-4/ligand binding, we employed a recombinant VCAM-IgG fusion protein (VCAM-Ig) as a soluble ligand for VLA-4. Using this soluble ligand, we have directly demonstrated that the VLA-4 receptor can exist in at least three different affinity states on the cell surface. Two distinct high affinity states are induced on normal peripheral blood T cells, one by the anti-α1 mAb TS2/16, and one of 15–20 fold higher affinity by the divalent cation Mn2+. Interestingly, activation through the T cell receptor (TcR), through CD31 or by the Macrophage Inflammatory Protein-1β chemokine (MIP-1β) do not detectably increase VLA-4 affinity although they do augment VLA-4 dependent cell adhesion in vitro. Thus, VCAM-Ig binding defines high affinity VLA-4 receptors, revealing unique effects of the TS2/16 mAb and Mn2+ cations in vitro, and distinguishes VLA-4/VCAM interactions from subsequent steps in cell adhesion.
Starting Page	131
Ending Page	142
Page Count	12
File Format	PDF HTM / HTML
ISSN	10292314
DOI	10.3109/15419069509081282
Journal	Cell Communication & Adhesion
Volume Number	3
Issue Number	2
Language	English
Publisher	Taylor & Francis
Publisher Date	2009-07-11
Access Restriction	Open
Subject Keyword	VLA-4 VCAM-1 Affinity states Integrin binding
Content Type	Text
Resource Type	Article

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