Adhesion of T and B lymphocytes to extracellular matrix and endothelial cells can be regulated through the beta subunit of VLA

Kemenade, E. van de Wiel-van; Kooyk, Yvette van; Boer, Annemiek J. de; Huijbens, R.J.F.; Weder, Pauline; Kasteele, Willeke van de; Melief, Cornelis J.M.; Figdor, Carl G.

doi:10.1083/jcb.117.2.461

Cited by 130 publications

(49 citation statements)

References 53 publications

(51 reference statements)

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“…Harlan (Beatty et al, 1983). The anti-132 mAb KIM185 (IgGl) was used to activate 12 integrins (Andrew et al, 1993) and the anti-,61 mAb TS2/16 to activate ,13 integrins (Hemler et al, 1984;van de Wiel-van Kemenade et al, 1992). The anti-a5 mAb SAM-1 (IgGl) was used to block very late antigen 5-dependent adhesion (Keizer et al, 1987).…”

Section: Materials and Methods Mabsmentioning

confidence: 99%

“…LFA-1 /ICAM-1 adhesion requires activation of LFA-1 through intracellular signals (Martz, 1987;Dustin and Springer, 1989; Kooyk et al, 1989;Hynes, 1992). This activation process, termed "inside-out" signaling, is common to all integrins including the ,B and (37 integrins (Keizer et al, 1988;Dustin and Springer, 1989; Kooyk et al, 1989;Altieri, 1991;Dransfield et al, 1992b;Andrew et al, 1993;Landis et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

“…This activation process, termed "inside-out" signaling, is common to all integrins including the ,B and (37 integrins (Keizer et al, 1988;Dustin and Springer, 1989; Kooyk et al, 1989;Altieri, 1991;Dransfield et al, 1992b;Andrew et al, 1993;Landis et al, 1993). Activation of LFA-1 is thought to result in a conformational change in the a/P heterodimer, leading to an enhanced binding affinity LFA-1 for its ligand ICAM-1 (Lollo et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

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Cytoplasmic tails of beta 1, beta 2, and beta 7 integrins differentially regulate LFA-1 function in K562 cells.

Lub

Vliet

Oomen

et al. 1997

MBoC

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The 132 integrin lymphocyte function-associated antigen 1 (LFA-1) mediates activationdependent adhesion of lymphocytes. To investigate whether lymphocyte-specific elements are essential for LFA-1 function, we expressed LFA-1 in the erythroleukemic cell line K562, which expresses only the integrin very late antigen 5. We observed that LFA-l-expressing K562 cannot bind to intercellular adhesion molecule 1-coated surfaces when stimulated by phorbol 12-myristate 13-acetate (PMA), whereas the LFA-1-activating antibody KIM185

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Section: Materials and Methods Mabsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Cytoplasmic tails of beta 1, beta 2, and beta 7 integrins differentially regulate LFA-1 function in K562 cells.

Lub

Vliet

Oomen

et al. 1997

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“…The ubiquitously expressed ECM molecule FN, present in human plasma and tissues, is up-regulated during inflammatory responses and is a ligand for the g 1 integrins VLA-4 and VLA-5 [17], whereas the coagulation product Fb is a well-known ligand for CD11b/CD18 on neutrophils. We studied the role of g 1 integrins more extensively using mAb 8A2 and TS2/16, which bind and activate the g 1 subunit [18,19]. In lymphocytes and eosinophilic granulocytes, mAb 8A2 can induce increased cell binding via VLA-4 and VLA-5 to the vascular ligand VCAM-1 and the ECM protein FN [20].…”

Section: Introductionmentioning

confidence: 99%

β 1 integrin activation on human neutrophils promotes β 2 integrin-mediated adhesion to fibronectin

Berg¹,

Mul²,

Schippers³

et al. 2001

Eur. J. Immunol.

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Although the importance of g 1 integrin-mediated binding to adhesion molecules and extracellular matrix (ECM) molecules is well established for most types of leukocytes, the expression patterns and functional importance of g 1 integrins on neutrophils have remained controversial. Using flow cytometry, we found that human neutrophils express the § 4 , § 5 , § 9 and g 1 integrin subunits. To examine whether the integrins VLA-4 ( § 4 / g 1 ) and VLA-5 ( § 5 / g 1 ) have a functional role on neutrophils, we studied adhesion to their ligand fibronectin. Treatment of neutrophils with antibody 8A2, which specifically binds and activates g 1 integrins, resulted in increased binding to fibronectin. However, addition of blocking mAb revealed that 8A2-induced adhesion did not depend on g 1 integrins, but on the g 2 integrin CD11b/CD18. Similarly, activation of g 1 integrins by 8A2 resulted in CD11b-dependent binding of neutrophils to fibrinogen. 8A2 treatment increased expression of an activation epitope of CD11b/CD18, which depended on phosphoinositide 3-OH kinase activity and an adequate concentration of intracellular free Ca 2+ . These data suggest that engagement of g 1 integrins on neutrophils results in a cross-talk signal that leads to activation of the g 2 integrin CD11b/CD18, followed by CD11b-mediated adhesion. As transmigrated neutrophils are surrounded by both g 1 and g 2 ligands in the ECM, this integrin cross-talk could play a role in modifying migration and cellular activation in inflamed tissues.

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“…Certain ␤1 subunit-specific monoclonal antibodies (mAbs) stimulate ligand-binding activities. mAbs 8A2 and Ts2/16 have been shown to stimulate high-avidity ligand binding of ␤1 integrins on eosinophils, T and B lymphocytes, myelomonocytic cell line U937, and melanoma A375 (Arroyo et al, 1992;Kovach et al, 1992;van de Wiel-van Kemenade et al, 1992;Arroyo et al, 1993;Kuijpers et al, 1993; SanchezMateos et al, 1993;Faull et al, 1994). In the presence of Ts2/16, the ␣2␤1 on K562 cells was stimulated to bind both collagen and laminin (Chan and Hemler, 1993).…”

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confidence: 99%

Modulation of In Vivo Migratory Function of α2β1 Integrin in Mouse Liver

Heinemann

Hangan

et al. 1997

MBoC

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We report herein that expression of ␣2␤1 integrin increased human erythroleukemia K562 transfectant (KX2C2) cell movement after extravasation into liver parenchyma. In contrast, a previous study demonstrated that ␣2␤1 expression conferred a stationary phenotype to human rhabdomyosarcoma RD transfectant (RDX2C2) cells after extravasation into the liver. We therefore assessed the adhesive and migratory function of ␣2␤1 on KX2C2 and RDX2C2 cells using a ␣2␤1-specific stimulatory monoclonal antibody (mAb), JBS2, and a blocking mAb, BHA2.1. In comparison with RDX2C2 cells, KX2C2 were only weakly adherent to collagen and laminin. JBS2 stimulated ␣2␤1-mediated interaction of KX2C2 cells with both collagen and laminin resulting in increases in cell movement on both matrix proteins. In the presence of Mn 2ϩ , JBS2-stimulated adhesion on collagen beyond an optimal level for cell movement. In comparison, an increase in RDX2C2 cell movement on collagen required a reduction in its adhesive strength provided by the blocking mAb BHA2.1. Consistent with these in vitro findings, in vivo videomicroscopy revealed that ␣2␤1-mediated postextravasation cell movement of KX2C2 cells in the liver tissue could also be stimulated by JBS2. Thus, results demonstrate that ␣2␤1 expression can modulate postextravasation cell movement by conferring either a stationary or motile phenotype to different cell types. These findings may be related to the differing metastatic activities of different tumor cell types. INTRODUCTIONIt is well established that ␤1 integrins represent the major receptors for providing the functional linkage between extracellular matrix (ECM) proteins and cytoskeletal components (for review, Hynes, 1992). The expression of ␣2␤1 integrin as receptors for collagen and laminin has been associated with the morphogenesis of mammary epithelial cells (Berdichevsky et al., 1992; Keely et al., 1995a,b) and differentiation of the human erythroleukemia cell line K562 (Burger et al., 1992). In comparison, ␣2␤1 expression was down-regulated on keratinocytes undergoing terminal differentiation (Adams and Watt, 1990). In addition, ␣2␤1 has also been associated with the metastatic activities of tumor cells. Interestingly, there is both a direct correlation (Dedhar and Saulnier, 1990;Chan et al., 1991;Klein et al., 1991;Mortarini et al., 1991;Danen et al., 1993;Chen et al., 1994;Santala et al., 1994) and an inverse correlation (Pignatelli et al., 1990(Pignatelli et al., , 1991Zutter, et al., 1990Zutter, et al., , 1995 of ␣2␤1 expression with tumor metastasis. The exact mechanisms whereby ␣2␤1 enhances or, in some cases, reduces the metastatic activities of tumor cells are still unclear. One possibility is that ␣2␤1 may confer distinct cell functions among the tumor cells. The present study focuses on ␣2␤1 interaction with ECM proteins and its in vivo effect on cell movement.Studies in recent years have demonstrated three distinct modes of ligand binding for ␣2␤1: no ligandbinding activity, binding collagen but not laminin, and binding both ...

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Adhesion of T and B lymphocytes to extracellular matrix and endothelial cells can be regulated through the beta subunit of VLA

Cited by 130 publications

References 53 publications

Cytoplasmic tails of beta 1, beta 2, and beta 7 integrins differentially regulate LFA-1 function in K562 cells.

Cytoplasmic tails of beta 1, beta 2, and beta 7 integrins differentially regulate LFA-1 function in K562 cells.

β 1 integrin activation on human neutrophils promotes β 2 integrin-mediated adhesion to fibronectin

Modulation of In Vivo Migratory Function of α2β1 Integrin in Mouse Liver

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