Signaling through Intercellular Adhesion Molecule 1 (ICAM-1) in a B Cell Lymphoma Line

Holland, Joanna; Owens, Trevor

doi:10.1074/jbc.272.14.9108

Cited by 88 publications

(37 citation statements)

References 46 publications

(35 reference statements)

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“…Although the biochemical link between ICAM-1 and PLC␥ phosphorylation is not known, ICAM-1-mediated PLC␥ 1 phosphorylation was abolished by pretreatment with herbimycin, a well known inhibitor of Src family kinases (not shown). Among these kinases, p53/p56 lyn , which is highly expressed in brain endothelial cells, has been shown to be strongly activated 1 min after ICAM-1 cross-linking in B cells (31). Because our results strongly suggest that Src is not the kinase responsible for PLC␥ 1 phosphorylation, the putative role of p53/ p56 lyn will need to be investigated in further studies.…”

Section: Discussionmentioning

confidence: 97%

ICAM-1-Coupled Cytoskeletal Rearrangements and Transendothelial Lymphocyte Migration Involve Intracellular Calcium Signaling in Brain Endothelial Cell Lines

Etienne-Manneville

Manneville

Adamson

et al. 2000

The Journal of Immunology

275

220

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Endothelium of the cerebral blood vessels, which constitutes the blood-brain barrier, controls adhesion and trafficking of leukocytes into the brain. Investigating signaling pathways triggered by the engagement of adhesion molecules expressed on brain endothelial cells using two rat brain endothelial cell lines (RBE4 and GP8), we report in this paper that ICAM-1 cross-linking induces a sustained tyrosine phosphorylation of the phosphatidylinositol-phospholipase C (PLC)γ1, with a concomitant increase in both inositol phosphate production and intracellular calcium concentration. Our results suggest that PLC are responsible, via a calcium- and protein kinase C (PKC)-dependent pathway, for p60Src activation and tyrosine phosphorylation of the p60Src substrate, cortactin. PKCs are also required for tyrosine phosphorylation of the cytoskeleton-associated proteins, focal adhesion kinase and paxillin, but not for ICAM-1-coupled p130Cas phosphorylation. PKC’s activation is also necessary for stress fiber formation induced by ICAM-1 cross-linking. Finally, cell pretreatment with intracellular calcium chelator or PKC inhibitors significantly diminishes transmonolayer migration of activated T lymphocytes, without affecting their adhesion to brain endothelial cells. In summary, our data demonstrate that ICAM-1 cross-linking induces calcium signaling which, via PKCs, mediates phosphorylation of actin-associated proteins and cytoskeletal rearrangement in brain endothelial cell lines. Our results also indicate that these calcium-mediated intracellular events are essential for lymphocyte migration through the blood-brain barrier.

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Section: Discussionmentioning

confidence: 97%

ICAM-1-Coupled Cytoskeletal Rearrangements and Transendothelial Lymphocyte Migration Involve Intracellular Calcium Signaling in Brain Endothelial Cell Lines

Etienne-Manneville

Manneville

Adamson

et al. 2000

The Journal of Immunology

275

220

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“…It is therefore possible that MT1-MMP-mediated cleavage of ICAM-1 may co-ordinate the TM process. Src and ERK signaling, an intrinsic part of ICAM-1-mediated adhesion and transmigration (29,35), are also implicated in MT1-MMP function (41,42) through its intracellular domain. Because the ICAM-1 cytoplasmic tyrosine mutations result in defective ERK signaling (7) and reduced TM (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…The cytoplasmic tail and the phosphoresidues regulate the ectodomain cleavage of ICAM-1 and EC survival (7). Therefore, monocyte TM through ICAM-1 ligation may be dependent on a variety of signals generated through the cytoplasmic interactions, and these could include mitogenactivated protein kinase (6, 7), Src, pCas (35), and effectors such as the small GTPase, Rho (36). The cytoplasmic tail of ICAM-1 directly associates with SHP-2 (6) and the actin-binding protein, ␣-actinin (37).…”

Section: Discussionmentioning

confidence: 99%

Membrane-type 1-Matrix Metalloproteinase Regulates Intracellular Adhesion Molecule-1 (ICAM-1)-mediated Monocyte Transmigration

Sithu

English

Olson

et al. 2007

Journal of Biological Chemistry

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The migration of leukocytes through the endothelium to sites of infection or inflammation is a key process for the maintenance of physiological defense mechanisms. When this process is dis-regulated and becomes chronic, inflammatory diseases such as arteriosclerosis and arthritis manifest. The steps in leukocyte transmigration (TM) 5 are initiated though activation of the endothelial cells (ECs) by cytokines such as TNF-␣, interleukin-1, and interleukin-6. The selectins initiate the rolling and tethering of leukocytes to the endothelium. This step permits the engagement between ␤ 2 and ␤ 1 integrins with intercellular cell adhesion molecule (ICAM-1) and vascular cell adhesion molecule (VCAM-1) to allow firm adhesion and spreading of leukocytes. ECs express low levels of ICAM-1 and VCAM-1, but cytokine stimulation elevates the expression of these receptors on ECs. The migration of leukocytes through the EC barrier involves platelet endothelial cell adhesion molecule-1 and junctional adhesion molecules. Finally, proteolytic degradation of the basement membrane extracellular matrix by metalloproteinases (MPs) in particular is required to promote extravasation (reviewed in Refs. 1 and 2).Although ICAM-1, VCAM-1, and platelet endothelial cell adhesion molecule-1 play an important role in in vivo and in vitro experimental models of TM (1-4), there is little data on the mechanistic role of the individual adhesion molecules. ICAM-1 comprises of five immunoglobulin-like motifs on the extracellular surface, followed by a stem, a transmembrane domain, and a short cytoplasmic tail (5). The cytoplasmic tail contains three tyrosine residues, two of which become phosphorylated at positions 485 and 474 upon ligation to modulate ICAM-1 function (6, 7). The role of these residues in leukocyteendothelial migration has not yet been defined.Proteolysis is an important step during and after transmigration (8, 9), as degradation of the basement membrane and matrix of the media (of larger vessels) or stroma is required. The zinc-dependent MPs belonging to the metzincin family possess a highly conserved catalytic domain, yet have an enormous * This work was supported in part by National Institutes of Health Grant PO1ES011860, the Jewish Hospital Foundation, Louisville (to S. E. D.), and an American Heart Association Postdoctoral Award (to S. D. S.) from the Ohio Valley Affiliate. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

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“…3). Several reports suggest that cross-linking ICAM-1 induces secretion of chemokines and cytokines (4,5), calcium mobilization (6), and expression of MHC class II (7). Activation of p60 src and p53/ 56 lyn , along with transient inhibition of cdc2 kinase activity, has also been demonstrated following ICAM-1 engagement (7-9).…”

Section: Vcam-1 Activates Phosphatidylinositol 3-kinase and Induces P120mentioning

confidence: 99%

VCAM-1 Activates Phosphatidylinositol 3-Kinase and Induces p120CblPhosphorylation in Human Airway Smooth Muscle Cells

Lazaar

Krymskaya

Das

2001

The Journal of Immunology

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VCAM-1 is a member of the Ig superfamily of receptors the expression of which is up-regulated on human airway smooth muscle (ASM) cells following stimulation with inflammatory mediators. The function of these receptors in adhesion is well known, but there is growing recognition that they also possess “outside-in” signaling functions, such as cytoskeletal reorganization, calcium mobilization, and cytokine release. The present study examined the activation of extracellular signal-regulated kinase and phosphatidylinositol 3-kinase (PI3K) in ASM cells following VCAM-1 engagement. VCAM-1 ligation activated extracellular signal-regulated kinase 2 and resulted in increased expression of cyclin D1, yet there was neither p27kip1 degradation nor an increase in smooth muscle cell DNA synthesis. VCAM-1 ligation, however, augmented the proliferative response to submitogenic concentrations of epidermal growth factor. VCAM-1 engagement also stimulated a rapid increase in PI3K activity. This was associated with phosphorylation of the adapter protein p120Cbl and an increase in Cbl-associated PI3K activity. These studies suggest that VCAM-1 is linked to multiple signaling pathways in human ASM cells and may function to augment growth factor-induced responses.

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Signaling through Intercellular Adhesion Molecule 1 (ICAM-1) in a B Cell Lymphoma Line

Cited by 88 publications

References 46 publications

ICAM-1-Coupled Cytoskeletal Rearrangements and Transendothelial Lymphocyte Migration Involve Intracellular Calcium Signaling in Brain Endothelial Cell Lines

ICAM-1-Coupled Cytoskeletal Rearrangements and Transendothelial Lymphocyte Migration Involve Intracellular Calcium Signaling in Brain Endothelial Cell Lines

Membrane-type 1-Matrix Metalloproteinase Regulates Intracellular Adhesion Molecule-1 (ICAM-1)-mediated Monocyte Transmigration

VCAM-1 Activates Phosphatidylinositol 3-Kinase and Induces p120CblPhosphorylation in Human Airway Smooth Muscle Cells

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