Protein I/II of Oral Viridans Streptococci Increases Expression of Adhesion Molecules on Endothelial Cells and Promotes Transendothelial Migration of Neutrophilsin Vitro

1998 ◽  
Vol 187 (2) ◽  
pp. 145-150 ◽  
Author(s):  
Aline Vernier-Georgenthum ◽  
Souad Al-Okla ◽  
Bénédicte Gourieux ◽  
Jean-Paul Klein ◽  
Dominique Wachsmann
Keyword(s):  
Endothelial Cells ◽  
Adhesion Molecules ◽  
Transendothelial Migration ◽  
Viridans Streptococci

Stromal Derived Factor-1–Induced Chemokinesis of Cord Blood CD34+ Cells (Long-Term Culture-Initiating Cells) Through Endothelial Cells Is Mediated by E-Selectin

Blood ◽  
1999 ◽  
Vol 94 (12) ◽  
pp. 4011-4019 ◽  
Author(s):  
Afzal J. Naiyer ◽  
Deog-Yeon Jo ◽  
Jongcheol Ahn ◽  
Robert Mohle ◽  
Mario Peichev ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Adhesion Molecules ◽  
Constitutive Expression ◽  
Transendothelial Migration ◽  
Hematopoietic Stem ◽  
Long Term Culture ◽  
Migration System ◽  
Cd34 Cells

Abstract Homing of hematopoietic stem cells to the bone marrow (BM) involves sequential interaction with adhesion molecules expressed on BM endothelium (BMEC) and chemokine stromal derived factor-1 (SDF-1). However, the mechanism whereby adhesion molecules regulate the SDF-1–induced transendothelial migration process is not known. E-selectin is an endothelial-specific selectin that is constitutively expressed by the BMEC in vivo. Hence, we hypothesized that E-selectin may mediate SDF-1–induced transendothelial migration of CD34+ cells. We show that CD34+ cells express both E-selectin ligand and fucosyltransferase-VII (FucT-VII). Soluble E-selectin–IgG chimera binds avidly to 75% ± 10% of CD34+ cells composed mostly of progenitors and cells with long-term culture-initiating cell (LTC-IC) potential. To assess the functional capacity of E-selectin to mediate CD34+ cell migration in a transendothelial migration system, CD34+ cells were placed on transwell plates coated with interleukin-1β–activated BMEC. In the absence of SDF-1, there was spontaneous migration of 7.0% ± 1.4% of CD34+ cells and 14.1% ± 2.2% of LTC-IC. SDF-1 induced migration of an additional 23.0% ± 4.4% of CD34+cells and 17.6% ± 3.6% of LTC-IC. Blocking MoAb to E-selectin inhibited SDF-1–induced migration of CD34+ cells by 42.0% ± 2.5% and LTC-IC by 90.9% ± 16.6%. To define the mechanism of constitutive expression of E-selectin by the BMEC in vivo, we have found that vascular endothelial growth factor (VEGF165) induces E-selectin expression by cultured endothelial cells. VEGF-stimulated endothelial cells support transendothelial migration of CD34+ cells that could be blocked by MoAb to E-selectin. These results suggest that trafficking of subsets of CD34+ cells with LTC-IC potential is determined in part by sequential interactions with E-selectin and SDF-1.

scholarly journals ICAM-1 Clustering on Endothelial Cells Recruits VCAM-1

2010 ◽  
Vol 2010 ◽  
pp. 1-9 ◽  
Author(s):  
Jaap D. van Buul ◽  
Jos van Rijssel ◽  
Floris P. J. van Alphen ◽  
Anna-Marieke van Stalborch ◽  
Erik P. J. Mul ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Adhesion Molecules ◽  
Lipid Rafts ◽  
Leukocyte Adhesion ◽  
Transendothelial Migration ◽  
Human Endothelial Cells ◽  
Strong Adhesion ◽  
Integrin Ligands

In the initial stages of transendothelial migration, leukocytes use the endothelial integrin ligands ICAM-1 and VCAM-1 for strong adhesion. Upon adhesion of the leukocyte to endothelial ICAM-1, ICAM-1 is clustered and recruited to the adhered leukocyte, promoting strong adhesion. In this study, we provide evidence for the colocalization of VCAM-1 at sites of ICAM-1 clustering. Anti-ICAM-1 antibody-coated beads were used to selectively cluster and recruit ICAM-1 on primary human endothelial cells. In time, co-localization of ICAM-1 and VCAM-1 around the adherent beads was observed. Biochemical pull-down assays showed that ICAM-1 clustering induced its association to VCAM-1, suggesting a physical link between these two adhesion molecules. The association was partly dependent on lipid rafts as well as on F-actin and promoted adhesion. These data show that VCAM-1 can be recruited, in an integrin-independent fashion, to clustered ICAM-1 which may serve to promote ICAM-1-mediated leukocyte adhesion.

Changes in the distribution of LFA-1, catenins, and F-actin during transendothelial migration of monocytes in culture

1997 ◽  
Vol 110 (22) ◽  
pp. 2807-2818 ◽  
Author(s):  
M. Sandig ◽  
E. Negrou ◽  
K.A. Rogers
Keyword(s):  
Endothelial Cells ◽  
Endothelial Cell ◽  
Adhesion Molecules ◽  
Laser Scanning ◽  
Transendothelial Migration ◽  
Cell Contact ◽  
Beta Catenin ◽  
Immunofluorescence Labeling ◽  
Cell Cell

To determine changes in the spatial and temporal distribution of cell-cell adhesion molecules during transendothelial migration of monocytes, we examined an in vitro model system of diapedesis using high resolution laser scanning confocal microscopy. Human arterial endothelial cells were cultured to confluence on coverslips coated with Matrigel and activated with IL-1beta before the addition of monocytic THP-1 cells. Seventy per cent of monocytes transmigrated through the endothelium within one hour. Diapedesis, but not adhesion and spreading, was inhibited 8-fold in co-cultures that contained endothelial cell conditioned medium, suggesting the release of an endothelial derived inhibitor. Double immunofluorescence labeling with antibodies to LFA-1, alpha- and beta-catenin, VE-cadherin and with Texas Red phalloidin, identified a circular transmigration passage in endothelial cell-cell contact regions. This passage was formed by an LFA-1-containing pseudopodium that penetrated between endothelial cells. Apical to the transmigration passage, monocytes remained round in shape, while underneath the endothelium, they spread along the Matrigel. The margins of the transmigration passage contained high levels of LFA-1 and F-actin, suggesting a major role of these molecules during the transmigration process itself. Endothelial adherens junctions, as judged by the presence of VE-cadherin and alpha-catenin adjacent to the passage, remained intact during diapedesis. The presence of catenins at heterotypic contact regions between monocytes and endothelial cells during diapedesis suggested cadherin-mediated interactions between the two cell types. These results reveal dynamic changes in the distribution of adhesion molecules and the actin cytoskeleton during monocyte transendothelial migration in culture.

Stromal Derived Factor-1–Induced Chemokinesis of Cord Blood CD34+ Cells (Long-Term Culture-Initiating Cells) Through Endothelial Cells Is Mediated by E-Selectin

Blood ◽  
1999 ◽  
Vol 94 (12) ◽  
pp. 4011-4019 ◽  
Author(s):  
Afzal J. Naiyer ◽  
Deog-Yeon Jo ◽  
Jongcheol Ahn ◽  
Robert Mohle ◽  
Mario Peichev ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Adhesion Molecules ◽  
Constitutive Expression ◽  
Transendothelial Migration ◽  
Hematopoietic Stem ◽  
Long Term Culture ◽  
Migration System ◽  
Cd34 Cells

Homing of hematopoietic stem cells to the bone marrow (BM) involves sequential interaction with adhesion molecules expressed on BM endothelium (BMEC) and chemokine stromal derived factor-1 (SDF-1). However, the mechanism whereby adhesion molecules regulate the SDF-1–induced transendothelial migration process is not known. E-selectin is an endothelial-specific selectin that is constitutively expressed by the BMEC in vivo. Hence, we hypothesized that E-selectin may mediate SDF-1–induced transendothelial migration of CD34+ cells. We show that CD34+ cells express both E-selectin ligand and fucosyltransferase-VII (FucT-VII). Soluble E-selectin–IgG chimera binds avidly to 75% ± 10% of CD34+ cells composed mostly of progenitors and cells with long-term culture-initiating cell (LTC-IC) potential. To assess the functional capacity of E-selectin to mediate CD34+ cell migration in a transendothelial migration system, CD34+ cells were placed on transwell plates coated with interleukin-1β–activated BMEC. In the absence of SDF-1, there was spontaneous migration of 7.0% ± 1.4% of CD34+ cells and 14.1% ± 2.2% of LTC-IC. SDF-1 induced migration of an additional 23.0% ± 4.4% of CD34+cells and 17.6% ± 3.6% of LTC-IC. Blocking MoAb to E-selectin inhibited SDF-1–induced migration of CD34+ cells by 42.0% ± 2.5% and LTC-IC by 90.9% ± 16.6%. To define the mechanism of constitutive expression of E-selectin by the BMEC in vivo, we have found that vascular endothelial growth factor (VEGF165) induces E-selectin expression by cultured endothelial cells. VEGF-stimulated endothelial cells support transendothelial migration of CD34+ cells that could be blocked by MoAb to E-selectin. These results suggest that trafficking of subsets of CD34+ cells with LTC-IC potential is determined in part by sequential interactions with E-selectin and SDF-1.

Endothelial adapter proteins in leukocyte transmigration

2009 ◽  
Vol 101 (04) ◽  
pp. 649-655 ◽  
Author(s):  
Jaap van Buul ◽  
Peter Hordijk
Keyword(s):  
Endothelial Cells ◽  
Cell Surface ◽  
Adhesion Molecules ◽  
Transendothelial Migration ◽  
Short Review ◽  
Adapter Proteins ◽  
Adapter Protein ◽  
Surface Adhesion ◽  
Leukocyte Transmigration ◽  
Leukocyte Transendothelial Migration

SummaryLeukocyte transendothelial migration (TEM) requires endothelial signalling. This signalling is initiated by clustering of cell-surface adhesion molecules and transmitted into the endothelium by a group of associated or co-clustered adapter proteins. These adapter proteins, such as cortactin and filamin, connect the adhesion molecules to the actin cytoskeleton as well as to signalling enzymes and downstream pathways. This short review aims to define common themes in adapter protein binding in endothelial cells and to propose critical functions that are exerted by these adapters in leukocyte transendothelial migration.

The roles of adhesion molecules and proteinases in lymphocyte transendothelial migration

1996 ◽  
Vol 74 (6) ◽  
pp. 749-757 ◽  
Author(s):  
Joseph A. Madri ◽  
Donnasue Graesser ◽  
Tara Haas
Keyword(s):  
T Cells ◽  
Endothelial Cells ◽  
Endothelial Cell ◽  
T Cell ◽  
Matrix Metalloproteinase ◽  
Adhesion Molecules ◽  
Cell Monolayer ◽  
Transendothelial Migration ◽  
Matrix Metalloproteinase 2

T cell extravasation into perivascular tissue during inflammation involves transmigration through the endothelial cell (EC) layer and basement membrane. We have demonstrated that matrix metalloproteinase-2 (MMP-2) is induced in T cells upon adhesion to endothelial cells and that the induction of MMP-2 is mediated by binding of T cell VLA-4 to VCAM-1. Cloned murine Th1 cells antigenic to myelin basic protein, either expressing VLA-4 on their cell surface and causing experimental autoimmune encephalomyelitis (EAE) or not expressing VLA-4 and not causing EAE, were used. VLA-4 positive (+) T cells that adhered to VCAM-1 positive (+) endothelial cells exhibited an induction in MMP-2 mRNA, protein, and activity, whereas MMP-2 was not induced in the T cells that adhered to the VCAM-1 negative (−) endothelial cells or VLA-4 negative (−) T cells that adhered to VCAM-1+ endothelial cells. Incubating T cells with rVCAM-1-coated dishes showed that VLA-4+ T cells adhered to the molecule and that adhesion to rVCAM-1 was sufficient to induce MMP-2. VLA-4+ T cells that had transmigrated through a VCAM-1+ endothelial cell monolayer exhibited MMP-2 activity. TTMP-2 was shown to reduce T cell transmigration in vitro. Transmigrated T cells exhibited downregulation of VLA-4 and LFA-1 integrin surface expression and decreased binding to rVCAM-1 and rICAM-1 and increased binding to collagens I and IV, fibronectin, and laminin. Brain sections of mice demonstrated that as T cells migrated farther into the tissue, VLA-4 expression was lost, although CD4 expression remained unchanged. These results demonstrate that binding to VCAM-1 on endothelial cells induces MMP-2 in T cells, which, in turn, may facilitate T cell migration into perivascular tissue. The significance of these findings in the modulation of the inflammatory response is discussed.Key words: T lymphocyte, endothelial cell, matrix metalloproteinase, inflammation, transendothelial migration, integrins, cell adhesion molecules.

ROCK2 Regulates the Expression of Cell Adhesion Molecules and Cell-to-Cell Adhesion in Vascular Endothelial Cells

Diabetes ◽  
2018 ◽  
Vol 67 (Supplement 1) ◽  
pp. 476-P
Author(s):  
YUSUKE TAKEDA ◽  
KEIICHIRO MATOBA ◽  
DAIJI KAWANAMI ◽  
YOSUKE NAGAI ◽  
TOMOYO AKAMINE ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Cell Adhesion ◽  
Adhesion Molecules ◽  
Cell Adhesion Molecules ◽  
Vascular Endothelial Cells ◽  
Vascular Endothelial ◽  
Cell To Cell Adhesion

scholarly journals Poldip2 controls leukocyte infiltration into the ischemic brain by regulating focal adhesion kinase-mediated VCAM-1 induction

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Lori N. Eidson ◽  
Qingzeng Gao ◽  
Hongyan Qu ◽  
Daniel S. Kikuchi ◽  
Ana Carolina P. Campos ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Cerebral Ischemia ◽  
Focal Adhesion Kinase ◽  
Adhesion Molecules ◽  
Focal Adhesion ◽  
Vascular Inflammation ◽  
Leukocyte Recruitment ◽  
Ischemic Brain ◽  
Inflammatory Monocytes

AbstractStroke is a multiphasic process involving a direct ischemic brain injury which is then exacerbated by the influx of immune cells into the brain tissue. Activation of brain endothelial cells leads to the expression of adhesion molecules such vascular cell adhesion molecule 1 (VCAM-1) on endothelial cells, further increasing leukocyte recruitment. Polymerase δ-interacting protein 2 (Poldip2) promotes brain vascular inflammation and leukocyte recruitment via unknown mechanisms. This study aimed to define the role of Poldip2 in mediating vascular inflammation and leukocyte recruitment following cerebral ischemia. Cerebral ischemia was induced in Poldip2+/+ and Poldip2+/− mice and brains were isolated and processed for flow cytometry or RT-PCR. Cultured rat brain microvascular endothelial cells were used to investigate the effect of Poldip2 depletion on focal adhesion kinase (FAK)-mediated VCAM-1 induction. Poldip2 depletion in vivo attenuated the infiltration of myeloid cells, inflammatory monocytes/macrophages and decreased the induction of adhesion molecules. Focusing on VCAM-1, we demonstrated mechanistically that FAK activation was a critical intermediary in Poldip2-mediated VCAM-1 induction. In conclusion, Poldip2 is an important mediator of endothelial dysfunction and leukocyte recruitment. Thus, Poldip2 could be a therapeutic target to improve morbidity following ischemic stroke.

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