Lymphocyte Adhesion Mediated by VLA (Beta 1) Integrins

2015 ◽  
pp. 34-54 ◽  
Author(s):  
Yoji Shimizu ◽  
Stephen Shaw
Keyword(s):  
Lymphocyte Adhesion

scholarly journals Lymphocyte Adhesion to Psoriatic Dermal Endothelium: Mechanism and Modulation

1990 ◽  
Vol 95 (5) ◽  
pp. S29-S31 ◽  
Author(s):  
Yee-Hon Chin ◽  
Vincent Falanga ◽  
Jian-Ping Cai
Keyword(s):  
Lymphocyte Adhesion

scholarly journals PLCε1 regulates SDF-1α–induced lymphocyte adhesion and migration to sites of inflammation

2017 ◽  
Vol 114 (10) ◽  
pp. 2693-2698 ◽  
Author(s):  
Marianne Strazza ◽  
Inbar Azoulay-Alfaguter ◽  
Michael Peled ◽  
Alan V. Smrcka ◽  
Edward Y. Skolnik ◽  
...  
Keyword(s):  
T Cell ◽  
Small Gtpase ◽  
The Body ◽  
Delayed Type Hypersensitivity ◽  
Intercellular Adhesion Molecule ◽  
Intercellular Adhesion Molecule 1 ◽  
Regional Lymph Nodes ◽  
Lymphocyte Adhesion ◽  
Enzymatic Function ◽  
And Migration

Regulation of integrins is critical for lymphocyte adhesion to endothelium and migration throughout the body. Inside-out signaling to integrins is mediated by the small GTPase Ras-proximate-1 (Rap1). Using an RNA-mediated interference screen, we identified phospholipase Cε 1 (PLCε1) as a crucial regulator of stromal cell-derived factor 1 alpha (SDF-1α)-induced Rap1 activation. We have shown that SDF-1α-induced activation of Rap1 is transient in comparison with the sustained level following cross-linking of the antigen receptor. We identified that PLCε1 was necessary for SDF-1α-induced adhesion using shear stress, cell morphology alterations, and crawling on intercellular adhesion molecule 1 (ICAM-1)–expressing cells. Structure–function experiments to separate the dual-enzymatic function of PLCε1 uncover necessary contributions of the CDC25, Pleckstrin homology, and Ras-associating domains, but not phospholipase activity, to this pathway. In the mouse model of delayed type hypersensitivity, we have shown an essential role for PLCε1 in T-cell migration to inflamed skin, but not for cytokine secretion and proliferation in regional lymph nodes. Our results reveal a signaling pathway where SDF-1α induces T-cell adhesion through activation of PLCε1, suggesting that PLCε1 is a specific potential target in treating conditions involving migration of T cells to inflamed organs.

VCAM-1 is a CS1 peptide-inhibitable adhesion molecule expressed by lymph node high endothelium

1993 ◽  
Vol 106 (1) ◽  
pp. 109-119 ◽  
Author(s):  
M.J. May ◽  
G. Entwistle ◽  
M.J. Humphries ◽  
A. Ager
Keyword(s):  
Lymph Node ◽  
Cell Interaction ◽  
Tnf Alpha ◽  
Dependent Manner ◽  
Ifn Gamma ◽  
Lymphocyte Adhesion ◽  
Peripheral Lymph ◽  
Endothelial Surface ◽  
Dose Dependent

Previous studies have shown that unactivated lymphocytes bind to CS1 peptide and that the adhesion of these cells to high endothelium is inhibited by CS1 peptide. These results suggest that lymphocyte binding occurs via recognition of the CS1-containing splice variant of fibronectin expressed on the high endothelial surface. We have now extended these studies by determining the role of the CS1 receptor, alpha 4 beta 1 (VLA-4) and the alternative VLA-4 ligand, VCAM-1 in a rat model of lymphocyte-high endothelial cell interaction. Anti-VLA-4 antibody, HP2/1, blocked lymphocyte adhesion to resting and IFN-gamma (interferon-gamma) pretreated cultured high endothelial cells (HEC) in a dose-dependent manner with maximal inhibition of 60%. HP2/1 completely blocked the adhesion of rat lymphocytes to immobilized CS1 peptide and to a recombinant soluble (rs) form of human VCAM-1. Lymphocyte binding to rsVCAM-1 was also completely blocked by CS1 peptide. Anti-rat VCAM-1 monoclonal antibody 5F10 inhibited adhesion to untreated and IFN-gamma-treated HEC equally and its effect at 50% inhibition was slightly less than that of HP2/1. These findings suggest that a CS1 peptide-inhibitable ligand expressed by high endothelium is VCAM-1. The majority of cultured HEC expressed significant levels of VCAM-1 under basal conditions, as did HEV in peripheral lymph nodes. VCAM-1 expression by HEC was upregulated by cytokine pretreatment and the effects were ordered: IFN-gamma > TNF-alpha > IL-1 beta. The results described here demonstrate that rat peripheral lymph node HEC express VCAM-1, its expression is upregulated by cytokines, in particular IFN-gamma, and it supports the adhesion of unactivated lymphocytes. They also suggest that the VLA-4/VCAM-1 adhesion pathway may operate during the constitutive migration of lymphocytes into lymphoid organs. Although the mechanism of CS1 peptide inhibition was not determined, these results show that VCAM-1 is a CS1 peptide-inhibitable ligand and therefore CS1, on its own, cannot be used as a specific indicator of fibronectin activity.

Physical linkage of genes encoding the lymphocyte adhesion molecules CD2 and its ligand LFA-3

1989 ◽  
Vol 30 (2) ◽  
pp. 123-125 ◽  
Author(s):  
Stephen F. Kingsmore ◽  
Mark L. Watson ◽  
Walton S. Moseley ◽  
Michael F. Seldin
Keyword(s):  
Adhesion Molecules ◽  
Lymphocyte Adhesion ◽  
Physical Linkage ◽  
Genes Encoding ◽  
Linkage Of Genes

scholarly journals Human Siglec-10 can bind to vascular adhesion protein-1 and serves as its substrate

Blood ◽  
2009 ◽  
Vol 114 (26) ◽  
pp. 5385-5392 ◽  
Author(s):  
Elina Kivi ◽  
Kati Elima ◽  
Kristiina Aalto ◽  
Yvonne Nymalm ◽  
Kaisa Auvinen ◽  
...  
Keyword(s):  
Primary Amines ◽  
Leukocyte Trafficking ◽  
Hydrogen Peroxide Production ◽  
Lymphocyte Adhesion ◽  
Adhesion Protein ◽  
Inflammatory Microenvironment ◽  
Inflamed Endothelium ◽  
End Products ◽  
Vascular Adhesion ◽  
Vascular Adhesion Protein 1

Abstract Leukocytes migrate from the blood into areas of inflammation by interacting with various adhesion molecules on endothelial cells. Vascular adhesion protein-1 (VAP-1) is a glycoprotein expressed on inflamed endothelium where it plays a dual role: it is both an enzyme that oxidizes primary amines and an adhesin that is involved in leukocyte trafficking to sites of inflammation. Although VAP-1 was identified more than 15 years ago, the counterreceptor(s) for VAP-1 on leukocytes has remained unknown. Here we have identified Siglec-10 as a leukocyte ligand for VAP-1 using phage display screenings. The binding between Siglec-10 and VAP-1 was verified by different adhesion assays, and this interaction was also consistent with molecular modeling. Moreover, the interaction between Siglec-10 and VAP-1 led to increased hydrogen peroxide production, indicating that Siglec-10 serves as a substrate for VAP-1. Thus, the Siglec-10–VAP-1 interaction seems to mediate lymphocyte adhesion to endothelium and has the potential to modify the inflammatory microenvironment via the enzymatic end products.

scholarly journals Hyaluronan and versican in the control of human T-lymphocyte adhesion and migration

2012 ◽  
Vol 31 (2) ◽  
pp. 90-100 ◽  
Author(s):  
Stephen P. Evanko ◽  
Susan Potter-Perigo ◽  
Paul L. Bollyky ◽  
Gerald T. Nepom ◽  
Thomas N. Wight
Keyword(s):  
T Lymphocyte ◽  
Lymphocyte Adhesion ◽  
Human T Lymphocyte ◽  
And Migration
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