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Pathways of Cell Recruitment to Mucosal Surfaces
Published in Bruce S. Bochner, Adhesion Molecules in Allergic Disease, 2020
Interactions between immunoglobulin-related vascular adhesion receptors and integrins play a key role in firm adhesive interactions and possibly transendothelial migration of leukocytes as well. ICAM-1, ICAM-2, and ICAM-3 are all similar yet distinct receptors that can interact with LFA-1 (9,15,26,27,30–32,74). ICAM-1 can also bind to MAC-1 by virtue of an interaction that is distinct from its binding to LFA-1 (75). ICAM-1 expression is induced in vascular endothelium and endothelial cell lines (76–78) in response to pro-inflammatory cytokines, and increased expression plays a significant role in homing to inflammatory sites, albeit not in a tissue-specific manner. ICAM-2 is constitutively expressed and may play a role in trafficking of leukocytes in uninflamed tissues, as is the case for recirculating lymphocytes. All of the ICAMS contribute to antigen-specific interactions inhibition experiments show that mAbs to all three receptors are required to completely block LFA-1-dependent antigen-specific T-cell responses (9,37,74). LFA-1 binding to one of the ICAM receptors contributes to lymphocyte localization in mucosal tissues as shown by in vivo homing experiments and in situ videomicroscopy (see below) (39,41,42,79,80).
Interaction of Immune and Connective Tissue Cells
Published in Brian J. Nickoloff, Dermal Immune System, 2019
Joseph H. Korn, Theresa Piela-Smith
ICAM-2 was originally described as a cDNA clone that encoded an additional counter-receptor for LFA-1.20 Whereas the extracellular domain of ICAM-1 is composed of five Ig-like domains, the extracellular domain of ICAM-2 possesses only two such domains;20 ICAM-2 is also a member of the Ig supergene family. Tissue expression of ICAM-2 is much more restricted than that of ICAM-1, being most pronounced on endothelial cells, where it is found at levels 10- to 15-fold greater than that of ICAM-1.21 In contrast to the regulation of ICAM-1 by cytokines, the relatively high levels of ICAM-2 are unaffected by cytokine treatment of endothelial cells. It is hypothesized that ICAM-1 is the major ligand on endothelial cells for LFA-1 during inflammatory or immune responses, while ICAM-2 is of more relative importance in the unstimulated resting state or early on during a response before ICAM-1 expression is increased.21
Endothelial Cells
Published in John H. Barker, Gary L. Anderson, Michael D. Menger, Clinically Applied Microcirculation Research, 2019
ECs possess at least three adhesive receptors in the immunoglobulin family, namely ICAM-1, ICAM-2, and VCAM (INCAM-110), which serve as counter receptors for the leukocyte integrins.60–62 They are single-chain N-glycosylated polypeptides. ICAM-1 contains five immunoglobulin domains. It is not only present on ECs, but is present on a variety of other cells including leukocytes. ECs constitutively express ICAM-1 in low amounts, but increased levels are easily induced by a variety of cytokines including interferon-γ, IL-1, and TNF-α.63 Following stimulation, increased expression can be detected within 4 h and expression is maintained for over 24 h. ICAM-2 is similar to ICAM-1 but contains only two immunoglobulin domains. ICAM-2 is constitutively expressed by ECs and is not increased after cytokine activation.64 This may indicate more of a role for ICAM-2 in routine EC-leukocyte interactions, whereas ICAM-1 becomes more important in activated ECs. VCAM-1 is also expressed following endothelial activation by cytokines.65 VCAM-1 selectively binds mononuclear cells such as lymphocytes and monocytes and is the counter-receptor for the β2 integrin VLA4.66 VCAM-1 has been found at sites of chronic inflammation but its expression is not restricted to ECs. Macrophages and fibroblast-like cells also appear to express VCAM-1.67
Increased Expressions of ICAM-2 and ICAM-3 in Pterygium
Published in Current Eye Research, 2019
Seniz Demiryürek, Ahmet Saracaloglu, Sabit Kimyon, Alper Mete, Omer Eronat, Ebru Temiz, Gülper Nacarkahya, Zeynep Sav Tunca, Betül Düzen, Oguzhan Saygili, Kıvanc Güngör, Metin Karakök, Abdullah T. Demiryürek
Intercellular adhesion molecule (ICAM)-2 (CD102) and ICAM-3 (CD50) are members of the immunoglobulin superfamily of adhesion molecules. ICAM-2 is expressed on the surface of the endothelial cells, neutrophils, platelets, and various other leukocyte subsets.5 ICAM-2 contributes to neutrophil-mediated vascular permeability and plasma leakage.5 ICAM-3 is highly expressed on peripheral blood monocytes, neutrophils, eosinophils, and lymphocytes.6–8 Although high rates of ICAM-1-positive cells in flow cytometrical analysis, and scattered ICAM-1 expression in immunohistochemical staining have been demonstrated in pterygium,9,10 ICAM-2 and ICAM-3 expressions have not been investigated in relation to pterygium formation. Therefore, the aim of this study was to assess the levels of ICAM-2 and ICAM-3 expressions in pterygium.
Focusing on the role of platelets in immune defence against invading pathogens
Published in Platelets, 2015
Steve W. Kerrigan, Alastair Poole
In order to orchestrate the immune response efficiently, platelets express a number of receptors critical for recruiting the professional immune cells. These include Intracellular Cell Adhesion Molecular (ICAM) 2 which binds to leukocyte β2 integrin; LFA-1 (α1β2, CD11a/CD18) and to dendritic cell specific ICAM grabbing nonintegrin (DC-SIGN). Trans-interactions of platelet-derived junctional adhesion molecules (JAM-A and JAM-C) have been found to support the luminal deposition of platelet chemokines and to enhance the recruitment of leukocytes. Upon activation, CD40L is upregulated on the platelet surface which results in stimulation of endothelial cells through its cognate receptor CD40 and in increased expression of adhesion molecules, release of chemokines (e.g. RANTES) enhancing recruitment of leukocytes [3]. Given the functional make-up of platelets there is little doubt that they are perfectly suited to direct and respond to immune processes.