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Varani, J. Vink, J. Rao, C. Iwamoto, Y. Murthy, M. Metastasis 10 , 39— Invasion Metastasis 13 , — Saiki, I. Tressler, R. Cancer Commun. Stoolman, L. The process of leukocyte accumulation at sites of inflammation is a dynamic one and involves multiple steps. The orchestration of these steps must be precisely regulated to ensure a rapid response, with only minimal damage to healthy tissue.
Leukocyte interaction with vascular endothelial cells is essential in guiding the inflammatory response and is mediated by several families of adhesion molecules. These include the integrins, the selectins, and members of the Ig superfamily. Each is involved in a different phase of leukocyte emigration through the endothelium, and the synchronization of their expression and function is crucial for the normal recruitment of leukocytes from the blood stream to the tissue.
Integrins Table 1 are transmembrane cell surface proteins that bind to cytoskeletal proteins and communicate extracellular signals. Within the integrin family of adhesion receptors, only five members have so far been shown to be involved in leukocyte adhesion to endothelium.
Both subunits are required for expression, and if CD18 is absent, CD11 is not detected on the cell surface, although the synthesis of the CD11 molecule is normal 6. LFA-1 is expressed by lymphocytes, monocytes, and neutrophils. Mac-1 and p,95 expression is restricted primarily to myeloid cells, although they are also expressed by some lymphocytes and natural killer cells. They participate in many leukocyte adhesion-related functions in addition to migration through the endothelial cells, such as phagocytosis, killing of bacteria, and antibody-dependent, cell-mediated cytotoxicity 7.
Neutrophil and monocyte adhesion to endothelium relies mainly on LFA-1 and Mac-1 with only a minor role for p, Lymphocyte adhesion involves the interaction of LFA-1 with its endothelial ligands 8. An important characteristic of the leukocyte integrins is that under baseline conditions they exist in a relatively inactive conformation, rendering the leukocyte nonadhesive.
One of the key events at the adhesion cascade is the activation and deactivation of these integrins at the proper times and places. Activation of leukocytes by a variety of mediators e. This increased adhesive ability occurs through qualitative changes, transformation of LFA-1 and Mac-1 from low to high avidity state, and, in phagocytes, up-regulation of the surface expression of Mac-1 and p, 1 , 2.
Leukocytes mediate adhesion through binding to their ligands, members of the Ig superfamily integrins, which are expressed on all cells and may affect leukocyte adherence and interactions with all cells in the body, particularly during inflammatory conditions. They comprise a series of cellular receptors for extracellular matrix proteins including fibronectin, collagen, and laminin. Because blood neutrophils do not express VLA-4, they cannot use this pathway to adhere to stimulated endothelium.
This family includes three molecules, ICAM-1, -2, and The gene for ICAM-1 is located on chromosome 19, and the molecule has five Ig-like domains, with a short hinge region separating the third and fourth Ig-like domain It is a ligand for both LFA-1 and Mac The binding sites for the integrins are distinct; LFA-1 binds to domains 1 and 2, whereas Mac-1 binds to domain 3. Human ICAM-2 is a single-copy gene located on chromosome It has only two extracellular Ig-like domains, and the binding site for LFA-1 is located in these domains Other integrin molecules do not bind ICAM Recently a third ICAM molecule was described.
The distribution and regulation of the ICAMs are quite distinct. ICAM-1 is expressed only at low levels on some vascular endothelial cells and on lymphocytes under normal conditions and is dramatically up-regulated by endotoxin, IL-1, and TNF. This increased expression which starts h after contact with the cytokines lasts for several days.
ICAM-2 expression, in contrast, is constitutive and is not regulated by the various cytokines ICAM-3 is constitutively and strongly expressed on resting lymphocytes but not on endothelial cells. Once the cell is activated, ICAM-3 will accumulate in the uropod of the cell, thus facilitating interaction and aggregation with more leukocytes 14 , and recruiting cells to the inflammatory area.
Recently, a soluble form of ICAM-1 has been reported. It retains its ability to bind to LFA-1 and was found to be elevated in the serum of patients with various pathologic conditions which are characterized by a prominent inflammatory response. ICAM-2 and -3 have not yet been shown to exist as soluble forms VCAM-1 also belongs to the Ig superfamily.
It contains seven Ig-like domains, the ligand binding site for the integrin VLA-4, and is located within the NH 2 -terminal first domain. A single VCAM-1 gene gives rise through alternative splicing to distinct isoforms that differ in the number of integrin binding sites A soluble form has also been described and has been found to correlate with disease activity in several inflammatory disorders Soluble forms of members of the Ig superfamily may play a role in activation of cells at local sites of inflammation or at distant sites via distribution through the circulation.
The genes for the selectins family are closely linked on chromosome 1, reflecting their common evolutionary origin. All three members have common structural features, most prominently an NH 2 -terminal lectin-like domain, which is central to the carbohydrate-binding properties of all three selectins. The lectin domain is followed by a domain homologous to the epidermal growth factor and a discrete number of molecules similar to those found in certain complement-binding proteins The term selectin was proposed to highlight the amino-terminal lectin domain and to indicate the selective function and expression of these molecules.
All three selectins are involved in the recruitment of leukocytes to sites of tissue injury, but there are fundamental differences in their distribution, activation, and mode of expression. E-selectin is restricted to endothelial cells, and its expression is induced when the cells are activated by IL-1 or TNF.
These substances activate the transcription of E-selectin, resulting in peak cell surface expression at h, decreasing to basal levels by 24 h Although E-selectin expression in vitro is typically transient, it is chronically expressed in certain inflammatory conditions and is also detected in the serum. The role of soluble E-selectin is still unclear, and its serum level does not correlate with disease activity.
P-selectin is expressed on platelets as well as on endothelial cells. Thus, within minutes of activation of either cell type by thrombin or histamine, P-selectin is rapidly redistributed to the surface of the cells. Its expression in vitro is typically very short-lived, up to 15 min. However, studies in vivo suggest that endothelial P-selectin may also be regulated at the level of protein synthesis, providing a mechanism for more prolonged expression In contrast to the E- and P-selectins, L-selectin is constitutively expressed on leukocytes but not on endothelial cells. Although originally described as a lymphocyte homing receptor, it was subsequently shown to be expressed on most other leukocytes.
After a transient increase of this selectin during activation, it is shed rapidly due to a proteolytic cleavage near the membrane insertion Soluble circulating L-selectin can be measured in the plasma of normal individuals as well as in several pathologic conditions This soluble form can partially inhibit leukocyte adhesion to cytokine stimulated endothelium, but its in vivo role is still unknown.
All three selectins have a major role in leukocyte adherence to endothelial cells, which is mediated through binding to ligands on the leukocyte E and P or endothelial cell L The lectin and the epidermal growth factor domains in the selectins play a crucial role in mediating this binding. One major selectin ligand is a member of a class of sialylated and fucosylated tetrasaccharides related to the sialylated Lewis X blood group SLeX, CD15 SLeX is heavily expressed on neutrophils and monocytes.
Peripheral lymphocyte express SLeX only after activation. Both the sialic acid and the fucose linkages were shown to be critical for efficient binding. MAb against SLeX block the binding of neutrophils to activated endothelial cells Furthermore, cell lines which do not express this ligand show no binding, but after induction of SLeX by transfection of appropriate fucosyltransferases, binding is observed. The migration of leukocytes from the blood stream to the tissue occurs in several steps Fig. First, loose adhesion to the vessel wall, primary in postcapillary venules, under conditions of flow causes the leukocytes to roll on the endothelium.
This transient and reversible step is a prerequisite for the next stage, the activation of leukocytes. This is followed by firm adhesion after which migration occurs. Each of these steps involves different adhesion molecules, and can be differentially regulated Fig. The various steps of the adhesion cascade. After endothelial activation by cytokines derived from the inflammatory tissue, selectins are expressed on the endothelium. The interaction between the selectins and their leukocyte ligands will start the rolling process. This will lead to leukocyte activation with increased expression of the integrins which will cause the sticking of the cells to the endothelium.
In the last phase, transmigration is mediated mainly by binding of platelet-endothelial cell adhesion molecule-1 PECAM-1 to integrins. Step 1: Rolling, selectin-dependent. Leukocytes in the circulation must resist tremendous shear forces to stop along the vascular endothelium. Under normal conditions, leukocytes move rapidly and do not adhere to the endothelium. The phenomenon of leukocyte rolling has been known for more than a century, but its molecular basis was delineated only recently. Several studies 25 , 26 showed that, although CD18 MAb block sticking, they do not effect rolling.
MAb to selectins, however, markedly reduced the rolling process in vivo and in vitro Moreover, rolling is dramatically diminished in P-selectin-deficient mice The selectins expressed on the endothelial cells, will bind to the leukocytes through their ligands, mainly SLeX. The presentation of SLeX to E- and P-selectins may be partially mediated by L-selectin which is expressed on the leukocytes.
The rolling phase is transient in part because L-selectin is shed quickly from the leukocytes, and P-selectin on endothelial cells is internalized. Furthermore, at the site of inflammation, free SLeX appears and may compete for binding to the selectins Step 2: Activation, integrin-dependent. The transition from selectin-mediated adhesion to integrin-mediated adhesion occurs rapidly and involves the activation of the integrin receptors.
During rolling, the slowly moving cells are exposed to diverse mediators, which are generated at the site of inflammation and are capable of activating integrins. These mediators may be secreted as soluble molecules and then bind to adjacent endothelium. Recent advances in biological experimental techniques and future studies may identify this lesion-specific cell adhesion as a major cause of various inflammatory diseases.
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. The authors thank Ms. Heather A. Berezin, V. Brain Res. Biederer, T. Bioinformatic characterization of the SynCAM family of immunoglobulin-like domain-containing adhesion molecules. Genomics 87, — Coombe, D. CrossRef Full Text. Demetriou, M. Integrin clipping: a novel adhesion switch?
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