L-Selectin: A Lectin-Like Leukocyte Adhesion Protein.:A Lectin-Like Leukocyte Adhesion Protein

概要

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L-Selectin is a calcium-dependent lectin-like receptor that is widely distributed on leukocytes. It belongs to the newly emerging selectin family of cell adhesion proteins, which includes E-selectin (ELAM-1) and P-selectin (PADGEM, GMP-140, CD62). L-Selectin was discovered as a lymphocyte homing receptor, involved in the organ-specific adherence of blood-borne lymphocytes to high endothelial venules (HEV) in lymph nodes. L-Selectin is now known to participate in the early stages of the interaction of neutrophils with venular endothelium at sites of acute inflammation. The endothelial and leukocyte ligands for the selectins are all fucosylated and all require sialic acid for functionality. The HEV-associated ligands for L-selectin are sulfated, fucosylated, and sialylated, O-linked glycoproteins. A major objective for future work is a detailed comparison of the carbohydrate structures of the selectin ligands. L-Selectin, in addition to its functions within the blood vascular compartment, can also mediate the attachment of lymphocytes, and possibly other leukocytes, to central nervous system myelinated tracts. This latter interaction may have pathophysiological significance in the etiology of demyelinating diseases. As the selectins participate in a number of leukocyte adhesive interactions pertinent to inflammation, these molecules are being investigated with increasing intensity.
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