Robert Feulgen Lecture 1993. L-selectin and its biological ligands.
This review considers the leukocyte adhesive receptor known as L-selectin. This protein, belonging to the selectin family of cell-cell adhesion receptors, mediates adhesion by virtue of a C-type lectin domain at its amino terminus. The protein was discovered as a lymphocyte homing receptor involved in the attachment of lymphocytes to high endothelial venules (HEV) of lymph nodes. Its widespread distribution on all leukocyte populations underlies a more general role in a variety of leukocyte-endothelial interactions. In the HEV interaction, cognate HEV ligands for L-selectin have been identified as two sulfated, sialylated, and fucosylated glycoproteins, known as GlyCAM-1 and Sgp90. These ligands have mucin-like domains which confer important properties for their proposed adhesive function. The carbohydrate features of these ligands, essential for their interaction with L-selectin, are reviewed. The existence of extralymphoid ligands for L-selectin is also discussed.
Rosen
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Department of Anatomy, University of California, San Francisco 94143-0452.
D015703:Antigens, CD / Q000502:physiology*; D018952:Antigens, CD34; D002236:Carbohydrate Conformation; D015815:Cell Adhesion Molecules / Q000502:physiology*; D005544:Forecasting; D006801:Humans; D019041:L-Selectin; D008024:Ligands; D009077:Mucins / Q000737:chemistry* / Q000502:physiology; D016201:Receptors, Lymphocyte Homing / Q000032:analysis / Q000502:physiology*
D015703:Antigens, CD; D018952:Antigens, CD34; D015815:Cell Adhesion Molecules; D008024:Ligands; D009077:Mucins; D016201:Receptors, Lymphocyte Homing; D019041:L-Selectin; C075185:sulfated glycoprotein p50