The Journal of Experimental Medicine · 1991 · 553 citations · 23 references
Life SciencesCell BiologyImmunologyCell AdhesionImmunopathologyInflammationAdhesion MoleculesAntibody-antigen RecognitionAntigen RecognitionCell Adhesion ReceptorsLeukocyte AdhesionLeukocyte RecruitmentCellular Adhesion MoleculesLeukocyte Adhesion MoleculesLeukocyte-endothelium InteractionsLymphocyte Homing ReceptorsLymphocyte PhysiologySialic Acid RecognitionSkin-homing Lymphocytes
A skin-associated population of memory T lymphocytes, defined by expression of the cutaneous lymphocyte antigen (CLA), binds selectively and avidly to the vascular lectin endothelial cell-leukocyte adhesion molecule 1 (ELAM-1), an interaction that may be involved in targeting of CLA+ T cells to cutaneous sites of chronic inflammation. Here we present evidence that CLA itself is the (or a) lymphocyte homing receptor for ELAM-1. Antigen isolated with anti-CLA monoclonal antibody HECA-452 from human tonsillar lysates avidly binds ELAM-1 transfected mouse cells. Anti-CLA antibody blocks T lymphocyte binding to ELAM-1 transfectants. HECA-452 and ELAM-1 binding to lymphocytes or to isolated tonsillar HECA-452 antigen is abrogated by neuraminidase treatment implying a prominent role for sialic acid in CLA structure and function. The dominant form of CLA on T cells is immunologically distinct from the major neutrophil ELAM-1 ligand, the sialyl Lewis x (sLex) antigen (NeuAc alpha 2-3Gal beta 1-4[Fuc alpha 1-3]GlcNAc), which is absent, weakly expressed, or masked on T cells. However, neuraminidase treatment of CLA+ T cells, but not of CLA- T cells, reveals Lewis x (CD15) structures. In combination with the known requirement for terminal NeuAc alpha 2-3Gal and fucose residues attached to N-acetylglucosamine for ELAM-1 and HECA-452 binding, this finding suggests that CLA may comprise an additionally sialylated or otherwise modified form of sLex. The identification of a lymphocyte homing receptor for skin may permit novel approaches to the diagnosis and therapy of cutaneous and inflammatory disorders.
23
ELAM-1 Mediates Cell Adhesion by Recognition of a Carbohydrate Ligand, Sialyl-Le <sup>x</sup>
M. Laurie Phillips, Edward Nudelman, F C Gaeta et al. · Science · 1990 · 1.3K citations
Neutrophil Mac-1 and MEL-14 Adhesion Proteins Inversely Regulated by Chemotactic Factors
Takashi Kishimoto, Mark A. Jutila, Ellen L. Berg et al. · Science · 1989 · 1.1K citations
Life Sciences, Immunology, Pathology +17
Recognition by Elam-1 of the Sialyl-Le <sup>x</sup> Determinant on Myeloid and Tumor Cells
Gerd Walz, Alejandro Aruffo, Waldemar Kolanus et al. · Science · 1990 · 967 citations
ELAM-1 is an adhesion molecule for skin-homing T cells
Louis J. Picker, Takashi Kishimoto, C. Wayne Smith et al. · Nature · 1991 · 831 citations