A Homing Receptor-IgG Chimera as a Probe for Adhesive Ligands of Lymph Node High Endothelial Venules

The binding of lymphocytes to high endothelial venules (HEV) within peripheral lymph nodes (pln) is thought to be mediated by a lectinlike adhesion molecule termed the pln homing receptor (pln HR). The cloning and sequencing of cDNAs encoding both murine and human pln HR revealed that these adhesion...

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Bibliographic Details
Published in:The Journal of cell biology 1990-06, Vol.110 (6), p.2221-2229
Main Authors: Watson, Susan R., Imai, Yasuyuki, Fennie, Christopher, Geoffroy, Joyce S., Rosen, Steven D., Lasky, Laurence A.
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Chimera - immunology
Chimera - physiology
Chimeras
Endothelial cells
Endothelium - cytology
Endothelium, Lymphatic - cytology
Endothelium, Lymphatic - immunology
Endothelium, Lymphatic - metabolism
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Hepatitis E virus
Homing
Immunobiology
Immunoglobulin G - immunology
Immunoglobulin G - metabolism
Immunohistochemistry
Lectins
Lectins - metabolism
Lectins - physiology
Ligands
Lymph nodes
Lymph Nodes - anatomy & histology
Lymph Nodes - cytology
Lymphocytes
Lymphoid organs: ontogeny, organization, homing phenomenon
Mannans - metabolism
Mice
Molecules
Plant Lectins
Receptors
Receptors, Immunologic - immunology
Receptors, Immunologic - metabolism
Receptors, Lymphocyte Homing
Veins - metabolism
Venules - cytology
Venules - immunology
Venules - metabolism
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Summary:The binding of lymphocytes to high endothelial venules (HEV) within peripheral lymph nodes (pln) is thought to be mediated by a lectinlike adhesion molecule termed the pln homing receptor (pln HR). The cloning and sequencing of cDNAs encoding both murine and human pln HR revealed that these adhesion molecules contain protein motifs that are homologous to C-type or calcium dependent lectin domains as well as to epidermal growth factor (egf) and complement-regulatory protein domains. We have produced a novel, antibody-like form of the murine HR by joining the extracellular region of the receptor to a human IgG heavy chain. This antibody-like molecule is capable of recognizing carbohydrates, blocking the binding of lymphocytes to pln HEV, and serving as a histochemical reagent for the staining of pln HEV. This murine HR-IgG chimera should prove useful in analyzing the distribution of the HR ligand(s) in normal as well as in inflammatory states.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.110.6.2221