Interaction of recombinant and natural soluble CD5 forms with an alternative cell surface ligand

CD5, a member of the scavenger receptor cysteine‐rich (SRCR) receptor family, plays a role in the thymocyte maturation, T cell activation and T cell‐antigen‐presenting cell interactions. To date only CD5 ligands (CD5L) compatible with a T‐B co‐stimulatory role have been described (CD72, gp40‐80 and...

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Veröffentlicht in:European journal of immunology 1999-07, Vol.29 (7), p.2119-2129
Hauptverfasser: Calvo, Javier, Places, Lourdes, Padilla, Olga, Vilà, Josep M., Vives, Jordi, Bowen, Michael A., Lozano, Francisco
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container_end_page 2129
container_issue 7
container_start_page 2119
container_title European journal of immunology
container_volume 29
creator Calvo, Javier
Places, Lourdes
Padilla, Olga
Vilà, Josep M.
Vives, Jordi
Bowen, Michael A.
Lozano, Francisco
description CD5, a member of the scavenger receptor cysteine‐rich (SRCR) receptor family, plays a role in the thymocyte maturation, T cell activation and T cell‐antigen‐presenting cell interactions. To date only CD5 ligands (CD5L) compatible with a T‐B co‐stimulatory role have been described (CD72, gp40‐80 and IgVH framework region) so the existence of alternative CD5L involved in other aspects of T cell biology warrants further exploration. Here we characterize the cell binding properties of a recombinant soluble human CD5 extracellular domain glycoprotein (rsCD5). In contrast to previously characterized ligands, this molecule binds to a broadly distributed cell surface receptor expressed on monocytes, lymphocytes and various cell lines of lymphoid, myelomonocytic and epithelial origin. The cell binding of rsCD5 is divalent cation independent and inhibited by high molar concentrations of certain monosaccharides. Both human CD5 Ig fusion proteins and a natural soluble CD5 form (present in human serum and resulting from proteolytic cleavage following lymphocyte activation) reproduce the cell binding pattern of rsCD5 and block its binding in a competitive form. The involvement of the most N‐terminal CD5 SRCR domains (D1 and D2) in binding is deduced from competition cell binding assays with CD5 Ig fusion proteins. These results imply a novel CD5/CD5L interaction model recalling some aspects of the interaction of CD6 with activated leukocyte cell adhesion molecule (ALCAM).
doi_str_mv 10.1002/(SICI)1521-4141(199907)29:07<2119::AID-IMMU2119>3.0.CO;2-F
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The involvement of the most N‐terminal CD5 SRCR domains (D1 and D2) in binding is deduced from competition cell binding assays with CD5 Ig fusion proteins. These results imply a novel CD5/CD5L interaction model recalling some aspects of the interaction of CD6 with activated leukocyte cell adhesion molecule (ALCAM).</abstract><cop>Weinheim</cop><pub>WILEY‐VCH Verlag GmbH</pub><pmid>10427974</pmid><doi>10.1002/(SICI)1521-4141(199907)29:07&lt;2119::AID-IMMU2119&gt;3.0.CO;2-F</doi><tpages>11</tpages></addata></record>
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subjects Animals
Antibodies, Monoclonal
Binding Sites
Binding, Competitive
CD5 antigen
CD5 Antigens - metabolism
CD5 ligand
CD5L protein
Cell Line
Cell Membrane - immunology
Humans
In Vitro Techniques
Ligands
Membrane Proteins
Mice
Precipitin Tests
Receptors, Immunologic - metabolism
Receptors, Lipoprotein
Receptors, Scavenger
Recombinant Fusion Proteins - metabolism
Recombinant Proteins - metabolism
scavenger receptors
Scavenger Receptors, Class B
Solubility
Soluble CD5
SRCR domain
T-Lymphocytes - immunology
T-Lymphocytes - metabolism
title Interaction of recombinant and natural soluble CD5 forms with an alternative cell surface ligand
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