Structural characterization of CD6: Properties of two distinct epitopes involved in T cell activation

Swack, Judith A.; Gangemi, Rosaria; Rudd, Christopher E.; Morimoto, Chikao; Schlossman, Stuart F.; Romain, Paul L.

doi:10.1016/0161-5890(89)90068-0

Molecular Immunology

1989

DOI: 10.1016/0161-5890(89)90068-0

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Structural characterization of CD6: Properties of two distinct epitopes involved in T cell activation

Judith A. Swack

Rosaria Gangemi

Christopher E. Rudd

et al.

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Cited by 32 publications

(30 citation statements)

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“…During thymocyte development, CD6-dependent signals contribute to thymocyte survival and positive selection (9). Several reports show that ligation of CD6 with mAbs is capable of delivering costimulatory signals to mature peripheral T lymphocytes (13)(14)(15)(16)(17)(18). However, the inhibition of Ag-specific responses of human T cell clones specific to tetanus toxoid by CD6 mAbs also has been reported (19).…”

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confidence: 96%

“…CD6 has a long cytoplasmic tail devoid of intrinsic catalytic activity, but it harbors several consensus motives related to signal transduction (25). CD6 is a constitutively phosphorylated molecule that becomes hyperphosphorylated by serum and protein kinase C (PKC) activators, causing a molecular mass shift from 105 to 130 kDa (15,26). Upon CD3 stimulation, either alone or by co-cross-linking with CD2 or CD4, CD6 becomes transiently phosphorylated on the two most C-terminal tyrosine residues (Y629 and Y662) (27,28).…”

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confidence: 99%

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Mitogen-Activated Protein Kinase Pathway Activation by the CD6 Lymphocyte Surface Receptor

Ibáñez

Sarrias

Farnós

et al. 2006

The Journal of Immunology

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CD6 is a cell surface receptor primarily expressed on immature thymocytes and mature T and B1a lymphocytes. Through its binding to activated leukocyte cell adhesion molecule (ALCAM/CD166), CD6 is considered to play an important role in lymphocyte development and activation. Accordingly, CD6 associates with the TCR/CD3 complex and colocalizes with it at the center of the mature immunological synapse on T lymphocytes. Moreover, the CD6-ALCAM interaction has been shown to be critical for proper immunological synapse maturation and T cell proliferative responses. However, the precise biological effects of CD6 ligation and its signaling pathway are still not well understood. The present study shows that CD6 ligation with three different specific mAbs (161.8, SPV-L14.2, and MAE1-C10) induces time- and dose-dependent activation of ERK1/2 on normal and leukemic human T cells. This effect was also observed upon CD6 ligation with a chimerical ALCAM protein (ALCAM-Fc). The C-terminal cytoplasmic region of CD6, as well as Src tyrosine kinases, was critical for CD6-induced ERK1/2 activation. Synergistic effects were observed upon coligation of the TCR/CD3 complex with CD6. The ligation of CD6 induced the transcriptional activation of reporter genes under the control of the c-Fos serum responsive element and AP-1. Accordingly, CD6-mediated activation of p38 and JNK was also observed. These findings indicate that the CD6-ALCAM interaction results in activation of the three MAPK cascades, likely influencing the dynamic balance that determines whether resting or activated lymphocytes survive or undergo apoptosis.

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confidence: 96%

mentioning

confidence: 99%

Mitogen-Activated Protein Kinase Pathway Activation by the CD6 Lymphocyte Surface Receptor

Ibáñez

Sarrias

Farnós

et al. 2006

The Journal of Immunology

View full text Add to dashboard Cite

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“…Available evidence indicates that it is an accessory molecule capable of providing co-stimulatory signals in mature T cells (27)(28)(29)(30)(31)(32). The signaling pathway used by CD6 to influence T cell activation is, however, mostly unknown.…”

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confidence: 99%

The Accessory Molecules CD5 and CD6 Associate on the Membrane of Lymphoid T Cells

Gimferrer¹,

Farnós²,

Calvo

et al. 2003

Journal of Biological Chemistry

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“…Its three extracellular cysteine-rich domains are coded by distinct exons (2), and the membraneproximal portion of CD6 binds the CD6 ligand (CD6L) 3 CD166. Anti-CD6 mAbs that bind epitopes of the CD6 extracellular portion, including and distinct from the CD166-binding site, influenced T cell signaling (3)(4)(5)(6), suggesting that individual CD6Ls contributed individually or in combination, to CD6-dependent costimulation. In addition, there exist multiple alternatively spliced forms of the CD6 cytoplasmic portion and contain different numbers of potential signaling motifs (7).…”

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confidence: 99%

Expression and Characterization of a Novel CD6 Ligand in Cells Derived from Joint and Epithelial Tissues

Saifullah

Fox

Sarkar

et al. 2004

The Journal of Immunology

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CD6 is a T cell surface glycoprotein that plays an important role in interactions of thymocytes with thymic epithelial cells and in mature T cell interactions with selected nonprofessional tissue APCs. We describe a novel CD6 ligand (CD6L) 3A11 Ag that is distinct from the known CD6L (CD166). The 3A11 protein is expressed on cells derived from human thymus, skin, synovium, and cartilage, and its expression is enhanced by IFN-γ. mAbs directed against the 3A11 Ag and CD166 exhibit distinct patterns of binding to a panel of cell lines. Confocal microscopy shows that both CD166 and the 3A11 Ag are expressed at the cell surface, and that these proteins colocalize. The 3A11 Ag has a molecular mass of 130 kDa and is immunoprecipitated using either mAb 3A11 or soluble CD6-Ig fusion protein. mAbs directed against individual CD6L were less potent than was soluble CD6-Ig fusion protein in reducing adhesion of T cells to adherent 3A11-positive epithelial cells in vitro, suggesting that these Abs recognize epitopes on the 3A11 Ag and CD166 that are distinct from CD6 binding sites. Finally, transfection of epithelial cells with CD166-specific small interfering RNAs significantly decreased CD166 expression without alteration in 3A11 Ag levels, and thus confirmed that these two CD6L are distinct. Taken together, our data identifies a novel 130-kDa CD6L that may mediate interactions of synovial and epithelial cells with T lymphocytes.

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Structural characterization of CD6: Properties of two distinct epitopes involved in T cell activation

Cited by 32 publications

References 38 publications

Mitogen-Activated Protein Kinase Pathway Activation by the CD6 Lymphocyte Surface Receptor

Mitogen-Activated Protein Kinase Pathway Activation by the CD6 Lymphocyte Surface Receptor

The Accessory Molecules CD5 and CD6 Associate on the Membrane of Lymphoid T Cells

Expression and Characterization of a Novel CD6 Ligand in Cells Derived from Joint and Epithelial Tissues

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