Modulation of superantigen‐induced T‐cell deletion by antibody anti‐Pgp‐1 (CD44)

We examined the effects of anti‐Pgp‐1 (CD44) antibody on the in vitro deletion of murine CD4 and CD8 single positive T cells induced by Staphylococcal enterotoxin B (SEB). Soluble anti‐Pgp‐1 antibody enhanced the apoptosis and decreased the proliferation of SEB‐responding T cells. In contrast, cross‐linked anti‐Pgp‐1 antibody provided costimulatory signals for the T‐cell activation induced by anti‐CD3 antibody. Hyaluronic acid (HA), a ligand of Pgp‐1, did not affect proliferation and deletion induced by SEB, whereas it mimicked the effects of the cross‐linked antibody in anti‐CD3‐driven proliferation. T‐cell Pgp‐1 surface expression after 48 hr incubation with SEB was unchanged as compared to unstimulated cells. However, when the memory T cells were established, some Vβ8+ (SEB‐specific) T cells Pgp‐1low became Pgp‐1high, displaying a bimodal character. Moreover, the Pgp‐1 increased expression correlated with an increase of Pgp‐1 soluble form in the supernatant. These findings suggested that signals following the triggering of the Pgp‐1 molecule are important in controlling T‐cell survival.

[1]  C. Riccardi,et al.  CD44 (Pgp-1) inhibits CD3 and dexamethasone-induced apoptosis. , 1995, Blood.

[2]  C. Riccardi,et al.  Superantigen-induced peripheral T-cell deletion: the effects of chemical modification of antigen-presenting cells, interleukin-4 and glucocorticoid hormones. , 1995, Immunology.

[3]  John Calvin Reed,et al.  Anchorage dependence, integrins, and apoptosis , 1994, Cell.

[4]  T. Krakauer Cell adhesion molecules are co-receptors for staphylococcal enterotoxin B-induced T-cell activation and cytokine production. , 1994, Immunology letters.

[5]  M. Sy,et al.  Monoclonal anti-CD44 antibody acts in synergy with anti-CD2 but inhibits anti-CD3 or T cell receptor-mediated signaling in murine T cell hybridomas. , 1993, Cellular immunology.

[6]  P. Herrlich,et al.  CD44 splice variants: metastases meet lymphocytes. , 1993, Immunology today.

[7]  P. Kincade,et al.  Antibody‐induced activation of the hyaluronan receptor function of CD44 requires multivalent binding by antibody , 1993, European journal of immunology.

[8]  E. Reinherz,et al.  Thymic and peripheral apoptosis of antigen‐specific T cells might cooperate in establishing self tolerance , 1993, European journal of immunology.

[9]  D. Longo,et al.  Enhanced lymphokine production and lymphokine receptor expression in multiple antibody-stimulated human CD4+ peripheral blood lymphocytes. , 1992, Journal of immunology.

[10]  V. Hořejší,et al.  Shedding of the CD44 adhesion molecule from leukocytes induced by anti-CD44 monoclonal antibody simulating the effect of a natural receptor ligand. , 1992, Journal of immunology.

[11]  R. Miller,et al.  Peripheral tolerance through clonal deletion of mature CD4-CD8+ T cells. , 1992, International immunology.

[12]  I. Stamenkovic,et al.  Distinct effects of two CD44 isoforms on tumor growth in vivo , 1991, The Journal of experimental medicine.

[13]  H. Macdonald,et al.  Clonal expansion precedes anergy and death of Vβ8+ peripheral T cells responding to staphylococcal enterotoxin B in vivo , 1991, European journal of immunology.

[14]  Y. Kawabe,et al.  Programmed cell death and extrathymic reduction of Vβ8+CD4+ T cells in mice tolerant to Staphylococcus aureus enterotoxin B , 1991, Nature.

[15]  D. Longo,et al.  Peripheral clonal elimination of functional T cells. , 1990, Science.

[16]  C. Nathan,et al.  Shedding of tumor necrosis factor receptors by activated human neutrophils , 1990, The Journal of experimental medicine.

[17]  K. Miyake,et al.  Hyaluronate can function as a cell adhesion molecule and CD44 participates in hyaluronate recognition , 1990, The Journal of experimental medicine.

[18]  I. Stamenkovic,et al.  CD44 is the principal cell surface receptor for hyaluronate , 1990, Cell.

[19]  R. Schwartz,et al.  A cell culture model for T lymphocyte clonal anergy. , 1990, Science.

[20]  S. Sharrow,et al.  Clonal deletion and clonal anergy in the thymus induced by cellular elements with different radiation sensitivities , 1990, The Journal of experimental medicine.

[21]  B. Haynes,et al.  Antibodies against the CD44 p80, lymphocyte homing receptor molecule augment human peripheral blood T cell activation. , 1990, Journal of immunology.

[22]  H. Pircher,et al.  Tolerance induction in double specific T-cell receptor transgenic mice varies with antigen , 1989, Nature.

[23]  B. Caillou,et al.  CD44 contributes to T cell activation. , 1989, Journal of immunology.

[24]  D. Willerford,et al.  Expression of lymphocyte adhesion receptors for high endothelium in primates. Anatomic partitioning and linkage to activation. , 1989, Journal of immunology.

[25]  Philippa Marrack,et al.  The Vβ-specific superantigen staphylococcal enterotoxin B: Stimulation of mature T cells and clonal deletion in neonatal mice , 1989, Cell.

[26]  R. Zinkernagel,et al.  Deletion of self-reactive T cells before entry into the thymus medulla , 1988, Nature.

[27]  David M. Kranz,et al.  Positive and negative selection of an antigen receptor on T cells in transgenic mice , 1988, Nature.

[28]  William,et al.  Characterization of the class III collagen receptor, a phosphorylated, transmembrane glycoprotein expressed in nucleated human cells. , 1988, The Journal of biological chemistry.

[29]  P. Marrack,et al.  Self-tolerance eliminates T cells specific for Mls-modified products of the major histocompatibility complex , 1988, Nature.

[30]  R. Germain,et al.  Functionally distinct subsites on a class II major histocompatibility complex molecule , 1987, Nature.

[31]  J. R. de los Toyos,et al.  Lymphocyte recognition of high endothelium: antibodies to distinct epitopes of an 85-95-kD glycoprotein antigen differentially inhibit lymphocyte binding to lymph node, mucosal, or synovial endothelial cells , 1987, The Journal of cell biology.

[32]  P. Marrack,et al.  T cell tolerance by clonal elimination in the thymus , 1987, Cell.

[33]  S. Meuer,et al.  Alternative pathway activation of T cells by binding of CD2 to its cell-surface ligand , 1987, Nature.

[34]  Michael Loran Dustin,et al.  The T lymphocyte glycoprotein CD2 binds the cell surface ligand LFA-3 , 1987, Nature.

[35]  P. Linsley,et al.  Role of the CD28 receptor in T-cell activation. , 1990, Immunology today.

[36]  S. Jalkanen,et al.  A lymphoid cell surface glycoprotein involved in endothelial cell recognition and lymphocyte homing in man , 1986, European journal of immunology.

[37]  E. Sercarz,et al.  The complexity of structures involved in T-cell activation. , 1983, Annual review of immunology.