Requirement of cell-cell contact in the induction of Jurkat T cell apoptosis: The membrane-anchored but not soluble form of fasL can trigger anti-CD3-induced apoptosis in Jurkat T cells

Naoki Oyaizu, Nobuhiko Kayagaki, Hideo Yagita, Savita G Pahwa, Yoji Ikawa

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35 Citations (Scopus)

Abstract

Fas ligand (FasL) has been shown to be processed by the action of certain metalloproteinase and released from the cell surface. However, it is unclear whether death of Fas-sensitive target cells is mediated by a membrane-bound form of FasL (mFasL) or by a soluble form of FasL (sFasL). In the present study, we demonstrated that JCaM, a p56lck-deficient mutant of Jurkat, underwent Fas-dependent apoptosis only upon physical contact with anti-CD3-stimulated Jurkat cells or with human FasL- expressing transfectant (hFas/L5178Y). Recombinant FasL or sFasL-containing supernatant failed to induce apoptosis in both Jurkat and JCaM. Moreover, addition of a metalloproteinase inhibitor, which led to the accumulation of mFasL in hFas/L5178Y, was found to augment apoptosis in both Jurkat and JCaM. These findings indicate that, in a physiologic setting represented by the activation-induced cell death in Jurkat T cells, cell-cell contact appears to be required for the induction of Fas-mediated killing.

Original languageEnglish
Pages (from-to)670-675
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume238
Issue number2
DOIs
StatePublished - Sep 18 1997
Externally publishedYes

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Fas Ligand Protein
Jurkat Cells
T-cells
Apoptosis
Membranes
T-Lymphocytes
Metalloproteases
Cell death
Cell Death
Chemical activation

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

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title = "Requirement of cell-cell contact in the induction of Jurkat T cell apoptosis: The membrane-anchored but not soluble form of fasL can trigger anti-CD3-induced apoptosis in Jurkat T cells",
abstract = "Fas ligand (FasL) has been shown to be processed by the action of certain metalloproteinase and released from the cell surface. However, it is unclear whether death of Fas-sensitive target cells is mediated by a membrane-bound form of FasL (mFasL) or by a soluble form of FasL (sFasL). In the present study, we demonstrated that JCaM, a p56lck-deficient mutant of Jurkat, underwent Fas-dependent apoptosis only upon physical contact with anti-CD3-stimulated Jurkat cells or with human FasL- expressing transfectant (hFas/L5178Y). Recombinant FasL or sFasL-containing supernatant failed to induce apoptosis in both Jurkat and JCaM. Moreover, addition of a metalloproteinase inhibitor, which led to the accumulation of mFasL in hFas/L5178Y, was found to augment apoptosis in both Jurkat and JCaM. These findings indicate that, in a physiologic setting represented by the activation-induced cell death in Jurkat T cells, cell-cell contact appears to be required for the induction of Fas-mediated killing.",
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T2 - The membrane-anchored but not soluble form of fasL can trigger anti-CD3-induced apoptosis in Jurkat T cells

AU - Oyaizu, Naoki

AU - Kayagaki, Nobuhiko

AU - Yagita, Hideo

AU - Pahwa, Savita G

AU - Ikawa, Yoji

PY - 1997/9/18

Y1 - 1997/9/18

N2 - Fas ligand (FasL) has been shown to be processed by the action of certain metalloproteinase and released from the cell surface. However, it is unclear whether death of Fas-sensitive target cells is mediated by a membrane-bound form of FasL (mFasL) or by a soluble form of FasL (sFasL). In the present study, we demonstrated that JCaM, a p56lck-deficient mutant of Jurkat, underwent Fas-dependent apoptosis only upon physical contact with anti-CD3-stimulated Jurkat cells or with human FasL- expressing transfectant (hFas/L5178Y). Recombinant FasL or sFasL-containing supernatant failed to induce apoptosis in both Jurkat and JCaM. Moreover, addition of a metalloproteinase inhibitor, which led to the accumulation of mFasL in hFas/L5178Y, was found to augment apoptosis in both Jurkat and JCaM. These findings indicate that, in a physiologic setting represented by the activation-induced cell death in Jurkat T cells, cell-cell contact appears to be required for the induction of Fas-mediated killing.

AB - Fas ligand (FasL) has been shown to be processed by the action of certain metalloproteinase and released from the cell surface. However, it is unclear whether death of Fas-sensitive target cells is mediated by a membrane-bound form of FasL (mFasL) or by a soluble form of FasL (sFasL). In the present study, we demonstrated that JCaM, a p56lck-deficient mutant of Jurkat, underwent Fas-dependent apoptosis only upon physical contact with anti-CD3-stimulated Jurkat cells or with human FasL- expressing transfectant (hFas/L5178Y). Recombinant FasL or sFasL-containing supernatant failed to induce apoptosis in both Jurkat and JCaM. Moreover, addition of a metalloproteinase inhibitor, which led to the accumulation of mFasL in hFas/L5178Y, was found to augment apoptosis in both Jurkat and JCaM. These findings indicate that, in a physiologic setting represented by the activation-induced cell death in Jurkat T cells, cell-cell contact appears to be required for the induction of Fas-mediated killing.

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