Metalloproteinase-mediated release of human Fas ligand.

Fas ligand (FasL) is a type II integral membrane protein homologous with tumor necrosis factor (TNF). Recent studies indicate that TNF is processed to yield the soluble cytokine by metalloproteinases at the cell surface of activated macrophages and T cells. In the present study, we investigated whether FasL is also released by metalloproteinases. Treatment with hydroxamic acid inhibitors of matrix metalloproteinases specifically led to accumulation of membrane-type FasL (p40) on the surface of human FasL cDNA transfectants and activated human T cells, as estimated by surface immunofluorescence and immunoprecipitation with newly established anti-human FasL monoclonal antibodies. This surface accumulation of mFasL was associated with the decrease of soluble FasL (p27) in the supernatant as estimated by quantitative ELISA and immunoprecipitation with anti-human FasL monoclonal antibodies. These results indicate that human FasL is efficiently released from the cell surface by metalloproteinases like TNF.

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Antibodies as antigens. The use of mouse monoclonal antibodies to focus human T cells against selected targets.

Journal of Experimental Medicine ◽

10.1084/jem.167.2.345 ◽

1988 ◽

Vol 167 (2) ◽

pp. 345-352 ◽

Cited By ~ 72

Author(s):

A Lanzavecchia ◽

S Abrignani ◽

D Scheidegger ◽

R Obrist ◽

B Dörken ◽

...

Keyword(s):

T Cells ◽

Monoclonal Antibodies ◽

Cell Surface ◽

Mhc Class Ii ◽

Class Ii ◽

Cell Surface Molecules ◽

Tumor Patients ◽

Surface Molecules ◽

Human T Cells ◽

Positive Target

We found that three tumor patients treated with mouse mAbs have T cells that recognize processed mouse Ig on autologous APC in a class II-restricted fashion, and we have shown that mouse mAbs directed against various cell surface molecules can be used as antigens to focus these T cells on an MHC class II-positive target of choice.

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Two NFAT Transcription Factor Binding Sites Participate in the Regulation of CD95 (Fas) Ligand Expression in Activated Human T Cells

Journal of Biological Chemistry ◽

10.1074/jbc.272.50.31427 ◽

1997 ◽

Vol 272 (50) ◽

pp. 31427-31434 ◽

Cited By ~ 161

Author(s):

Kevin M. Latinis ◽

Lyse A. Norian ◽

Steve L. Eliason ◽

Gary A. Koretzky

Keyword(s):

T Cells ◽

Transcription Factor ◽

Binding Sites ◽

Fas Ligand ◽

Transcription Factor Binding Sites ◽

Transcription Factor Binding ◽

Factor Binding ◽

Human T Cells ◽

Ligand Expression ◽

Nfat Transcription Factor

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Degranulation plays an essential part in regulating cell surface expression of Fas ligand in T cells and natural killer cells

Nature Medicine ◽

10.1038/4779 ◽

1999 ◽

Vol 5 (1) ◽

pp. 90-96 ◽

Cited By ~ 259

Author(s):

G. Bossi ◽

G.M. Griffiths

Keyword(s):

T Cells ◽

Natural Killer Cells ◽

Cell Surface ◽

Natural Killer ◽

Fas Ligand ◽

Surface Expression ◽

Cell Surface Expression ◽

Killer Cells

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Tumor necrosis factor induces rapid down-regulation of TXNIP in human T cells

Scientific Reports ◽

10.1038/s41598-019-53234-x ◽

2019 ◽

Vol 9 (1) ◽

Cited By ~ 2

Author(s):

Trine B. Levring ◽

Martin Kongsbak-Wismann ◽

Anna K. O. Rode ◽

Fatima A. H. Al-Jaberi ◽

Daniel V. Lopez ◽

...

Keyword(s):

T Cells ◽

Tumor Necrosis Factor ◽

Glucose Uptake ◽

Tumor Necrosis ◽

Gradient Centrifugation ◽

Tumor Necrosis Factor Receptor ◽

Down Regulation ◽

Interacting Protein ◽

Human T Cells ◽

Necrosis Factor

Abstract In addition to antigen-driven signals, T cells need co-stimulatory signals for robust activation. Several receptors, including members of the tumor necrosis factor receptor superfamily (TNFRSF), can deliver co-stimulatory signals to T cells. Thioredoxin interacting protein (TXNIP) is an important inhibitor of glucose uptake and cell proliferation, but it is unknown how TXNIP is regulated in T cells. The aim of this study was to determine expression levels and regulation of TXNIP in human T cells. We found that naïve T cells express high levels of TXNIP and that treatment of blood samples with TNF results in rapid down-regulation of TXNIP in the T cells. TNF-induced TXNIP down-regulation correlated with increased glucose uptake. Furthermore, we found that density gradient centrifugation (DGC) induced down-regulation of TXNIP. We demonstrate that DGC induced TNF production that paralleled the TXNIP down-regulation. Treatment of blood with toll-like receptor (TLR) ligands induced TNF production and TXNIP down-regulation, suggesting that damage-associated molecular patterns (DAMPs), such as endogenous TLR ligands, released during DGC play a role in DGC-induced TXNIP down-regulation. Finally, we demonstrate that TNF-induced TXNIP down-regulation is dependent on caspase activity and is caused by caspase-mediated cleavage of TXNIP.

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Interaction of IL-1β, IL-6 and tumour necrosis factor-alpha (TNF-α) in human T cells activated by murine antigens

Clinical & Experimental Immunology ◽

10.1111/j.1365-2249.1993.tb08203.x ◽

1993 ◽

Vol 93 (3) ◽

pp. 471-478 ◽

Cited By ~ 21

Author(s):

S. PANZER ◽

M. MADDEN ◽

K. MATSUKI

Keyword(s):

T Cells ◽

Tumour Necrosis Factor ◽

Tumour Necrosis ◽

Tumour Necrosis Factor Alpha ◽

Necrosis Factor Alpha ◽

Human T Cells ◽

Tnf Α ◽

Factor Alpha ◽

Necrosis Factor

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Phenomenon of Rosette Formation of Human T Cells Analyzed with Monoclonal Antibodies. The Same Mechanism of Interaction Accounts for Rosette Formation with Erythrocytes from Many Species, Including Autologous Erythrocytes

Leucocyte Typing ◽

10.1007/978-3-642-68857-7_15 ◽

1984 ◽

pp. 281-293 ◽

Cited By ~ 2

Author(s):

M. Amiot ◽

A. Bernard ◽

C. Gelin ◽

B. Raynal ◽

L. Boumsell

Keyword(s):

T Cells ◽

Monoclonal Antibodies ◽

Rosette Formation ◽

Human T Cells ◽

Mechanism Of Interaction

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Analysis of T lymphocytes after bone marrow transplantation using monoclonal antibodies

Blood ◽

10.1182/blood.v60.3.578.578 ◽

1982 ◽

Vol 60 (3) ◽

pp. 578-582 ◽

Cited By ~ 20

Author(s):

R Fox ◽

R McMillan ◽

W Spruce ◽

P Tani ◽

D Mason

Keyword(s):

Bone Marrow ◽

T Cells ◽

Monoclonal Antibodies ◽

Bone Marrow Transplantation ◽

T Cell ◽

Cell Surface ◽

Marrow Transplantation ◽

T Cell Subsets ◽

Clinically Significant ◽

Abnormal Ratio

Abstract Using monoclonal antibodies to cell surface antigens and fluorescent cell sorter analysis, we studied peripheral blood lymphocyte subsets after bone marrow transplantation (BMT). In 13 patients studied 3 mo or more after BMT, the ratio of T-cell subsets defined by antibodies OKT4 and OKT8 was reversed (OKT4/OK%8 = 0.7 +/- 0.3) in comparison to normal volunteers or bone marrow donors (ratio OKT4/OKT8 = 1.7 +/- 0.4) (p less than 0.001). This reversed ratio persisted for up to 3 yr after BMT. In contrast to a previous report, presence of an abnormal ratio of T-cell subsets did not correlate with clinically significant graft- versus-host disease (GVHD). In agreement with a previous study, (26% +/- 8%; less than 4% in normals (p less than 0.001) and antibody OKT10 reactive cells (39% +/- 20% versus 10% +/- 4%) (p less than 0.01), suggesting in vivo activation. However, their PBL did not react with antibody B3/25 (antitransferrin receptor), a marker found on normal PBL after in vitro activation by mitogens (BMT patients less than 5%; normal PBL T cells plus PHA 45% +/- 11%). These results demonstrate that BMT patients have: (A) an abnormal ratio of T-cell subsets in the presence or absence of clinically significant GVDH disease so that these measurements were not useful in monitoring patients; (B) an increased number of T cells with cell surface phenotype (OKT8+, Ia+, OKT10+, B3/25-) that is distinct from normals but similar to patients with infectious mononucleosis or acquired hypogammaglobulinemia.

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