Direct evidence of involvement of glycosylphosphatidylinositol‐anchored proteins in the heavy metal‐mediated signal delivery into T lymphocytes

Pu, Mei-yi; Ma, Li; Ohkusu, Kozo; Isobe, Ken‐ichi; Taguchi, Ryo; Ikezawa, Hiroh; Hamaguchi, Michinari; Nakashima, Izumi

doi:10.1016/0014-5793(95)00193-d

Cited by 12 publications

(8 citation statements)

References 27 publications

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“…HgCl 2 is able to directly modify intracellular signaling in T cells [45,46]. We show that HgCl 2 enhances the effect of PMA on CD134 expression, similar to ionomycin.…”

Section: Discussionmentioning

confidence: 70%

Strong expression of CD134 (OX40), a member of the TNF receptor family, in a T helper 2-type cytokine environment

Roos

Schilder-Tol

Weening

et al. 1998

Journal of Leukocyte Biology

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“…HgCl 2 is able to directly modify intracellular signaling in T cells [45,46]. We show that HgCl 2 enhances the effect of PMA on CD134 expression, similar to ionomycin.…”

Section: Discussionmentioning

confidence: 70%

Strong expression of CD134 (OX40), a member of the TNF receptor family, in a T helper 2-type cytokine environment

Roos

Schilder-Tol

Weening

et al. 1998

Journal of Leukocyte Biology

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“…Correspondingly, we previously suggested that GPI-anchored proteins are obligatorily involved in Hg 2ϩ -induced signaling in T lymphocytes (36,40). To investigate the possible role of the detergentinsoluble membrane raft structure in protein tyrosine phosphorylation and subsequent MAPK family member activation by arsenite, we preincubated thymocytes with ␤ cyclodextrin, which disrupts cholesterol-rich microdomains in the membrane (23,41), before adding NaAsO 2 .…”

Section: The Role Of the Membrane Raft Structure In Arsenite-mediatedmentioning

confidence: 99%

Arsenite Induces Apoptosis of Murine T Lymphocytes Through Membrane Raft-Linked Signaling for Activation of c-Jun Amino-Terminal Kinase

Hossain

Akhand

Kato

et al. 2000

The Journal of Immunology

Self Cite

112

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Because of its dual roles in acute toxicity and in therapeutic application in cancer treatment, arsenic has recently attracted a renewed attention. In this study, we report NaAsO2-induced signal cascades from the cell surface to the nucleus of murine thymic T lymphocytes that involve membrane rafts as an initial signal transducer. NaAsO2 induced apoptosis through fragmentation of DNA, activation of caspase, and reciprocal regulation of Bcl-2/Bax with the concomitant reduction of membrane potential. We demonstrated that NaAsO2-induced caspase activation is dependent on curcumin-sensitive c-Jun amino-terminal kinase and barely dependent on SB203580-sensitive p38 kinase or PD98059-sensitive extracellular signal-regulated kinase. Additionally, staurosporine, which severely inhibited the activation of mitogen-activated protein (MAP) family kinases and c-Jun, partially blocked the NaAsO2-mediated signal for poly(ADP-ribose) polymerase (PARP) degradation. Potentially as the initial cell surface event for intracellular signaling, NaAsO2 induced aggregation of GPI-anchored protein Thy-1 and superoxide production. This Thy-1 aggregation and subsequent activation of MAP family kinase and c-Jun and the degradation of PARP induced by NaAsO2 were all inhibited by DTT, suggesting the requirement of interaction between arsenic and protein sulfhydryl groups for those effects. β cyclodextrin, which sequestrates cholesterol from the membrane rafts, inhibited NaAsO2-induced activation of protein tyrosine kinases and MAP family kinases, degradation of PARP, and production of superoxide. In addition, β cyclodextrin dispersed NaAsO2-induced Thy-1 clustering. These results suggest that a membrane raft integrity-dependent cell surface event is a prerequisite for NaAsO2-induced protein tyrosine kinase/c-Jun amino-terminal kinase activation, superoxide production, and downstream caspase activation.

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“…Some of these proteins are enzymes, such as placental alkaline phosphatase (5) and erythrocyte acetylcholinesterase (6), whereas others appear to be involved in cell adhesion, complement regulation, or even in transport (1). Still others are thought to play roles in communication between cells (7)(8)(9)(10)(11), and there is accumulating evidence that clustering of some GPI-anchored proteins may represent a new mechanism of signal transduction. Thus macrophages and neutrophils are activated by antibody cross-linking of CD14 (lipopolysaccharide receptor) and CD16 (Fc-␥RIIIB), which leads to cytokine expression and oxidative burst (12)(13)(14), and cross-linking of several T-lymphocyte GPI-anchored proteins produces profound regulatory signals (15)(16)(17)(18).…”

Section: Glycosylphosphatidylinositol (Gpi)mentioning

confidence: 99%

Glycosylphosphatidylinositol Anchors of Membrane Glycoproteins Are Binding Determinants for the Channel-forming Toxin Aerolysin

Diep

Nelson

Raja

et al. 1998

Journal of Biological Chemistry

179

173

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Cells that are sensitive to the channel-forming toxin aerolysin contain surface glycoproteins that bind the toxin with high affinity. Here we show that a common feature of aerolysin receptors is the presence of a glycosylphosphatidylinositol anchor, and we present evidence that the anchor itself is an essential part of the toxin binding determinant. The glycosylphosphatidylinositol (GPI)-anchored T-lymphocyte protein Thy-1 is an example of a protein that acts as an aerolysin receptor. This protein retained its ability to bind aerolysin when it was expressed in Chinese hamster ovary cells, but could not bind the toxin when expressed in Escherichia coli, where the GPI anchor is absent. An unrelated GPI-anchored protein, the variant surface glycoprotein of trypanosomes, was shown to bind aerolysin with similar affinity to Thy-1, and this binding ability was significantly reduced when the anchor was removed chemically. Cathepsin D, a protein with no affinity for aerolysin, was converted to an aerolysin binding form when it was expressed as a GPI-anchored hybrid in COS cells. Not all GPI-anchored proteins bind aerolysin. In some cases this may be due to differences in the structure of the anchor itself. Thus the GPI-anchored proteins procyclin of Trypanosoma congolense and gp63 of Leishmania major did not bind aerolysin, but when gp63 was expressed with a mammalian GPI anchor in Chinese hamster ovary cells, it bound the toxin.

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Direct evidence of involvement of glycosylphosphatidylinositol‐anchored proteins in the heavy metal‐mediated signal delivery into T lymphocytes

Cited by 12 publications

References 27 publications

Strong expression of CD134 (OX40), a member of the TNF receptor family, in a T helper 2-type cytokine environment

Strong expression of CD134 (OX40), a member of the TNF receptor family, in a T helper 2-type cytokine environment

Arsenite Induces Apoptosis of Murine T Lymphocytes Through Membrane Raft-Linked Signaling for Activation of c-Jun Amino-Terminal Kinase

Glycosylphosphatidylinositol Anchors of Membrane Glycoproteins Are Binding Determinants for the Channel-forming Toxin Aerolysin

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