Effects of staurosporine on the capacitative regulation of the state of the Ca2+ reserves in activated Jurkat T lymphocytes

Ahnadi, Charaf E.; Payet, M; Dupuis, Gilles

doi:10.1016/s0143-4160(96)90060-3

Cited by 13 publications

(14 citation statements)

References 49 publications

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“…Indeed, induction of CD152L via adhesion was enhanced by staurosporine treatment, whereas IFN-␥ induction remained unaffected. Because staurosporine is an inhibitor of PKC but is also known to inhibit PTKs in some cell types at higher doses (36), these results suggest a potential role for a PKC signaling pathway or a requirement for PTKs when ICOSL is expressed after monocytes become activated by adhesion or IFN-␥. In addition, the observation that ICOSL is not detectable on resting human peripheral blood T or B cells from most donors, but is expressed only at low levels by a subset of dense tonsillar B cells suggests that ICOSL may have a specialized function for monocytic/DC APCs.…”

Section: Discussionmentioning

confidence: 86%

Characterization of Human Inducible Costimulator Ligand Expression and Function

Aicher¹,

Hayden-Ledbetter

Brady

et al. 2000

The Journal of Immunology

223

163

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The inducible costimulator (ICOS) is the newest member of the CD28/CD152 receptor family involved in regulating T cell activation. We constructed a soluble-Ig fusion protein of the extracellular domain of human ICOS and used it as a probe to characterize expression patterns of the ICOS ligand (ICOSL). ICOSIg did not bind to CD80- or CD86-transfected Chinese hamster ovary cell lines, demonstrating that ICOSL is distinct from those ligands identified for CD28/CD152. ICOSIg showed selective binding to monocytic and B cell lines, whereas binding was undetectable on unstimulated monocytes and peripheral blood T and B cells. Expression of ICOSL was induced on monocytes after integrin-dependent plastic adhesion. Pretreatment of monocytes with mAb to the β2-integrin subunit CD18 decreased adhesion and abolished ICOSL up-regulation but had no effect on CD80/86 (CD152 ligand (CD152L)) expression. Both ICOSL and CD152L were up-regulated on monocytes by IFN-γ but by distinct signaling pathways. Unlike CD152L expression, ICOSL expression did not change when monocytes were differentiated into dendritic cells (DCs) or after DCs were induced to mature by LPS, TNF-α, or CD40 ligation. Addition of ICOSIg to allogeneic MLRs between DCs and T cells reduced T cell proliferative responses but did so less efficiently than CTLA4Ig (CD152Ig) did. Similarly, ICOSIg also blocked Ag-specific T cell proliferation to tetanus toxoid. Thus, ICOSL, like CD80/86, is expressed on activated monocytes and dendritic cells but is regulated differently and delivers distinct signals to T cells that can be specifically inhibited by ICOSIg.

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Section: Discussionmentioning

confidence: 86%

Characterization of Human Inducible Costimulator Ligand Expression and Function

Aicher¹,

Hayden-Ledbetter

Brady

et al. 2000

The Journal of Immunology

223

163

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“…Jurkat E6.1 cells were provided by Dr. A. Weiss (Howard Hughes Institute, San Francisco, CA) and cultured as described [34]. Human umbilical cord-derived ECV 304 endothelial cells (American Type Culture Collection, Rockville, MD) were cultured in M199 medium containing penicillin, streptomycin, garamycin, and 10 % FBS.…”

Section: Cellsmentioning

confidence: 99%

“…Jurkat cells in suspension were loaded as described [34]. Jurkat cells and PBL bound to poly-L-lysine-coated [37] coverslips were loaded in the following manner.…”

Section: Furamentioning

confidence: 99%

Clustering the adhesion molecules VLA‐4 (CD49d/CD29) in Jurkat T cells or VCAM‐1 (CD106) in endothelial (ECV 304) cells activates the phosphoinositide pathway and triggers Ca²⁺ mobilization

1997

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Ligation of very late antigen (VLA)-4 (alpha 4 beta 1 integrin) with a cross-linked anti-alpha 4 subunit monoclonal antibody (mAb) triggered a biphasic Ca2+ response in Jurkat cell populations and in peripheral human lymphocytes. Cross-linking vascular cell adhesion molecule (VCAM)-1 (the counter-receptor of VLA-4) in ECV 304 endothelial cells generated a biphasic Ca2+ response. Tumor necrosis factor-alpha-primed human umbilical cord vascular endothelial cells also responded to the cross-linked mAb with a biphasic Ca2+ profile. Ligated VLA-4 (Jurkat cells) or VCAM-1 (ECV 304) stimulated the production of myo-inositol 1,4,5-trisphosphate. ECV 304 cells induced a biphasic Ca2+ response in Fura2-loaded Jurkat cells, whereas a transient response was observed when Jurkat cells were added to Fura2-loaded ECV 304 cells. The Ca2+ responses in these experiments involved VLA-4/VCAM-1 interactions since they were significantly reduced (approximately 80%) by prior treatment of the target cells with the relevant noncross-linked mAb. Close contact between the cells triggered mutual Ca2+ signaling as shown by spectrofluorimetric and confocal microscopy time-dependent recordings. Fibronectin and its CS-1 fragment (V25) triggered a sustained Ca2+ response in Jurkat cells (confocal microscopy). Our results suggest that the VLA-4 and VCAM-1 adhesion molecules can transduce a signal that involves activation of the phosphoinositide pathway and the mobilization of Ca2+.

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“…Also, activators of protein kinase C have repeatedly been found to regulate this process negatively (18,26,27). Staurosporine, an inhibitor of several protein kinases, including protein kinase C (34), has in several reports been shown to augment capacitative Ca 2ϩ entry (35)(36)(37)(38)(39). This suggests that different protein kinases may be active at different steps in the regulation of this pathway and that the balance among antagonistic regulatory reactions dependent on protein phosphorylation may dictate the time dependence and/or steady-state level of Ca 2ϩ influx.…”

Section: From the Department Of Cell Biology The University Of Alabamentioning

confidence: 99%

“…Staurosporine is a microbial alkaloid that was initially described as an inhibitor of protein kinase C but has since been shown to be a broad range inhibitor of protein kinase activity (34). Staurosporine augments capacitative Ca 2ϩ influx in rat parotid acinar (36) and mesangial cells (38) and modulates Ca 2ϩ responses in Jurkat T lymphocytes (39). Also, in Xenopus oocytes the t1 ⁄2 of inhibition of capacitative Ca 2ϩ entry by GTP␥S was found to be increased by staurosporine (37).…”

Section: Staurosporine Reverses the 2dglc-mediated Inhibition Of Capamentioning

confidence: 99%

The Inhibition of Capacitative Calcium Entry Due to ATP Depletion but Not Due to Glucosamine Is Reversed by Staurosporine

Vemuri

Marchase

1999

Journal of Biological Chemistry

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The capacitative Ca 2؉ entry pathway in J774 macrophages is rapidly inhibited by the amino sugar glucosamine. This pathway is also inhibited by treatments such as 2-deoxy-D-glucose (2dGlc) or glucose deprivation that inhibit glycolysis and lead to significant decreases in cellular ATP and other trinucleotides. We sought to determine whether glucosamine's effect on capacitative Ca 2؉ entry was also due to ATP depletion, as has been suggested recently for its link to insulin resistance. In contrast to brief treatments with 2dGlc, there was no significant decrease in ATP following exposure to glucosamine. In addition, the 2dGlc-mediated inhibition of capacitative Ca 2؉ influx was reversed by staurosporine, a microbial alkaloid that inhibits a broad range of protein kinases. Staurosporine was also able to reverse the inhibition of capacitative Ca 2؉ entry seen following other treatments that decreased cellular ATP levels, including cytochalasin B and iodoacetic acid. Other inhibitors of protein kinase C, including bisindolylmaleimide, K252a, H-7, and calphostin C, were unable to mimic this effect of staurosporine. However, the inhibition of capacitative Ca 2؉ influx in the presence of glucosamine was not reversed by staurosporine. These data indicate that the inhibitory action on capacitative Ca 2؉ entry of glucosamine is distinct from that caused by ATP depletion.The amino sugar glucosamine has been shown to have a variety of effects on cell and animal physiology. Numerous reports dating from over 40 years ago (1, 2) document that dietary glucosamine is selectively toxic to some experimentally induced tumors in rodents. In addition, Marshall et al. (3) determined that exogenous glucosamine induced insulin resistance in cultured adipocytes in a manner similar to that caused by hyperglycemia but at a 40-fold lower concentration than that required for glucose. They also showed that inhibition of glucose flux through the hexosamine biosynthetic pathway prevented hyperglycemia-induced insulin resistance from developing. These results have been extended to show that insulin resistance develops in animals infused with glucosamine (4, 5) or in cells (6) and animals (7) that overexpress the rate-limiting enzyme in the hexosamine biosynthetic pathway, glutamine: fructose-6-phosphate amidotransferase. Glucosamine treatment has also been shown to elicit the expression of transform-

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Effects of staurosporine on the capacitative regulation of the state of the Ca2+ reserves in activated Jurkat T lymphocytes

Cited by 13 publications

References 49 publications

Characterization of Human Inducible Costimulator Ligand Expression and Function

Characterization of Human Inducible Costimulator Ligand Expression and Function

Clustering the adhesion molecules VLA‐4 (CD49d/CD29) in Jurkat T cells or VCAM‐1 (CD106) in endothelial (ECV 304) cells activates the phosphoinositide pathway and triggers Ca²⁺ mobilization

The Inhibition of Capacitative Calcium Entry Due to ATP Depletion but Not Due to Glucosamine Is Reversed by Staurosporine

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Effects of staurosporine on the capacitative regulation of the state of the Ca2+ reserves in activated Jurkat T lymphocytes

Cited by 13 publications

References 49 publications

Characterization of Human Inducible Costimulator Ligand Expression and Function

Characterization of Human Inducible Costimulator Ligand Expression and Function

Clustering the adhesion molecules VLA‐4 (CD49d/CD29) in Jurkat T cells or VCAM‐1 (CD106) in endothelial (ECV 304) cells activates the phosphoinositide pathway and triggers Ca2+ mobilization

The Inhibition of Capacitative Calcium Entry Due to ATP Depletion but Not Due to Glucosamine Is Reversed by Staurosporine

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Clustering the adhesion molecules VLA‐4 (CD49d/CD29) in Jurkat T cells or VCAM‐1 (CD106) in endothelial (ECV 304) cells activates the phosphoinositide pathway and triggers Ca²⁺ mobilization