Cytoskeletal disruption induces T cell apoptosis by a caspase-3 mediated mechanism

Suria, Hamza; Chau, Luan A.; Negrou, Ella; Kelvin, David J.; Madrenas, Joaquı́n

doi:10.1016/s0024-3205(99)00538-x

Cited by 59 publications

(54 citation statements)

References 63 publications

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“…Conversely, disruption of the actin cytoskeleton can induce apoptosis via activation of death receptors and other mechanisms (32)(33)(34). To determine which is the primary event in a large population of cells, we quantitated F-actin levels in YpkA-expressing cells with and without caspase inhibition using phalloidin staining in a two-color flow cytometric assay.…”

Section: Actin Depolymerization Induced By Ypka Is Secondary To Apoptmentioning

confidence: 99%

The Yersinia Effector Protein YpkA Induces Apoptosis Independently of Actin Depolymerization

Park

Teja

O’Shea

et al. 2007

The Journal of Immunology

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The pathogenicity of the plague agent Yersinia pestis is largely due to the injection of effector proteins that potently block immune responses into host cells through a type III secretion apparatus. One Yersinia effector protein, YpkA, a putative serine/threonine kinase, has been reported to act by depolymerizing actin and disrupting actin microfilament organization. Using YpkA-GFP fusion proteins to directly visualize cells expressing YpkA, we found instead that YpkA triggered rapid cell death that can be blocked by caspase inhibitors and Bcl-xL, but was not dependent on caspase-8. The actin depolymerization promoted by YpkA was only seen in cells with other features of apoptosis, and was blocked by inhibiting apoptosis, indicating that actin filament disruption is likely to be a result, rather than a cause of YpkA-induced apoptosis. A region including aa 133–262 in YpkA was sufficient for inducing apoptosis independent of localization to the plasma membrane. These data suggest that YpkA can act as a direct inducer of cell death.

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Section: Actin Depolymerization Induced By Ypka Is Secondary To Apoptmentioning

confidence: 99%

The Yersinia Effector Protein YpkA Induces Apoptosis Independently of Actin Depolymerization

Park

Teja

O’Shea

et al. 2007

The Journal of Immunology

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“…3F), indicating that cytochalasin B induces capping, irrespective of caspase activity. While cytochalasin B may indeed cause apoptosis under higher concentrations and with protracted treatment, [30][31][32] collectively, these results indicate that at the levels we used, treatment with cytochalasin B does not induce apoptosis in Jurkat cells. Therefore, we can conclude that capping alone is sufficient to signal macrophages to commence phagocytosis.…”

Section: Cytochalasin B-induced Capping Of Cd43 On the Surface Of Jurmentioning

confidence: 63%

“…Independence of Capping and Recognition of Cytochalasin B-Treated Jurkat Cells from Apoptosis Because cytochalasin B is known to cause apoptosis under certain conditions, [30][31][32] it is possible that our treated cells also be- came apoptotic, thereby leading to the observed phagocytosis. In order to eliminate this possibility, we checked the treated cells for additional signs of apoptosis.…”

Section: Cytochalasin B-induced Capping Of Cd43 On the Surface Of Jurmentioning

confidence: 98%

Clearance of CD43-Capped Cells by Macrophages: Capping Alone Leads to Phagocytosis

Oguri

Miki

Hirano

et al. 2012

Biological & Pharmaceutical Bulletin

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“…Generally, cytochalasins inhibit several cellular functions such as chemotaxis, cytokinesis, phagocytosis, and receptor capping under the condition of actin filament depolymerization (8,26,30,36,37,41,44). However, it has been reported that cytochalasins also have some unique abilities to enhance the proliferation and/or differentiation of chemotactic peptide-induced respiratory burst and mitogen-induced T cells (18,23,28).…”

Section: Discussionmentioning

confidence: 99%

Depolymerization of Actin Filament by Cytochalasin E Induces Interleukin‐8 Production and Up‐Regulates CD54 in the HeLa Epithelial Cell Line

Ikewaki

Yamada

Inoko

2003

Microbiology and Immunology

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We previously reported that the depolymerization of actin filament by cytochalasin E enhances low affinity Fcε receptor II (CD23) expression on the human monocyte‐like cell line, U937 (J. Clin. Immunol. 20: 235, 2000). In this study, we found that cytochalasin E strongly induces interleukin‐8 through an epithelial cell line, HeLa, in dose‐ and time‐dependent manners as assessed by enzyme‐linked immunoassay and reverse transcription‐polymerase chain reaction techniques. In addition, interleukin‐8 production in the HeLa cells cultured with cytochalasin E was blocked in the presence of protein kinase C inhibitors, Go6976 and H‐7. On the other hand, it was found that CD54 (intercellular adhesion molecule‐1; ICAM‐1) expression on the HeLa cells and the secretion of soluble CD54 were significantly up‐regulated after culturing with cytochalasin E, and that these up‐regulations of CD54 were also suppressed by Go6976. Taken together, these findings indicate that cytochalasin E activates protein kinase C under the depolymerization of actin filament, leading to the induction of interleukin‐8 production and the up‐regulation of CD54 in HeLa cells.

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Cytoskeletal disruption induces T cell apoptosis by a caspase-3 mediated mechanism

Cited by 59 publications

References 63 publications

The Yersinia Effector Protein YpkA Induces Apoptosis Independently of Actin Depolymerization

The Yersinia Effector Protein YpkA Induces Apoptosis Independently of Actin Depolymerization

Clearance of CD43-Capped Cells by Macrophages: Capping Alone Leads to Phagocytosis

Depolymerization of Actin Filament by Cytochalasin E Induces Interleukin‐8 Production and Up‐Regulates CD54 in the HeLa Epithelial Cell Line

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