Roles of calcium in the regulation of apoptosis in HL-60 promyelocytic leukemia cells

Zhu, Wenhui; Loh, Tatt‐Tuck

doi:10.1016/0024-3205(95)02202-t

Cited by 57 publications

(32 citation statements)

References 22 publications

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“…We used DMSO-differentiated HL-60 cells to further exam- [47][48][49]. More specifically, the cited investigators used undifferentiated HL-60 cells and exposed them to the ionophore for several hours, whereas we used differentiated HL-60 cells treated for only 30 min.…”

Section: Discussionmentioning

confidence: 99%

Activation of the granule pool of the NADPH oxidase accelerates apoptosis in human neutrophils

Lundqvist-Gustafsson

Bengtsson

1999

Journal of Leukocyte Biology

134

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Oxidative stress induces apoptosis in many types of cells, including human neutrophils. Our objective was to determine whether reactive oxygen species (ROS) produced by activated neutrophils are associated with accelerated apoptosis. Exposing neutrophils to ionomycin or phorbol myristate acetate (PMA) induced intracellular H 2 O 2 production and rapid onset of apoptosis, measured as condensed chromatin, cellular shrinkage, and DNA fragmentation. Neutrophils activated with formyl-methionyl-leucyl-phenylalanine (fMLP) generated mainly extracellular H 2 O 2 and did not undergo apoptosis. Exogenously added H 2 O 2 , together with the catalase blocker sodium azide, induced apoptosis to the same extent and with similar kinetics as PMA and ionomycin. Adenosine inhibited ionomycin-induced intracellular H 2 O 2 production and apoptosis. Neither PMA nor ionomycin caused apoptosis in dimethyl sulfoxide-differentiated HL-60 cells, which are incapable of intracellular H 2 O 2 production, whereas H 2 O 2 induced apoptosis more efficiently in these cells than in neutrophils. We propose that activated neutrophils use intracellularly formed H 2 O 2 to commit suicide.

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Section: Discussionmentioning

confidence: 99%

Activation of the granule pool of the NADPH oxidase accelerates apoptosis in human neutrophils

Lundqvist-Gustafsson

Bengtsson

1999

Journal of Leukocyte Biology

134

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“…Although there are examples in the literature of both increases (Furuya et al, 1994;Zhu and Loh, 1995) and decreases (Waterhouse et al, 1996;Chiesa et al, 1998;Mizuno et al, 1998) in CaZte leading to apoptosis, in neurons it is generally decreases in cell Ca2+ that lead to apoptotic cell death (Koh and Cotman, 1992;Franklin et al, 1995;Tong et al, 1996). Apoptosis is elicited in cultured neurons by removing Ca2+ from the media (Koh and Cotman, 1992) or by removing increased K+, which maintains high intracellular Ca2+ often needed for survival of cultured neurons (Franklin et al, 1995).…”

Section: Discussionmentioning

confidence: 99%

“…Loss of endoplasmic reticulum Ca2+ is associated with dramatic decreases in protein synthesis (Bronstrom and Bronstrom, 1990) and has been linked to the release of a deoxyribonuclease, which may contribute to apoptosis (Peitsch et al, 1993). The loss of endoplasmic reticulum Ca2' was proposed as the cause of apoptosis in HL60 leukemia cells (Zhu and Loh, 1995) and GT1-7 hypothalamic cells (Wei et al, 1998). Furthermore, in GT1-7 cells bcl-2 protects against thapsigarginmediated apoptosis without affecting changes in [Ca2'], (Wei et al, 1998 …”

Section: Discussionmentioning

confidence: 99%

“…However, the mode of cell death and direction of change in Ca2fi differ among cell types McConkey and Orrenius, 1997). An overload of Ca2+, contributes directly to excitotoxicity-induced necrosis (Munir et a]., 1995;Ikeda et al, 1996;Gwag et al, 1997) but can also lead to apoptosis (Furuya et al, 1994;Zhu and Loh, 1995) depending on the cell type. Chelation of extracellular Ca" (Ca",) protects against apoptosis induced by specific agents in thymocytes (McConkey et al, 1989;Story …”

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confidence: 99%

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Alterations of Extracellular Calcium Elicit Selective Modes of Cell Death and Protease Activation in SH‐SY5Y Human Neuroblastoma Cells

McGinnis¹,

Wang²,

Gnegy³

1999

Journal of Neurochemistry

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Abstract:The role of intracellular Ca2+ homeostasis in mechanisms of neuronal cell death and cysteine protease activation was investigated in SH-SY5Y human neuroblastoma cells. Cells were incubated in 2 mM EGTA to lower intracellular Ca2+ or 5 mM CaCI, to raise it. Cell death and activation of calpain and caspase-3 were measured. Both EGTA and excess CaCI, elicited cell death. EGTA induced DNA laddering and an increase in caspase-3-like, but not calpain, activity. Pan-caspase inhibitors protected against EGTA-, but not CaCI,-, induced cell death. Conversely, excess Ca2+ elicited necrosis and activated calpain but not caspase-3. Calpain inhibitors did not preserve cell viability. Ca2+ was the death-mediating factor, because restoration of extracelMar Ca2+ protected against cell death induced by EGTA and blockade of Ca2+ channels by Ni'+ protected against that induced by high Ca2+. We conclude that the EGTA treatment lowered intracellular Ca2+ and elicited caspase-3-like protease activity, which led to apoptosis. Conversely, excess extracellular Ca2+ entered Ca2+ channels and increased intracellular Ca2+ leading to calpain activation and necrosis. The mode of cell death and protease activation in response to changing Ca2+ were selective and mutually exclusive, demonstrating that these are useful models to individually investigate apoptosis and necrosis. Key Words: Apoptosis-Necrosis-Calpain-Caspase-3-Ca2+ homeostasis-Neuronal death.

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“…DNA fragmentation was detected as described (Zhu & Loh 1995). In brief, 5¿10 6 cells were collected and lysed in 250 ml lysis buffer (5 mM Tris-HCl, 0.5% Triton X-100 and 20 mM ethylenediaminetetraacetic acid).…”

Section: Methodsmentioning

confidence: 99%

Cyclic Adenosine Monophosphate Inhibits Quinolone Alkaloid Evocarpine‐Induced Apoptosis via Activation of Protein Kinase A in Human Leukaemic HL‐60 Cells

Kim

Pae

Kang

et al. 2000

Pharmacology & Toxicology

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Evocarpine, an isoquinolone alkaloid isolated from the fruit of Evodia rutaecarpa, was found to induce apoptotic cell death in promyelocytic leukaemia HL-60 cells in dose-and time-dependent manners. We investigated the involvement of protein kinase A during the evocarpine-induced apoptotic cell death. Evocarpine-induced apoptosis was markedly inhibited by treatment of the cells with dibutyryl-cyclic adenosine monophosphate. Similar results were obtained with other commonly used cyclic adenosine monophosphate analogues, chlorophenylthio-cyclic adenosine monophosphate and the intracellular cyclic adenosine monophosphate-elevating agent, forskolin. In contrast, pretreatment of HL-60 cells with KT5720, an inhibitor of cyclic adenosine monophosphate-dependent protein kinase A, abrogated the protective effects of cyclic adenosine monophosphate analogues and forskolin on evocrpine-induced apoptosis. These findings suggest that cyclic adenosine monophosphate-dependent activation of protein kinase A plays a crucial role in protecting HL-60 cells from the evocarpine-induced apoptotic cell death.

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Roles of calcium in the regulation of apoptosis in HL-60 promyelocytic leukemia cells

Cited by 57 publications

References 22 publications

Activation of the granule pool of the NADPH oxidase accelerates apoptosis in human neutrophils

Activation of the granule pool of the NADPH oxidase accelerates apoptosis in human neutrophils

Alterations of Extracellular Calcium Elicit Selective Modes of Cell Death and Protease Activation in SH‐SY5Y Human Neuroblastoma Cells

Cyclic Adenosine Monophosphate Inhibits Quinolone Alkaloid Evocarpine‐Induced Apoptosis via Activation of Protein Kinase A in Human Leukaemic HL‐60 Cells

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