Journal articles: 'Apoptosis/Necrosis'

1

Peter, Marcus E. "Apoptosis meets necrosis." Nature 471, no. 7338 (March 2011): 310–12. http://dx.doi.org/10.1038/471310a.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Zhivotovsky, Boris. "Apoptosis, Necrosis and Between." Cell Cycle 3, no. 1 (January 2004): 63–65. http://dx.doi.org/10.4161/cc.3.1.606.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Hurtley, S. M. "Apoptosis, necrosis, and pyroptosis." Science 352, no. 6281 (March 31, 2016): 48–50. http://dx.doi.org/10.1126/science.352.6281.48-j.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Proskuryakov, S. Ya, V. L. Gabai, A. G. Konoplyannikov, I. A. Zamulaeva, and A. I. Kolesnikova. "Immunology of Apoptosis and Necrosis." Biochemistry (Moscow) 70, no. 12 (December 2005): 1310–20. http://dx.doi.org/10.1007/s10541-005-0263-4.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Zhivotovsky, Boris, Afshin Samali, and Sten Orrenius. "Determination of Apoptosis and Necrosis." Current Protocols in Toxicology 00, no. 1 (May 1999): 2.2.1–2.2.34. http://dx.doi.org/10.1002/0471140856.tx0202s00.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

Liu, Huiping, Bradley C. McPherson, and Zhenhai Yao. "Preconditioning attenuates apoptosis and necrosis: role of protein kinase Cε and -δ isoforms." American Journal of Physiology-Heart and Circulatory Physiology 281, no. 1 (July 1, 2001): H404—H410. http://dx.doi.org/10.1152/ajpheart.2001.281.1.h404.

Full text

Abstract:

Preconditioning reduces cardiomyocyte necrosis in vivo and in vitro, but it is unknown whether preconditioning blocks apoptosis. We wanted to compare the effects of preconditioning on necrosis and apoptosis in cardiomyocytes. Necrosis was detected with propidium iodide, and apoptosis was quantified by three complementary techniques: flow cytometry, TdT-mediated dUTP nick-end labeling assay, and DNA-laddering electrophoresis. Apoptosis increased with simulated ischemia time (6 h, 19 ± 1%; 12 h, 27 ± 2%; 18 h, 40 ± 4%; 24 h, 54 ± 4%; and 36 h, 83 ± 4%; n = 6 for each group). Simulated ischemia and reoxygenation contributed equally to apoptosis (12-h ischemia, 27 ± 2%, n = 6; 12-h ischemia and 12-h reoxygenation, 51 ± 4%, n = 6; and 24-h ischemia, 54 ± 5%, n = 8). Necrosis occurred primarily during reoxygenation; none was detected during simulated ischemia. Preconditioning with 10 min of simulated ischemia reduced necrosis (18 ± 6%, n = 8) but had no effect on apoptosis. However, three 1-min cycles of simulated ischemia separated by 5 min of reoxygenation reduced necrosis and apoptosis similarly. The protein kinase C (PKC) inhibitors Go6976 (0.1 μM) or chelerythrene (4 μM) abolished the effect of preconditioning. Preconditioning selectively activated PKCε but had no effect on PKCδ and on total PKC enzyme activity. Preconditioning protected against necrosis and apoptosis, but the preconditioning ischemia required for blocking apoptosis was less than that for reducing necrosis. Activation of PKCε isoform is important in mediating the protection.

APA, Harvard, Vancouver, ISO, and other styles

7

SNIDER, B. JOY, FRANK J. GOTTRON, and DENNIS W. CHOI. "Apoptosis and Necrosis in Cerebrovascular Disease." Annals of the New York Academy of Sciences 893, no. 1 OXIDATIVE/ENE (November 1999): 243–53. http://dx.doi.org/10.1111/j.1749-6632.1999.tb07829.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Jaeschke, Hartmut, Jaspreet S. Gujral, and Mary Lynn Bajt. "Apoptosis and necrosis in liver disease." Liver International 24, no. 2 (April 2004): 85–89. http://dx.doi.org/10.1111/j.1478-3231.2004.0906.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Nicotera, Pierluigi, and Stuart A. Lipton. "Excitotoxins in Neuronal Apoptosis and Necrosis." Journal of Cerebral Blood Flow & Metabolism 19, no. 6 (June 1999): 583–91. http://dx.doi.org/10.1097/00004647-199906000-00001.

Full text

Abstract:

Neuronal loss is common to many neurodegenerative diseases. Although necrosis is a common histopathologic feature observed in neuropathologic conditions, evidence is increasing that apoptosis can significantly contribute to neuronal demise. The prevalence of either type of cell death, apoptosis or necrosis, and the relevance for the progression of disease is still unclear. The debate on the occurrence and prevalence of one or the other type of death in pathologic conditions such as stroke or neurotoxic injury may in part be resolved by the proposal that different types of cell death within a tissue reflect either partial or complete execution of a common death program. Apoptosis is an active process of cell destruction, characterized morphologically by cell shrinkage, chromatin aggregation with extensive genomic fragmentation, and nuclear pyknosis. In contrast, necrosis is characterized by cell swelling, linked to rapid energy loss, and generalized disruption of ionic and internal homeostasis. This swiftly leads to membrane lysis, release of intracellular constituents that evoke a local inflammatory reaction, edema, and injury to the surrounding tissue. During the past few years, our laboratories have studied the signals and mechanisms responsible for induction or prevention of apoptosis/necrosis in neuronal injury and this is the subject of this review.

APA, Harvard, Vancouver, ISO, and other styles

10

McConkey, David J. "Biochemical determinants of apoptosis and necrosis." Toxicology Letters 99, no. 3 (November 1998): 157–68. http://dx.doi.org/10.1016/s0378-4274(98)00155-6.

Full text

APA, Harvard, Vancouver, ISO, and other styles

11

Bhatia, Madhav. "Apoptosis versus necrosis in acute pancreatitis." American Journal of Physiology-Gastrointestinal and Liver Physiology 286, no. 2 (February 2004): G189—G196. http://dx.doi.org/10.1152/ajpgi.00304.2003.

Full text

Abstract:

Acute pancreatitis is a disease of variable severity in which some patients experience mild, self-limited attacks, whereas others manifest a severe, highly morbid, and frequently lethal attack. The events that regulate the severity of acute pancreatitis are, for the most part, unknown. It is generally believed that the earliest events in acute pancreatitis occur within acinar cells and result in acinar cell injury. Other processes, such as recruitment of inflammatory cells and generation of inflammatory mediators, are believed to occur subsequent to acinar cell injury, and these “downstream” events are believed to influence the severity of the disease. Several recently reported studies, however, have suggested that the acinar cell response to injury may, itself, be an important determinant of disease severity. In these studies, mild acute pancreatitis was found to be associated with extensive apoptotic acinar cell death, whereas severe acute pancreatitis was found to involve extensive acinar cell necrosis but very little acinar cell apoptosis. These observations led to the hypothesis that apoptosis could be a favorable response to acinar cells and that interventions that favor induction of apoptotic, as opposed to necrotic, acinar cell death might reduce the severity of an attack of acute pancreatitis. Indeed, in an experimental setting, the induction of pancreatic acinar cell apoptosis protects mice against acute pancreatitis. Little is known about the mechanism of apoptosis in the pancreatic acinar cell, although some early attempts have been made in that direction. Also, clinical relevance of these experimental studies remains to be investigated.

APA, Harvard, Vancouver, ISO, and other styles

12

Nikoletopoulou, Vassiliki, Maria Markaki, Konstantinos Palikaras, and Nektarios Tavernarakis. "Crosstalk between apoptosis, necrosis and autophagy." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1833, no. 12 (December 2013): 3448–59. http://dx.doi.org/10.1016/j.bbamcr.2013.06.001.

Full text

APA, Harvard, Vancouver, ISO, and other styles

13

Nicotera, Pierluigi, and Gerry Melino. "Regulation of the apoptosis–necrosis switch." Oncogene 23, no. 16 (April 2004): 2757–65. http://dx.doi.org/10.1038/sj.onc.1207559.

Full text

APA, Harvard, Vancouver, ISO, and other styles

14

Morioka, Sho, Peter Broglie, Emily Omori, Yuka Ikeda, Giichi Takaesu, Kunihiro Matsumoto, and Jun Ninomiya-Tsuji. "TAK1 kinase switches cell fate from apoptosis to necrosis following TNF stimulation." Journal of Cell Biology 204, no. 4 (February 17, 2014): 607–23. http://dx.doi.org/10.1083/jcb.201305070.

Full text

Abstract:

TNF activates three distinct intracellular signaling cascades leading to cell survival, caspase-8–mediated apoptosis, or receptor interacting protein kinase 3 (RIPK3)–dependent necrosis, also called necroptosis. Depending on the cellular context, one of these pathways is activated upon TNF challenge. When caspase-8 is activated, it drives the apoptosis cascade and blocks RIPK3-dependent necrosis. Here we report the biological event switching to activate necrosis over apoptosis. TAK1 kinase is normally transiently activated upon TNF stimulation. We found that prolonged and hyperactivation of TAK1 induced phosphorylation and activation of RIPK3, leading to necrosis without caspase activation. In addition, we also demonstrated that activation of RIPK1 and RIPK3 promoted TAK1 activation, suggesting a positive feedforward loop of RIPK1, RIPK3, and TAK1. Conversely, ablation of TAK1 caused caspase-dependent apoptosis, in which Ripk3 deletion did not block cell death either in vivo or in vitro. Our results reveal that TAK1 activation drives RIPK3-dependent necrosis and inhibits apoptosis. TAK1 acts as a switch between apoptosis and necrosis.

APA, Harvard, Vancouver, ISO, and other styles

15

Priante, Giovanna, Lisa Gianesello, Monica Ceol, Dorella Del Prete, and Franca Anglani. "Cell Death in the Kidney." International Journal of Molecular Sciences 20, no. 14 (July 23, 2019): 3598. http://dx.doi.org/10.3390/ijms20143598.

Full text

Abstract:

Apoptotic cell death is usually a response to the cell’s microenvironment. In the kidney, apoptosis contributes to parenchymal cell loss in the course of acute and chronic renal injury, but does not trigger an inflammatory response. What distinguishes necrosis from apoptosis is the rupture of the plasma membrane, so necrotic cell death is accompanied by the release of unprocessed intracellular content, including cellular organelles, which are highly immunogenic proteins. The relative contribution of apoptosis and necrosis to injury varies, depending on the severity of the insult. Regulated cell death may result from immunologically silent apoptosis or from immunogenic necrosis. Recent advances have enhanced the most revolutionary concept of regulated necrosis. Several modalities of regulated necrosis have been described, such as necroptosis, ferroptosis, pyroptosis, and mitochondrial permeability transition-dependent regulated necrosis. We review the different modalities of apoptosis, necrosis, and regulated necrosis in kidney injury, focusing particularly on evidence implicating cell death in ectopic renal calcification. We also review the evidence for the role of cell death in kidney injury, which may pave the way for new therapeutic opportunities.

APA, Harvard, Vancouver, ISO, and other styles

16

Elmore, Susan A., Darlene Dixon, James R. Hailey, Takanori Harada, Ronald A. Herbert, Robert R. Maronpot, Thomas Nolte, et al. "Recommendations from the INHAND Apoptosis/Necrosis Working Group." Toxicologic Pathology 44, no. 2 (February 2016): 173–88. http://dx.doi.org/10.1177/0192623315625859.

Full text

Abstract:

Historically, there has been confusion relating to the diagnostic nomenclature for individual cell death. Toxicologic pathologists have generally used the terms “single cell necrosis” and “apoptosis” interchangeably. Increased research on the mechanisms of cell death in recent years has led to the understanding that apoptosis and necrosis involve different cellular pathways and that these differences can have important implications when considering overall mechanisms of toxicity, and, for these reasons, the separate terms of apoptosis and necrosis should be used whenever differentiation is possible. However, it is also recognized that differentiation of the precise pathway of cell death may not be important, necessary, or possible in routine toxicity studies and so a more general term to indicate cell death is warranted in these situations. Morphological distinction between these two forms of cell death can sometimes be straightforward but can also be challenging. This article provides a brief discussion of the cellular mechanisms and morphological features of apoptosis and necrosis as well as guidance on when the pathologist should use these terms. It provides recommended nomenclature along with diagnostic criteria (in hematoxylin and eosin [H&E]-stained sections) for the most common forms of cell death (apoptosis and necrosis). This document is intended to serve as current guidance for the nomenclature of cell death for the International Harmonization of Nomenclature and Diagnostic Criteria Organ Working Groups and the toxicologic pathology community at large. The specific recommendations are: Use necrosis and apoptosis as separate diagnostic terms. Use modifiers to denote the distribution of necrosis (e.g., necrosis, single cell; necrosis, focal; necrosis, diffuse; etc.). Use the combined term apoptosis/single cell necrosis when There is no requirement or need to split the processes, or When the nature of cell death cannot be determined with certainty, or When both processes are present together. The diagnosis should be based primarily on the morphological features in H&E-stained sections. When needed, additional, special techniques to identify and characterize apoptosis can also be used.

APA, Harvard, Vancouver, ISO, and other styles

17

Bisgin, A., H. Eyigor, U. Osma, M. D. Yilmaz, and A. D. Yalcin. "Serum soluble tumour necrosis factor related apoptosis-inducing ligand level and peripheral eosinophil count in patients with nasal polyposis." Journal of Laryngology & Otology 129, no. 3 (February 6, 2015): 250–53. http://dx.doi.org/10.1017/s0022215114003442.

Full text

Abstract:

AbstractBackground:Nasal polyposis is one of the most common inflammatory pathologies of the nasal cavity. Eosinophilic inflammation plays an important role in the pathogenesis. This study aimed to investigate soluble tumour necrosis factor related apoptosis-inducing ligand levels and eosinophil count in nasal polyposis patients.Methods:The study was performed on 24 adult nasal polyposis patients and 24 age-matched healthy individuals. The patients had not received any medical or surgical treatment. Pre-operative computed tomography scans were assessed using the Lund–MacKay grading system, and soluble tumour necrosis factor related apoptosis-inducing ligand levels were measured with a sandwich enzyme-linked immunosorbent assay.Results:Compared with controls, eosinophil levels in nasal polyposis patients were increased (p = 0.024), but there was no significant difference in soluble tumour necrosis factor related apoptosis-inducing ligand levels (p = 0.529). The Lund–Mackay mean grading was 12.43 ± 6.9. There was no correlation between soluble tumour necrosis factor related apoptosis-inducing ligand level and Lund–Mackay grading and eosinophil count.Conclusion:There was no relationship between soluble tumour necrosis factor related apoptosis-inducing ligand level and blood eosinophil or clinical markers; however, soluble tumour necrosis factor related apoptosis-inducing ligand level remains of interest for future studies.

APA, Harvard, Vancouver, ISO, and other styles

18

Herman, Brian. "Protein Dynamics During Apoptosis." Microscopy and Microanalysis 5, S2 (August 1999): 1040–41. http://dx.doi.org/10.1017/s1431927600018523.

Full text

Abstract:

Apoptosis is an actively regulated process of cell death necessary for proper control of tissue growth. The phenomenon is characterized by plasma membrane blebbing, cell shrinkage, chromatin condensation, and degradation of DNA. Apoptosis is distinctly different from necrosis. Unlike necrosis, which is a passive form of cell death, apoptosis appears to be an active physiological process using a controlled genetic “program” of gene expression. Furthermore, apoptosis does not involve severe tissue damage or inflammation. Membrane integrity is preserved, and there is no loss of cellular contents before phagocytosis. Apoptosis is also distinct from necrosis in that it can be triggered or suppressed by tissue-specific hormones and growth factors.Apoptosis plays a critical role in tissue homeostasis by counterbalancing mitosis. It is an essential component of many physiological processes, including embryonic development, clonal selection in thymocytes, and in protection against disease.

APA, Harvard, Vancouver, ISO, and other styles

19

Nicotera, Pierluigi, Marcel Leist, and Elisa Ferrando-May. "Apoptosis and necrosis: different execution of the same death." Biochemical Society Symposia 66 (September 1, 1999): 69–73. http://dx.doi.org/10.1042/bss0660069.

Full text

Abstract:

Regardless of whether apoptosis or necrosis are elicited by toxicants or by pathophysiological conditions, they are considered conceptually distinct forms of cell death. Nevertheless, there is increasing evidence that classical apoptosis and necrosis represent only the extreme ends of a wide range of possible morphological and biochemical deaths. The two classical types of demise can occur simultaneously in tissues or cell cultures exposed to the same stimulus and, often, the intensity of the same initial insult decides the prevalence of either apoptosis or necrosis. The execution of the death programme seems to involve a relatively limited number of pathways. In many instances, their ordered execution results in characteristic morphological and biochemical changes termed apoptosis. However, some subroutines of the degradation programme may not be active in all cases of cell death. Then, the morphological appearance of dying cells and some of their biochemical alterations differ from those of classical apoptosis. We have recently shown that intracellular energy levels and mitochondrial function are rapidly compromised in necrosis, but not in apoptosis, of neuronal cells. Then we went on to show that pre-emptying human T-cells of ATP switches the type of demise caused by two classic apoptotic triggers (staurosporine and CD95 stimulation) from apoptosis to necrosis. Conditions of controlled intracellular ATP depletion, obtained by blocking mitochondrial and/or glycolytic ATP generation, were used in combination with repletion of the cytosolic ATP pool with glucose to redirect the death programme towards apoptosis or necrosis.

APA, Harvard, Vancouver, ISO, and other styles

20

Wang, J. H., H. P. Redmond, R. W. Watson, and D. Bouchier-Hayes. "Role of lipopolysaccharide and tumor necrosis factor-alpha in induction of hepatocyte necrosis." American Journal of Physiology-Gastrointestinal and Liver Physiology 269, no. 2 (August 1, 1995): G297—G304. http://dx.doi.org/10.1152/ajpgi.1995.269.2.g297.

Full text

Abstract:

The occurrence of acute hepatic failure during systemic inflammatory response syndrome (SIRS) is related to the extent of hepatocyte (HC) damage and cell death resulting from necrosis or apoptosis. We hypothesized that proinflammatory mediators such as lipopolysaccharide (LPS) and tumor necrosis factor-alpha (TNF-alpha) can, either directly or indirectly through neutrophil (PMN) and Kupffer cell (KC) activation, induce HC damage and cell death, and that the mechanism is cellular necrosis rather than apoptosis. The results in this study demonstrated that LPS and TNF-alpha alone and in combination are directly cytotoxic to cultured rat HC as indicated by the hepatocellular enzyme release and HC necrosis. However, LPS and TNF-alpha, in the presence of sodium arsenite (a heat shock inducer), were unable to induce HC apoptosis. Both KC and PMN activated by either LPS or TNF-alpha induced significant hepatocellular enzyme release and HC necrosis, which was dependent on the ratio of KC and PMN to HC. It is concluded that LPS and TNF-alpha may play a central role in the development of acute hepatic failure after severe trauma and sepsis by directly or indirectly inducing HC necrosis rather than apoptosis.

APA, Harvard, Vancouver, ISO, and other styles

21

Herceg, Zdenko, and Zhao-Qi Wang. "Failure of Poly(ADP-Ribose) Polymerase Cleavage by Caspases Leads to Induction of Necrosis and Enhanced Apoptosis." Molecular and Cellular Biology 19, no. 7 (July 1, 1999): 5124–33. http://dx.doi.org/10.1128/mcb.19.7.5124.

Full text

Abstract:

ABSTRACT Activation of poly(ADP-ribose) polymerase (PARP) by DNA breaks catalyzes poly(ADP-ribosyl)ation and results in depletion of NAD+ and ATP, which is thought to induce necrosis. Proteolytic cleavage of PARP by caspases is a hallmark of apoptosis. To investigate whether PARP cleavage plays a role in apoptosis and in the decision of cells to undergo apoptosis or necrosis, we introduced a point mutation into the cleavage site (DEVD) of PARP that renders the protein resistant to caspase cleavage in vitro and in vivo. Here, we show that after treatment with tumor necrosis factor alpha, fibroblasts expressing this caspase-resistant PARP exhibited an accelerated cell death. This enhanced cell death is attributable to the induction of necrosis and an increased apoptosis and was coupled with depletion of NAD+ and ATP that occurred only in cells expressing caspase-resistant PARP. The PARP inhibitor 3-aminobenzamide prevented the NAD+ drop and concomitantly inhibited necrosis and the elevated apoptosis. These data indicate that this accelerated cell death is due to NAD+ depletion, a mechanism known to kill various cell types, caused by activation of uncleaved PARP after DNA fragmentation. The present study demonstrates that PARP cleavage prevents induction of necrosis during apoptosis and ensures appropriate execution of caspase-mediated programmed cell death.

APA, Harvard, Vancouver, ISO, and other styles

22

Tidball, J. G., D. E. Albrecht, B. E. Lokensgard, and M. J. Spencer. "Apoptosis precedes necrosis of dystrophin-deficient muscle." Journal of Cell Science 108, no. 6 (June 1, 1995): 2197–204. http://dx.doi.org/10.1242/jcs.108.6.2197.

Full text

Abstract:

The current view that death of dystrophin-deficient muscle fibers is a necrotic process relies primarily upon the histological appearance of the tissue after the degenerative process is well advanced. Here, we tested this view by examining the possibility that apoptosis is a component of dystrophin-deficient muscle cell death. Three assays for apoptosis were employed in analyzing prenecrotic, peak necrotic and regenerated hindlimb muscle of mdx mice: (1) terminal deoxynucleotidyl transferase (TdT) mediated end-labeling of DNA in nuclei in tissue sections; (2) assays for DNA ladders; and (3) electron microscopic assays for the presence of organelles undergoing structural changes characteristic of apoptosis. At all ages sampled, mdx muscle contained apoptotic nuclei, according to TdT-mediated dUTP labeling of tissue sections. Nuclei in regenerated mdx muscle fibers did not display apoptosis. dUTP-labeled nuclei in control C57 muscles were rare or absent at all ages sampled. DNA from 4-week-old mdx mice was found to be cleaved into fragments indicative of preferential cleavage at internucleosomal sites. Electron microscopic analysis showed that organelle structural changes indicating apoptosis appear before pathological changes diagnostic of necrosis. For example, condensed mitochondria, fragmented sarcoplasmic reticulum and nuclei with chromatin condensations resembling apoptosis appear in fibers that otherwise possess normal morphology. Together, the findings show that apoptosis precedes any detectable necrotic change in mdx muscle, and that apoptotic events continue into the stage of dystrophic pathology that is currently viewed as necrosis. Thus, apoptosis characterizes the onset of pathology in dystrophin-deficient muscle which is followed secondarily by necrotic processes.

APA, Harvard, Vancouver, ISO, and other styles

23

Brown, Guy C. "Mitochondria and cell death: Apoptosis and necrosis." Biochemist 27, no. 3 (June 1, 2005): 15–18. http://dx.doi.org/10.1042/bio02703015.

Full text

Abstract:

“To be, or not to be: that is the question:Whether ‘tis nobler in the mind to suffer The slings and arrows of outrageous fortune, Or to take arms against a sea of troubles,And by opposing end them? To die” William Shakespeare, Hamlet

APA, Harvard, Vancouver, ISO, and other styles

24

Davidovich, Pavel, Conor J. Kearney, and Seamus J. Martin. "Inflammatory outcomes of apoptosis, necrosis and necroptosis." Biological Chemistry 395, no. 10 (October 1, 2014): 1163–71. http://dx.doi.org/10.1515/hsz-2014-0164.

Full text

Abstract:

Abstract Microbial infection and tissue injury are well established as the two major drivers of inflammation. However, although it is widely accepted that necrotic cell death can trigger or potentiate inflammation, precisely how this is achieved still remains relatively obscure. Certain molecules, which have been dubbed ‘damage-associated molecular patterns’ (DAMPs) or alarmins, are thought to promote inflammation upon release from necrotic cells. However, the precise nature and relative potency of DAMPs, compared to conventional pro-inflammatory cytokines or pathogen-associated molecular patterns (PAMPs), remains unclear. How different modes of cell death impact on the immune system also requires further clarification. Apoptosis has long been regarded as a non-inflammatory or even anti-inflammatory mode of cell death, but recent studies suggest that this is not always the case. Necroptosis is a programmed form of necrosis that is engaged under certain conditions when caspase activation is blocked. Necroptosis is also regarded as a highly pro-inflammatory mode of cell death but there has been little explicit examination of this issue. Here we discuss the inflammatory implications of necrosis, necroptosis and apoptosis and some of the unresolved questions concerning how dead cells influence inflammatory responses.

APA, Harvard, Vancouver, ISO, and other styles

25

Kung, Gloria, Klitos Konstantinidis, and Richard N. Kitsis. "Programmed Necrosis, Not Apoptosis, in the Heart." Circulation Research 108, no. 8 (April 15, 2011): 1017–36. http://dx.doi.org/10.1161/circresaha.110.225730.

Full text

APA, Harvard, Vancouver, ISO, and other styles

26

OHSHIMA, S. "Apoptosis and Necrosis in Senescent Human Fibroblasts." Annals of the New York Academy of Sciences 1067, no. 1 (May 1, 2006): 228–34. http://dx.doi.org/10.1196/annals.1354.029.

Full text

APA, Harvard, Vancouver, ISO, and other styles

27

Watson, A. J. "Necrosis and apoptosis in the gastrointestinal tract." Gut 37, no. 2 (August 1, 1995): 165–67. http://dx.doi.org/10.1136/gut.37.2.165.

Full text

APA, Harvard, Vancouver, ISO, and other styles

28

Zamzami, N., N. Larochette, and G. Kroemer. "Mitochondrial permeability transition in apoptosis and necrosis." Cell Death & Differentiation 12, S2 (October 25, 2005): 1478–80. http://dx.doi.org/10.1038/sj.cdd.4401682.

Full text

APA, Harvard, Vancouver, ISO, and other styles

29

McHugh, Patrick, and Matthias Turina. "Apoptosis and Necrosis: A Review for Surgeons." Surgical Infections 7, no. 1 (February 2006): 53–68. http://dx.doi.org/10.1089/sur.2006.7.53.

Full text

APA, Harvard, Vancouver, ISO, and other styles

30

Hatano, Etsuro. "Tumor necrosis factor signaling in hepatocyte apoptosis." Journal of Gastroenterology and Hepatology 22, s1 (June 2007): S43—S44. http://dx.doi.org/10.1111/j.1440-1746.2006.04645.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

31

Lipton, Stuart A., and Pierluigi Nicotera. "■ REVIEW : Excitotoxicity, Free Radicals, Necrosis, and Apoptosis." Neuroscientist 4, no. 5 (September 1998): 345–52. http://dx.doi.org/10.1177/107385849800400516.

Full text

APA, Harvard, Vancouver, ISO, and other styles

32

Krysko, Dmitri V., Tom Vanden Berghe, Katharina D’Herde, and Peter Vandenabeele. "Apoptosis and necrosis: Detection, discrimination and phagocytosis." Methods 44, no. 3 (March 2008): 205–21. http://dx.doi.org/10.1016/j.ymeth.2007.12.001.

Full text

APA, Harvard, Vancouver, ISO, and other styles

33

Rollins, Shadon, Eddie Perkins, George Mandybur, and John H. Zhang. "Oxyhemoglobin produces necrosis, not apoptosis, in astrocytes." Brain Research 945, no. 1 (July 2002): 41–49. http://dx.doi.org/10.1016/s0006-8993(02)02562-3.

Full text

APA, Harvard, Vancouver, ISO, and other styles

34

Edinger, Aimee L., and Craig B. Thompson. "Death by design: apoptosis, necrosis and autophagy." Current Opinion in Cell Biology 16, no. 6 (December 2004): 663–69. http://dx.doi.org/10.1016/j.ceb.2004.09.011.

Full text

APA, Harvard, Vancouver, ISO, and other styles

35

Ludwig, Aaron T., Jill M. Moore, Yi Luo, Xiaohong Chen, Nicole A. Saltsgaver, Michael A. O’Donnell, and Thomas S. Griffith. "Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand." Cancer Research 64, no. 10 (May 15, 2004): 3386–90. http://dx.doi.org/10.1158/0008-5472.can-04-0374.

Full text

APA, Harvard, Vancouver, ISO, and other styles

36

Lachaud, C. "Apoptosis and necrosis in human ejaculated spermatozoa." Human Reproduction 19, no. 3 (January 29, 2004): 607–10. http://dx.doi.org/10.1093/humrep/deh130.

Full text

APA, Harvard, Vancouver, ISO, and other styles

37

Schulze- Osthoff, Klaus, and Heike Bantel. "Necrosis versus apoptosis in acetaminophen-induced hepatotoxicity." Hepatology 53, no. 3 (December 28, 2010): 1070. http://dx.doi.org/10.1002/hep.24027.

Full text

APA, Harvard, Vancouver, ISO, and other styles

38

Schobesberger, M., A. Zurbriggen, A. Summerfield, M. Vandevelde, and C. Griot. "Oligodendroglial degeneration in distemper: apoptosis or necrosis?" Acta Neuropathologica 97, no. 3 (March 8, 1999): 279–87. http://dx.doi.org/10.1007/s004010050986.

Full text

APA, Harvard, Vancouver, ISO, and other styles

39

Skulachev, V. P. "Bioenergetic aspects of apoptosis, necrosis and mitoptosis." Apoptosis 11, no. 4 (March 9, 2006): 473–85. http://dx.doi.org/10.1007/s10495-006-5881-9.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

Los, Marek, Malgorzata Mozoluk, Davide Ferrari, Anna Stepczynska, Christopher Stroh, Andrea Renz, Zdenko Herceg, Zhao-Qi Wang, and Klaus Schulze-Osthoff. "Activation and Caspase-mediated Inhibition of PARP: A Molecular Switch between Fibroblast Necrosis and Apoptosis in Death Receptor Signaling." Molecular Biology of the Cell 13, no. 3 (March 2002): 978–88. http://dx.doi.org/10.1091/mbc.01-05-0272.

Full text

Abstract:

Death ligands not only induce apoptosis but can also trigger necrosis with distinct biochemical and morphological features. We recently showed that in L929 cells CD95 ligation induces apoptosis, whereas TNF elicits necrosis. Treatment with anti-CD95 resulted in typical apoptosis characterized by caspase activation and DNA fragmentation. These events were barely induced by TNF, although TNF triggered cell death to a similar extent as CD95. Surprisingly, whereas the caspase inhibitor zVAD prevented CD95-mediated apoptosis, it potentiated TNF-induced necrosis. Cotreatment with TNF and zVAD was characterized by ATP depletion and accelerated necrosis. To investigate the mechanisms underlying TNF-induced cell death and its potentiation by zVAD, we examined the role of poly(ADP-ribose)polymerase-1 (PARP-1). TNF but not CD95 mediated PARP activation, whereas a PARP inhibitor suppressed TNF-induced necrosis and the sensitizing effect of zVAD. In addition, fibroblasts expressing a noncleavable PARP-1 mutant were more sensitive to TNF than wild-type cells. Our results indicate that TNF induces PARP activation leading to ATP depletion and subsequent necrosis. In contrast, in CD95-mediated apoptosis caspases cause PARP-1 cleavage and thereby maintain ATP levels. Because ATP is required for apoptosis, we suggest that PARP-1 cleavage functions as a molecular switch between apoptotic and necrotic modes of death receptor-induced cell death.

APA, Harvard, Vancouver, ISO, and other styles

41

Vanden Berghe, Tom, Michael Kalai, Geert van Loo, Wim Declercq, and Peter Vandenabeele. "Disruption of HSP90 Function Reverts Tumor Necrosis Factor-induced Necrosis to Apoptosis." Journal of Biological Chemistry 278, no. 8 (November 18, 2002): 5622–29. http://dx.doi.org/10.1074/jbc.m208925200.

Full text

APA, Harvard, Vancouver, ISO, and other styles

42

Troyano, Alfonso, Carlos Fernández, Patricia Sancho, Elena de Blas, and Patricio Aller. "Effect of Glutathione Depletion on Antitumor Drug Toxicity (Apoptosis and Necrosis) in U-937 Human Promonocytic Cells." Journal of Biological Chemistry 276, no. 50 (October 15, 2001): 47107–15. http://dx.doi.org/10.1074/jbc.m104516200.

Full text

Abstract:

Treatment with the DNA topoisomerase inhibitors etoposide, doxorubicin, and camptothecin, and with the alkylating agents cisplatin and melphalan, caused peroxide accumulation and apoptosis in U-937 human promonocytic cells. Preincubation with the reduced glutathione (GSH) synthesis inhibitorl-buthionine-(S,R)-sulfoximine (BSO) always potentiated peroxide accumulation. However, although GSH depletion potentiated the toxicity of cisplatin and melphalan, occasionally switching the mode of death from apoptosis to necrosis, it did not affect the toxicity of the other antitumor drugs. Hypoxia or preincubation with antioxidant agents attenuated death induction, apoptotic and necrotic, by alkylating drugs. The generation of necrosis by cisplatin could not be mimicked by addition of exogenous H2O2instead of BSO and was not adequately explained by caspase inactivation nor by a selective fall in ATP content. Treatment with cisplatin and melphalan caused a late decrease in mitochondrial transmembrane potential (ΔΨm), which was much greater during necrosis than during apoptosis. The administration of the antioxidant agentsN-acetyl-l-cysteine and butylated hydroxyanisole after pulse treatment with cisplatin or melphalan did not affect apoptosis but attenuated necrosis. Under these conditions, both antioxidants attenuated the necrosis-associated ΔΨm decrease. These results indicate that oxidation-mediated alterations in mitochondrial function regulate the selection between apoptosis and necrosis in alkylating drug-treated human promonocytic cells.

APA, Harvard, Vancouver, ISO, and other styles

43

Helm, Katharina, Marlena Beyreis, Christian Mayr, Markus Ritter, Martin Jakab, Tobias Kiesslich, and Kristjan Plaetzer. "In Vitro Cell Death Discrimination and Screening Method by Simple and Cost-Effective Viability Analysis." Cellular Physiology and Biochemistry 41, no. 3 (2017): 1011–19. http://dx.doi.org/10.1159/000460910.

Full text

Abstract:

Background/Aims: For in vitro cytotoxicity testing, discrimination of apoptosis and necrosis represents valuable information. Viability analysis performed at two different time points post treatment could serve such a purpose because the dynamics of metabolic activity of apoptotic and necrotic cells is different, i.e. a more rapid decline of cellular metabolism during necrosis whereas cellular metabolism is maintained during the entire execution phase of apoptosis. This study describes a straightforward approach to distinguish apoptosis and necrosis. Methods: A431 human epidermoid carcinoma cells were treated with different concentrations/doses of actinomycin D (Act-D), 4,5,6,7-tetrabromo-2-azabenzimidazole (TBB), Ro 31-8220, H2O2 and photodynamic treatment (PDT). The resazurin viability signal was recorded at 2 and 24 hrs post treatment. Apoptosis and necrosis were verified by measuring caspase 3/7 and membrane integrity. Results: Calculation of the difference curve between the 2 and 24 hrs resazurin signals yields the following information: a positive difference signal indicates apoptosis (i.e. high metabolic activity at early time points and low signal at 24 hrs post treatment) while an early reduction of the viability signal indicates necrosis. For all treatments, this dose-dependent sequence of cellular responses could be confirmed by independent assays. Conclusion: Simple and cost-effective viability analysis provides reliable information about the dose ranges of a cytotoxic agent where apoptosis or necrosis occurs. This may serve as a starting point for further in-depth characterisation of cytotoxic treatments.

APA, Harvard, Vancouver, ISO, and other styles

44

Vayssier, Muriel, Nathalie Banzet, Dominique François, Kerstin Bellmann, and Barbara S. Polla. "Tobacco smoke induces both apoptosis and necrosis in mammalian cells: differential effects of HSP70." American Journal of Physiology-Lung Cellular and Molecular Physiology 275, no. 4 (October 1, 1998): L771—L779. http://dx.doi.org/10.1152/ajplung.1998.275.4.l771.

Full text

Abstract:

Tobacco smoke (TS) has been implicated as a major risk factor in human pulmonary diseases including cancer. In this study, we used TS as a model of oxidative stress. TS-mediated oxidative stress has been shown to induce protein oxidation, DNA damage, and cell death. Here we investigated, in human and rodent cell lines, whether TS induces cell death by apoptosis or by necrosis. As described for classic oxidants, TS induced apoptosis at low concentrations and necrosis at higher concentrations. We have previously described the induction of heat shock (HS) protein (HSP) (in particular, HSP70) in human monocytes exposed to TS. HSP70 is implicated in the regulation of cell injury and cell death and, in particular, modulates apoptosis, as does the antiapoptotic oncoprotein Bcl-2. At both apoptotic and necrotic concentrations, TS induced a dose-dependent HSP70 expression, whereas Bcl-2 was induced only at necrotic concentrations. TS- or HS-induced HSP had no protective effects either on apoptosis or on necrosis, but HSP70 overexpression prevented TS-induced necrosis and consequently led to increased apoptosis. These results might reconcile the apparently contradictory data previously reported on the effects of HSP on apoptosis.

APA, Harvard, Vancouver, ISO, and other styles

45

Cao, Li-Li, and You-Ping Li. "Relationship between tumor necrosis factor related apoptosis induced ligand and hepatocyte apoptosis." World Chinese Journal of Digestology 16, no. 23 (2008): 2626. http://dx.doi.org/10.11569/wcjd.v16.i23.2626.

Full text

APA, Harvard, Vancouver, ISO, and other styles

46

Russo, Thomas A., Bruce A. Davidson, Stacy A. Genagon, Natalie M. Warholic, Ulrike MacDonald, Patrick D. Pawlicki, Janet M. Beanan, Ruth Olson, Bruce A. Holm, and Paul R. Knight. "E. colivirulence factor hemolysin induces neutrophil apoptosis and necrosis/lysis in vitro and necrosis/lysis and lung injury in a rat pneumonia model." American Journal of Physiology-Lung Cellular and Molecular Physiology 289, no. 2 (August 2005): L207—L216. http://dx.doi.org/10.1152/ajplung.00482.2004.

Full text

Abstract:

Enteric gram-negative bacilli, such as Escherichia coli are the most common cause of nosocomial pneumonia. In this study a wild-type extraintestinal pathogenic strain of E. coli (ExPEC)(CP9) and isogenic derivatives deficient in hemolysin (Hly) and cytotoxic necrotizing factor (CNF) were assessed in vitro and in a rat model of gram-negative pneumonia to test the hypothesis that these virulence factors induce neutrophil apoptosis and/or necrosis/lysis. As ascertained by in vitro caspase-3/7 and LDH activities and neutrophil morphology, Hly mediated neutrophil apoptosis at lower E. coli titers (1 × 105–6cfu) and necrosis/lysis at higher titers (≥1 × 107cfu). Data suggest that CNF promotes apoptosis but not necrosis or lysis. We also demonstrate that annexin V/7-amino-actinomycin D staining was an unreliable assessment of apoptosis using live E. coli. The use of caspase-3/7 and LDH activities and neutrophil morphology supported the notion that necrosis, not apoptosis, was the primary mechanism by which neutrophils were affected in our in vivo gram-negative pneumonia model using live E. coli. In addition, in vivo studies demonstrated that Hly mediates lung injury. Neutrophil necrosis was not observed when animals were challenged with purified lipopolysaccharide, demonstrating the importance of using live bacteria. These findings establish that Hly contributes to ExPEC virulence by mediating neutrophil toxicity, with necrosis/lysis being the dominant effect of Hly on neutrophils in vivo and by lung injury. Whether Hly-mediated lung injury is due to neutrophil necrosis, a direct effect of Hly, or both is unclear.

APA, Harvard, Vancouver, ISO, and other styles

47

Marshall, Kurt D., Michelle A. Edwards, Maike Krenz, J. Wade Davis, and Christopher P. Baines. "Proteomic mapping of proteins released during necrosis and apoptosis from cultured neonatal cardiac myocytes." American Journal of Physiology-Cell Physiology 306, no. 7 (April 1, 2014): C639—C647. http://dx.doi.org/10.1152/ajpcell.00167.2013.

Full text

Abstract:

Cardiac injury induces myocyte apoptosis and necrosis, resulting in the secretion and/or release of intracellular proteins. Currently, myocardial injury can be detected by analysis of a limited number of biomarkers in blood or coronary artery perfusate. However, the complete proteomic signature of protein release from necrotic cardiac myocytes is unknown. Therefore, we undertook a proteomic-based study of proteins released from cultured neonatal rat cardiac myocytes in response to H2O2 (necrosis) or staurosporine (apoptosis) to identify novel specific markers of cardiac myocyte cell death. Necrosis and apoptosis resulted in the identification of 147 and 79 proteins, respectively. Necrosis resulted in a relative increase in the amount of many proteins including the classical necrotic markers lactate dehydrogenase (LDH), high-mobility group B1 (HMGB1), myoglobin, enolase, and 14-3-3 proteins. Additionally, we identified several novel markers of necrosis including HSP90, α-actinin, and Trim72, many of which were elevated over control levels earlier than classical markers of necrotic injury. In contrast, the majority of identified proteins remained at low levels during apoptotic cell death, resulting in no candidate markers for apoptosis being identified. Blotting for a selection of these proteins confirmed their release during necrosis but not apoptosis. We were able to confirm the presence of classical necrotic markers in the extracellular milieu of necrotic myocytes. We also were able to identify novel markers of necrotic cell death with relatively early release profiles compared with classical protein markers of necrosis. These results have implications for the discovery of novel biomarkers of necrotic myocyte injury, especially in the context of ischemia-reperfusion injury.

APA, Harvard, Vancouver, ISO, and other styles

48

Louis, JC, E. Magal, S. Takayama, and S. Varon. "CNTF protection of oligodendrocytes against natural and tumor necrosis factor-induced death." Science 259, no. 5095 (January 29, 1993): 689–92. http://dx.doi.org/10.1126/science.8430320.

Full text

Abstract:

A proportion of developing oligodendrocytes undergo natural cell death by apoptosis, and mature oligodendrocytes die, either by apoptosis or necrosis, in response to injurious signals such as cytotoxic cytokines and complement. Ciliary neurotrophic factor (CNTF), a trophic factor found in astrocytes in the central nervous system (CNS), promoted the survival and maturation of cultured oligodendrocytes. This trophic factor also protected oligodendrocytes from death induced by tumor necrosis factors (apoptosis) but not against complement (necrosis). These results suggest that CNTF functions in the survival of oligodendrocytes during development and may lead to therapeutic approaches for degenerative diseases of the CNS that involve oligodendrocyte destruction.

APA, Harvard, Vancouver, ISO, and other styles

49

Jaeschke, Hartmut, Michael A. Fisher, Judy A. Lawson, Carol A. Simmons, Anwar Farhood, and David A. Jones. "Activation of Caspase 3 (CPP32)-Like Proteases Is Essential for TNF-α-Induced Hepatic Parenchymal Cell Apoptosis and Neutrophil-Mediated Necrosis in a Murine Endotoxin Shock Model." Journal of Immunology 160, no. 7 (April 1, 1998): 3480–86. http://dx.doi.org/10.4049/jimmunol.160.7.3480.

Full text

Abstract:

Abstract Endotoxin (ET)-induced liver failure is characterized by parenchymal cell apoptosis and inflammation leading to liver cell necrosis. Members of the caspase family have been implicated in the signal transduction pathway of apoptosis. The aim of this study was to characterize ET-induced hepatic caspase activation and apoptosis and to investigate their effect on neutrophil-mediated liver injury. Treatment of C3Heb/FeJ mice with 700 mg/kg galactosamine (Gal) and 100 μg/kg Salmonella abortus equi ET increased caspase 3-like protease activity (Asp-Val-Glu-Asp-substrate) by 1730 ± 140% at 6 h. There was a parallel enhancement of apoptosis (assessed by DNA fragmentation ELISA and terminal deoxynucleotidyl transferase-mediated dUTP nick end labeling assay). In contrast, activity of caspase 1 (IL-1β-converting enzyme)-like proteases (Tyr-Val-Ala-Asp-substrate) did not change throughout the experiment. Caspase 3-like protease activity and apoptosis was not induced by Gal/ET in ET-resistant mice (C3H/HeJ). Furthermore, only murine TNF-α but not IL-1αβ increased caspase activity and apoptosis. Gal/ET caused neutrophil-dependent hepatocellular necrosis at 7 h (area of necrosis, 45 ± 3%). Delayed treatment with the caspase 3-like protease inhibitor Z-Val-Ala-Asp-CH2F (Z-VAD) (10 mg/kg at 3 h) attenuated apoptosis by 81 to 88% and prevented liver cell necrosis (≤5%). Z-VAD had no effect on the initial inflammatory response, including the sequestration of neutrophils in sinusoids. However, Z-VAD prevented neutrophil transmigration and necrosis. Our data indicate that activation of the caspase 3 subfamily of cysteine proteases is critical for the development of parenchymal cell apoptosis. In addition, excessive hepatocellular apoptosis can be an important signal for transmigration of primed neutrophils sequestered in sinusoids.

APA, Harvard, Vancouver, ISO, and other styles

50

Yang, Kun-Han, Jen-Yang Tang, Yan-Ning Chen, Ya-Ting Chuang, I.-Hsuan Tsai, Chien-Chih Chiu, Li-Jie Li, et al. "Nepenthes Extract Induces Selective Killing, Necrosis, and Apoptosis in Oral Cancer Cells." Journal of Personalized Medicine 11, no. 9 (August 31, 2021): 871. http://dx.doi.org/10.3390/jpm11090871.

Full text

Abstract:

Ethyl acetate Nepenthes extract (EANT) from Nepenthes thorellii × (ventricosa × maxima) shows antiproliferation and apoptosis but not necrosis in breast cancer cells, but this has not been investigated in oral cancer cells. In the present study, EANT shows no cytotoxicity to normal oral cells but exhibits selective killing to six oral cancer cell lines. They were suppressed by pretreatment of the antioxidant inhibitor N-acetylcysteine (NAC), demonstrating that EANT-induced cell death was mediated by oxidative stress. Concerning high sensitivity to EANT, Ca9-22 and CAL 27 oral cancer cells were chosen for exploring detailed selective killing mechanisms. EANT triggers a mixture of necrosis and apoptosis as determined by annexin V/7-aminoactinmycin D analysis. Still, they show differential switches from necrosis at a low (10 μg/mL) concentration to apoptosis at high (25 μg/mL) concentration of EANT in oral cancer cells. NAC induces necrosis but suppresses annexin V-detected apoptosis in oral cancer cells. Necrostatin 1 (NEC1), a necroptosis inhibitor, moderately suppresses necrosis but induces apoptosis at 10 μg/mL EANT. In contrast, Z-VAD-FMK, a pancaspase inhibitor, slightly causes necrosis but suppresses apoptosis at 10 μg/mL EANT. Furthermore, the flow cytometry-detected pancaspase activity is dose-responsively increased but is suppressed by NAC and ZVAD, although not for NEC1 in oral cancer cells. EANT causes several oxidative stress events such as reactive oxygen species, mitochondrial superoxide, and mitochondrial membrane depolarization. In response to oxidative stresses, the mRNA for antioxidant signaling, such as nuclear factor erythroid 2-like 2 (NFE2L2), catalase (CAT), heme oxygenase 1 (HMOX1), and thioredoxin (TXN), are overexpressed in oral cancer cells. Moreover, EANT also triggers DNA damage, as detected by γH2AX and 8-oxo-2′-deoxyguanosine adducts. The dependence of oxidative stress is validated by the evidence that NAC pretreatment reverts the changes of cellular and mitochondrial stress and DNA damage. Therefore, EANT exhibits antiproliferation involving an oxidative stress-dependent necrosis/apoptosis switch and DNA damage in oral cancer cells.

APA, Harvard, Vancouver, ISO, and other styles

Journal articles on the topic 'Apoptosis/Necrosis'

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles