Caspase activation pathways induced by staurosporine and low potassium: Role of caspase-2

2002 ◽  
Vol 71 (3) ◽  
pp. 383-396 ◽  
Author(s):  
Andrea Caballero-Benítez ◽  
Julio Morán
Keyword(s):  
Caspase Activation ◽  
Low Potassium ◽  
Caspase 2 ◽  
Activation Pathways

scholarly journals Inflammasome activation and IL-1 signaling during placental malaria induce poor pregnancy outcomes

2020 ◽  
Vol 6 (10) ◽  
pp. eaax6346 ◽  
Author(s):  
Aramys S. Reis ◽  
Renato Barboza ◽  
Oscar Murillo ◽  
André Barateiro ◽  
Erika P. M. Peixoto ◽  
...  
Keyword(s):  
Pregnancy Outcomes ◽  
Intrauterine Growth Restriction ◽  
Malaria Infection ◽  
Placental Malaria ◽  
Inflammasome Activation ◽  
Genetic Dissection ◽  
Intrauterine Growth ◽  
Activation Pathways ◽  
Nlrp3 Inflammasomes

Placental malaria (PM) is associated with severe inflammation leading to abortion, preterm delivery, and intrauterine growth restriction. Innate immunity responses play critical roles, but the mechanisms underlying placental immunopathology are still unclear. Here, we investigated the role of inflammasome activation in PM by scrutinizing human placenta samples from an endemic area and ablating inflammasome components in a PM mouse model. The reduction in birth weight in babies from infected mothers is paralleled by increased placental expression of AIM2 and NLRP3 inflammasomes. Using genetic dissection, we reveal that inflammasome activation pathways are involved in the production and detrimental action of interleukin-1β (IL-1β) in the infected placenta. The IL-1R pharmacological antagonist Anakinra improved pregnancy outcomes by restoring fetal growth and reducing resorption in an experimental model. These findings unveil that IL-1β–mediated signaling is a determinant of PM pathogenesis, suggesting that IL-1R antagonists can improve clinical outcomes of malaria infection in pregnancy.

Abstract A24: Biomarker analysis and the role of caspase-2 in apoptotic signaling in AML cells.

2011 ◽  
Author(s):  
Petra Haag ◽  
Marita Lagergren Lindberg ◽  
Lena Kanter ◽  
Rolf Lewensohn ◽  
Leif Stenke ◽  
...  
Keyword(s):  
Apoptotic Signaling ◽  
Biomarker Analysis ◽  
Caspase 2

Abstract 4090: The role of caspase-2 in apoptotic signaling in AML cells

2011 ◽  
Author(s):  
Petra Haag ◽  
Marita Lagergren Lindberg ◽  
Lena Kanter ◽  
Leif Stenke ◽  
Rolf Lewensohn ◽  
...  
Keyword(s):  
Apoptotic Signaling ◽  
Caspase 2

scholarly journals The role of cytochrome c in caspase activation in Drosophila melanogaster cells

2002 ◽  
Vol 156 (6) ◽  
pp. 1089-1098 ◽  
Author(s):  
Loretta Dorstyn ◽  
Stuart Read ◽  
Dimitrios Cakouros ◽  
Jun R. Huh ◽  
Bruce A. Hay ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Mammalian Cells ◽  
Significant Proportion ◽  
Ectopic Expression ◽  
Caspase Activation ◽  
Cytochrome C Release ◽  
Cell Extracts ◽  
Effector Caspase ◽  
Drosophila Cells

The release of cytochrome c from mitochondria is necessary for the formation of the Apaf-1 apoptosome and subsequent activation of caspase-9 in mammalian cells. However, the role of cytochrome c in caspase activation in Drosophila cells is not well understood. We demonstrate here that cytochrome c remains associated with mitochondria during apoptosis of Drosophila cells and that the initiator caspase DRONC and effector caspase DRICE are activated after various death stimuli without any significant release of cytochrome c in the cytosol. Ectopic expression of the proapoptotic Bcl-2 protein, DEBCL, also fails to show any cytochrome c release from mitochondria. A significant proportion of cellular DRONC and DRICE appears to localize near mitochondria, suggesting that an apoptosome may form in the vicinity of mitochondria in the absence of cytochrome c release. In vitro, DRONC was recruited to a >700-kD complex, similar to the mammalian apoptosome in cell extracts supplemented with cytochrome c and dATP. These results suggest that caspase activation in insects follows a more primitive mechanism that may be the precursor to the caspase activation pathways in mammals.

Plasma Protein Concentrations of Complement Components C4 and C3 Are Inversely Associated with Anticardiolipin Antibodies in APS Patients.

Blood ◽  
2005 ◽  
Vol 106 (11) ◽  
pp. 2645-2645
Author(s):  
Stephanie L. Savelli ◽  
Robert A.S. Roubey ◽  
Gail S. Buxton ◽  
Yan Yang ◽  
Yeeling Wu ◽  
...  
Keyword(s):  
Antiphospholipid Syndrome ◽  
Lupus Erythematosus ◽  
Anticardiolipin Antibodies ◽  
Plasma Samples ◽  
Complement Components ◽  
Protein Levels ◽  
Patient Groups ◽  
The Mean ◽  
Activation Pathways

Abstract Recently, it has been shown that injection of human antiphospholipid antibodies (aPL) into pregnant mice resulted in fetal resorption and complement proteins were implicated in the pathophysiologic process of the antiphospholipid syndrome (APS). Studies have been unable to determine definitively which complement components are responsible for the human disease. A significant number of systemic lupus erythematosus (SLE) patients have elevated titers of aPL and lupus anticoagulants. Homozygous and heterozygous deficiencies of complement C4A are known risk factors for the development of SLE. Complement C4 is a subunit protein of the C3 and C5 convertases for the classical and lectin activation pathways. C4A is the acidic isotype involved in immunoclearance and immunotolerance whereas C4B, the basic isotype, is important in the propagation of the complement activation pathways. To investigate the possible role of C4 in APS, we examined the phenotypic diversities of C4A and C4B as well as the plasma C4 and C3 protein concentrations. Peripheral blood plasma samples and genomic DNAs were provided by the Antiphospholipid Syndrome Collaborative Registry (APSCORE). Two patient groups were studied: (1) patients with definite APS as defined by the Sapporo criteria (APS) and (2) patients with elevated aPL without clinical sequelae (asymptomatic aPL). The APS group consisted of 184 patients. The mean age was 44 ±13 years. Among them 79% were female and 84% were Caucasian. The asymptomatic aPL group included 166 subjects. The mean age was 43 ± 13 years. Among them 87% were female and 78% were Caucasian. Complement C4A and C4B protein polymorphisms were determined by immunofixation of plasma samples. Plasma C3 and C4 protein concentrations were determined by single radial immunoassays. Factors known to have an effect on plasma C4 levels including body mass index (BMI), race and gender, were also examined by regression analyses. When compared to sex and race-matched normal controls, we found that total C4, C4A and C4B protein levels are significantly lower in the patient study populations (p<0.001). The lowest total C4 levels were observed in the asymptomatic aPL group that has a mean total C4 level of 16.5 mg/dL, compared to 31.2 mg/dL and 23 mg/dL in the control and APS groups, respectively. C4A and C4B levels were also lowest in the asymptomatic aPL subjects. C3 protein levels are positively associated with C4 in both APS and asymptomatic aPL groups (p<0.001); the strongest association was noted in the asymptomatic aPL group (R2=0.324). Anticardiolipin (ACLA) IgM is inversely associated with C4 concentrations in both APS (p=0.006) and asymptomatic aPL (p=0.015). The asymptomatic aPL subjects also showed an association of higher ACLA IgG titers with lower C3 concentrations (p=0.008). We also found that both APS and asymptomatic aPL have higher BMI (APS: 28.6 ± 6.8; asymptomatic aPL: 28.1 ± 6.1; controls: 25.6.± 5.8). Our results underscore an important role of C4 and C3 in human APS. We are currently determining C4A and C4B polygenic variations in these patient groups. The ultimate goal is to elucidate the intricate relationships among APS, asymptomatic aPL, SLE and low plasma levels of total C4, C4A and C4B.

Caspases: cellular demolition experts

2001 ◽  
Vol 29 (6) ◽  
pp. 696-702 ◽  
Author(s):  
E. M. Creagh ◽  
S. J. Martin
Keyword(s):  
Cytochrome C ◽  
Limited Proteolysis ◽  
Cysteine Proteases ◽  
Caspase Activation ◽  
Caspase Family ◽  
Hierarchical Nature ◽  
Caspase Cascade ◽  
Cellular Stresses ◽  
Pro Inflammatory Cytokines

Apoptosis is co-ordinated by a family of cysteine proteases, the caspases, that dismantle the cell by targeting a panoply of proteins for limited proteolysis. The mammalian caspase family contains 14 members, a subset of which participates in apoptosis, with the remainder likely to be involved in the processing of pro-inflammatory cytokines. Apical caspase activation events are typically initiated by adaptor molecules that promote caspase aggregation and facilitate caspase auto-activation. In contrast, distal caspase activation events are controlled by caspases activated earlier in the cascade. Many cellular stresses provoke apoptosis by damaging mitochondria which results in the release of factors [such as cytochrome c and SMAC (second mitochondrial-derived activator of caspase)/Diablo] that trigger caspase activation and cell death. Here, we discuss the hierarchical nature of the caspase cascade that is triggered upon the release of mitochondrial cytochrome c into the cytoplasm, and the role of specific caspases within this cascade in targeting proteins for degradation. Finally, feedback amplification loops and important control points within the caspase cascade will be discussed.

Role of the spleen in congenital stomatocytosis associated with high sodium low potassium erythrocytes

1981 ◽  
Vol 59 (4) ◽  
pp. 173-179 ◽  
Author(s):  
W. Schr�ter ◽  
K. Ungefehr ◽  
W. Tillmann
Keyword(s):  
High Sodium ◽  
Low Potassium
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