Caspase and calpain function in cell death: bridging the gap between apoptosis and necrosis
- BiologyAnnals of clinical biochemistry
An assessment of the contribution that caspase and calpain make to human physiology and pathology is provided, with a description of how these proteases can be detected and quantified.
Cleaved Fragments Prediction Algorithm (CFPA) application to calpain and caspase in apoptosis and necrotic cell death
- Biology2015 IEEE International Conference on Electro/Information Technology (EIT)
The main purpose of this work is to establish a new efficient and accurate methodological tool based on dynamic programming to predict those BDPs computationally with an algorithm of space complexity O (mn) and time complexity O(NN'mn), where the comprised parameters correspond to number of protein sequences, number of consensus sequences, length of each protein sequence, and length ofEach consensus sequence, respectively.
Calpain Facilitates the Neuron Death Induced by 3‐Nitropropionic Acid and Contributes to the Necrotic Morphology
- Biology, ChemistryJournal of neuropathology and experimental neurology
Results indicate that following 3NP administration, increased calpain activity precedes caspase-3 activation, contributes to the necrotic morphology, and facilitates and accelerates the cell death.
Implication of calpain in neuronal apoptosis
- BiologyThe FEBS journal
The understanding of calpain‐dependent apoptotic neuronal cell death and the ability of these proteases to regulate intracellular signaling pathways leading to chronic neurodegenerative disorders such as Alzheimer's disease are reviewed.
Calpain activates caspase‐3 during UV‐induced neuronal death but only calpain is necessary for death
- Biology, ChemistryJournal of neurochemistry
It is suggested that UV neurotoxicity is mediated by a loss of Ca2+ homeostasis which leads to a calpain‐dependent, caspase‐independent cell death, which may have relevance to other neuronal death models.
Involvement of caspases and calpains in cerebrocortical neuronal cell death is stimulus‐dependent
- Biology, ChemistryBritish journal of pharmacology
The existence of stimulus‐dependent routes for the activation of caspases and calpains during death of cortical neurones is suggested and implies that although caspase and calPains are activated, their involvement in the execution of cell death varies with the stimulus.
Concurrent Assessment of Calpain and Caspase-3 Activation after Oxygen–Glucose Deprivation in Primary Septo-Hippocampal Cultures
- BiologyJournal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism
Calpain activation is associated with expression of apoptotic cell death phenotypes after OGD, and calpain activation, in combination with caspase-3 activation, could contribute to the expression of suicide cell death by assisting in the degradation of important cellular proteins.
Inhibition of caspases but not of calpains temporarily protect against C2-ceramide-induced death of CAD cells
- BiologyNeuroscience Letters
Multiple alphaII-spectrin breakdown products distinguish calpain and caspase dominated necrotic and apoptotic cell death pathways
- Biology, ChemistryApoptosis
These results suggested calpains and caspases which dominate the two major types of cell death could be independently discriminated by specifically examining the multiple αII-spectrin cleavage breakdown products.
Apoptotic and necrotic cell death induced by death domain receptors
- BiologyCellular and Molecular Life Sciences CMLS
What is known about the apoptotic and necrotic cell death pathways is described, including principal elements of necrosis include mitochondrial oxidative phosphorylation, reactive oxygen production, and non-caspase proteolytic cascades depending on serine proteases, calpains, or cathepsins.
SHOWING 1-10 OF 83 REFERENCES
Effects of ICE‐like protease and calpain inhibitors on neuronal apoptosis
- Biology, ChemistryNeuroreport
The results suggest that ICE-like protease plays a critical role in neuronal apoptosis whereas the contributions of calpain are more cell-type dependent.
Cleavage of the calpain inhibitor, calpastatin, during apoptosis
- Biology, ChemistryCell Death and Differentiation
The results of the present study suggest that caspases may cleave calpastatin and thus, regulate calpain activity during apoptotic cell death.
Caspase-mediated fragmentation of calpain inhibitor protein calpastatin during apoptosis.
- Biology, ChemistryArchives of biochemistry and biophysics
It is reported that the endogenous calpain inhibitor calpastatin is fragmented by caspase(s) to various extents during early apoptosis in two cell types and proposed that the proteolysis of calpastatins might have yet unidentified effects on the cross-talk between the two protease systems.
Constitutive Apoptosis in Human Neutrophils Requires Synergy between Calpains and the Proteasome Downstream of Caspases*
- BiologyThe Journal of Biological Chemistry
It is provided evidence that calpains and the proteasome function synergistically downstream of caspases to assist the constitutive apoptotic program of aging neutrophils, which plays an important role in resolution of inflammatory responses.
Mechanisms of Cell Death Induced by the Mitochondrial Toxin 3-Nitropropionic Acid: Acute Excitotoxic Necrosis and Delayed Apoptosis
- BiologyThe Journal of Neuroscience
It is concluded that 3-NP triggers two separate cell death pathways: an excitotoxic necrosis as a result of NMDA receptor activation and a delayed apoptosis that isNMDA receptor-independent.
Activation of the CED3/ICE-Related Protease CPP32 in Cerebellar Granule Neurons Undergoing Apoptosis But Not Necrosis
- BiologyThe Journal of Neuroscience
Results demonstrate that the CED3/ICE homolog CPP32 is processed and activated during cerebellar granule neuron apoptosis, and suggests that proteolytic processing and activation of CED 3/ICE proteases are specific biochemical markers of apoptosis.
Conversion of Bcl-2 to a Bax-like death effector by caspases.
Inhibitor studies indicated that cleavage of Bcl-2 may further activate downstream caspases and contribute to amplification of the caspase cascade, and Cleavage-resistant mutants of B cl-2 had increased protection from interleukin-3 withdrawal and Sindbis virus-induced apoptosis.
Calpain activation in apoptosis
- Biology, ChemistryJournal of cellular physiology
A required role for calpain is suggested in both “induction” and “release” models of apoptotic cell death, and it is found that apoptosis in thymocytes, whether induced by dexamethasone or by low‐level irradiation, is blocked by specific inhibitors of calpain.
Bax cleavage is mediated by calpain during drug-induced apoptosis
- Biology, ChemistryOncogene
The results suggest that calpains and caspases are activated during drug-induced apoptosis and thatCalpains, along with caspase, may be involved in modulating cell death by acting selectively on cellular substrates.
Caspase-3 Is Required for α-Fodrin Cleavage but Dispensable for Cleavage of Other Death Substrates in Apoptosis*
- Biology, ChemistryThe Journal of Biological Chemistry
It is suggested that caspase-3 is essential for cleavage of α-fodrin, but dispensable for the cleaved of PARP, Rb, PAK2, DNA-PKcs, gelsolin, and DFF-45 and imply that one or more caspases other than caspasing 2, 3, and 7 is activated and plays a crucial role in the cleaving of these substrates in MCF-7 cells.