scholarly journals Determining the contributions of caspase-2, caspase-8 and effector caspases to intracellular VDVADase activities during apoptosis initiation and execution

2013 ◽  
Vol 1833 (10) ◽  
pp. 2279-2292 ◽  
Author(s):  
M. Eugenia Delgado ◽  
Magnus Olsson ◽  
Frank A. Lincoln ◽  
Boris Zhivotovsky ◽  
Markus Rehm
Keyword(s):  
Caspase 8 ◽  
Effector Caspases ◽  
Caspase 2 ◽  
Apoptosis Initiation

Caspase-2 is activated at the CD95 death-inducing signaling complex in the course of CD95-induced apoptosis

Blood ◽  
2006 ◽  
Vol 108 (2) ◽  
pp. 559-565 ◽  
Author(s):  
Inna N. Lavrik ◽  
Alexander Golks ◽  
Simone Baumann ◽  
Peter H. Krammer
Keyword(s):  
B Cell ◽  
Molecular Mechanism ◽  
Cell Lines ◽  
Caspase 8 ◽  
Signaling Complex ◽  
Deficient Cell ◽  
Apoptotic Pathways ◽  
Caspase 2 ◽  
Induced Apoptosis

Caspase-2 was reported to be involved in a number of apoptotic pathways triggered by various stimuli. However, the molecular mechanism of procaspase-2 activation in the course of apoptosis remains poorly defined. In this report, we demonstrate that procaspase-2 is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex (DISC) in human T- and B-cell lines. We show that procaspase-2 is activated at the DISC on CD95 stimulation. Despite its presence at the DISC, caspase-2 does not initiate apoptosis on CD95 stimulation in caspase-8–deficient cell lines. Taken together, our data reveal that caspase-2 is activated at the DISC but does not play an initiating role in the CD95-induced apoptosis.

scholarly journals Effect of glyprolines on serum caspase levels under “social” stress

2021 ◽  
Vol 24 (2) ◽  
pp. 46-52
Author(s):  
Anna L. Yasenyavskaya ◽  
Alexandra A. Tsibizova ◽  
Lyudmila A. Andreeva ◽  
Nikolay F. Myasoedov ◽  
Olga A. Bashkina ◽  
...  
Keyword(s):  
Blood Serum ◽  
Social Stress ◽  
Caspase 3 ◽  
Male Rats ◽  
Laboratory Animals ◽  
Caspase 8 ◽  
Elisa Kit ◽  
White Rats ◽  
Effector Caspases ◽  
Adhesive Proteins

Objective. To investigate the effect of glyprolines on the levels of initiating and effector caspases in the serum of white rats under "social" stress. Materials and methods. The study was conducted on 90 white male rats of 6 months of age. All manipulations with animals were carried out in accordance with international and domestic requirements for working with laboratory animals. When modeling "social" stress, groups of animals with aggressive and submissive behavior were formed. Laboratory animals, taking into account the types of behavior, were divided into groups (n=10): a group of intact males (control); a group of animals exposed to" social " stress for 20 days (stress); groups of individuals who received intraperitoneal Selank (Thr-Lys-Pro-Arg-Pro-Gly-Pro), Pro-Gly-Pro, Pro-Gly-Pro-Leu at doses of 100 mcg/kg / day from the 1st day of stress exposure within a 20- day course. The effect of neuropeptides on the activity of apoptosis processes was evaluated by determining the level of initiating and effector caspases (caspase-8 and caspase-3) (ELISA Kit for Caspase-8 and ELISA Kit for Caspase-3; USA) in the blood serum of white rats by enzyme immunoassay. Results. According to the results of the study, it was found that under conditions of "social" stress, an increase in apoptotic processes was observed, accompanied by an increase in the level of caspase-3 and caspase-8 in the blood serum of white rats. The introduction of the studied compounds against the background of stress contributed to a decrease in the level of the studied indicators, which is most likely due to the presence of antiapoptotic action in glyprolins due to inhibition of the caspase-dependent cascade of apoptosis reactions, as a result of which the destruction of cellular structures occurs by hydrolysis of nuclear lamina, cleavage of adhesive proteins, destruction of the cytoskeleton. Conclusion. Thus, the conducted study established the presence of Thr-Lys-Pro-Arg-Pro-Gly-Pro (Selank), Pro-Gly-Pro and Pro-Gly-Pro-Leu under conditions of stress-induced antiapoptotic activity due to inhibition of the caspase-dependent cascade of apoptosis reactions.

scholarly journals Coupling Activation of Pro-Apoptotic Caspases With Autophagy in the Meckel´s Cartilage

2018 ◽  
pp. 135-140 ◽  
Author(s):  
P. Bíliková ◽  
E. Švandová ◽  
B. Veselá ◽  
J. Doubek ◽  
A. Poliard ◽  
...  
Keyword(s):  
Caspase 3 ◽  
Beclin 1 ◽  
Hypertrophic Chondrocytes ◽  
Caspase 8 ◽  
Major Mechanism ◽  
Histological Sections ◽  
Temporary Structure ◽  
Caspase 2 ◽  
First Time

Mammalian Meckel´s cartilage is a temporary structure associated with mandible development. Notably, its elimination is not executed by apoptosis, and autophagy was suggested as the major mechanism. Simultaneous reports point to pro-apoptotic caspases as novel participants in autophagic pathways in general. The aim of this research was to find out whether activation of pro-apoptotic caspases (-2, -3, -6, -7, -8 and -9) was associated with autophagy of the Meckel´s cartilage chondrocytes. Active caspases were examined in serial histological sections of mouse mandible using immunodetection and were correlated with incidence of autophagy based on Beclin-1 expression. Caspase-2 and caspase-8 were found in Beclin-1 positive regions, whereas caspase-3, -6, -7 and -9 were not present. Caspase-8 was further correlated with Fas/FasL and HIF-1alpha, potential triggers for its activation. Some Fas and FasL positivity was observed in the chondrocytes but caspase-8 activation was found also in FasL deficient cartilage. HIF-1alpha was abundantly present in the hypertrophic chondrocytes. Taken together, caspase-8 activation in the Meckel´s cartilage was demonstrated for the first time. Caspase-8 and caspase-2 were the only pro-apoptotic caspases detected in the Beclin-1 positive segment of the cartilage. Activation of caspase-8 appears FasL/Fas independent but may be switched on by HIF-1alpha.

scholarly journals Bcl-2–regulated apoptosis and cytochrome c release can occur independently of both caspase-2 and caspase-9

2004 ◽  
Vol 165 (6) ◽  
pp. 775-780 ◽  
Author(s):  
Vanessa S. Marsden ◽  
Paul G. Ekert ◽  
Mark Van Delft ◽  
David L. Vaux ◽  
Jerry M. Adams ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Embryonic Brain ◽  
Caspase 9 ◽  
Cytochrome C Release ◽  
Hematopoietic Development ◽  
Adult Mice ◽  
Perinatal Lethality ◽  
Caspase 2 ◽  
Apoptosis Initiation ◽  
Redundant Role

Apoptosis in response to developmental cues and stress stimuli is mediated by caspases that are regulated by the Bcl-2 protein family. Although caspases 2 and 9 have each been proposed as the apical caspase in that pathway, neither is indispensable for the apoptosis of leukocytes or fibroblasts. To investigate whether these caspases share a redundant role in apoptosis initiation, we generated caspase-2−/−9−/− mice. Their overt phenotype, embryonic brain malformation and perinatal lethality mirrored that of caspase-9−/− mice but were not exacerbated. Analysis of adult mice reconstituted with caspase-2−/−9−/− hematopoietic cells revealed that the absence of both caspases did not influence hematopoietic development. Furthermore, lymphocytes and fibroblasts lacking both remained sensitive to diverse apoptotic stimuli. Dying caspase-2−/−9−/− lymphocytes displayed multiple hallmarks of caspase-dependent apoptosis, including the release of cytochrome c from mitochondria, and their demise was antagonized by several caspase inhibitors. These findings suggest that caspases other than caspases 2 and 9 can promote cytochrome c release and initiate Bcl-2–regulated apoptosis.

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