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  • 1
    Electronic Resource
    Electronic Resource
    Humanin peptide suppresses apoptosis by interfering with Bax activation (2003)
    [s.l.] : Macmillian Magazines Ltd.
    Nature 423 (2003), S. 456-461 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Bax (Bcl2-associated X protein) is an apoptosis-inducing protein that participates in cell death during normal development and in various diseases. Bax resides in an inactive state in the cytosol of many cells. In response to death stimuli, Bax protein undergoes conformational changes that ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature01627
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  • 2
    Electronic Resource
    Electronic Resource
    Double identity for proteins of the Bcl-2 family (1997)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 387 (1997), S. 773-776 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Bcl-2 is an oncogenic protein that acts by inhibiting programmed cell death. The mechanisms used by this and related anti-apoptotic proteins to protect cells from cytotoxic stimuli are now emerging, with the discovery that Bcl-2 can function both as an ion channel and as an adaptor or docking ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/387773a0
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  • 3
    Electronic Resource
    Electronic Resource
    Correlation Between Structure of Bcl-2 and Its Inhibitory Function of JNK and Caspase Activity in Dopaminergic Neuronal Apoptosis (2000)
    Oxford UK : Blackwell Science Ltd.
    Journal of neurochemistry 74 (2000), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: To examine the correlation between the structure of Bcl-2and its inhibitory function of c-Jun N-terminal kinase (JNK) and caspaseactivity, we established a dopaminergic neuronal cell line, MN9Doverexpressing Bcl-2 (MN9D/Bcl-2) or its structural mutants. The mutantscomprised a point mutation in the BH1 (G145A; MN9D/BH1) or BH2 (W188A;MN9D/BH2) domain and a deletion mutation in the C-terminal (MN9D/C22), BH3(MN9D/BH3), or BH4 (MN9D/BH4) domain. As determined by the TUNEL (terminaldeoxynucleotidyltransferase nick end-labeling) and MTT[3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide] reductionassay, apoptotic death of MN9D/Neo cells reached 80-90% within 24 h inresponse to 1 μM staurosporine. Upon staurosporine treatment, JNK activity increased six- to sevenfold over the basal level within 2-4 h. Treatment of MN9D/Neo with both staurosporine and a caspase inhibitor, Z-VAD, attenuated cell death without suppressing JNK activation. Both staurosporine-induced cell death and JNK activation were attenuated in MN9D/Bcl-2. As determined by cleavage of poly(ADP-ribose) polymerase into 85 kDa, Bcl-2 blocked caspase activity as well. When cells overexpressing one of the Bcl-2 mutants were treated with staurosporine, death was attenuated in MN9D/BH1, MN9D/BH2, and MN9D/C22 but not in MN9D/BH3 and MN9D/BH4. Similarly, both JNK and caspase activation were blocked in MN9D/BH1, MN9D/BH2, and MN9D/C22, whereas they were not suppressed in MN9D/BH3 and MN9D/BH4. Taken together, our data indicate that there exists a close structural and functional correlation of Bcl-2 to JNK and caspase activity in staurosporine-induced dopaminergic neuronal cell death.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.2000.0741621.x
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  • 4
    Electronic Resource
    Electronic Resource
    Temporal and spatial profile of caspase 8 expression and proteolysis after experimental traumatic brain injury (2001)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 78 (2001), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Recent studies have demonstrated that the downstream caspases, such as caspase 3, act as executors of the apoptotic cascade after traumatic brain injury (TBI) in vivo. However, little is known about the involvement of caspases in the initiation phase of apoptosis, and the interaction between these initiator caspases (e.g. caspase 8) and executor caspases after experimental brain injuries in vitro and in vivo. This study investigated the temporal expression and cell subtype distribution of procaspase 8 and cleaved caspase 8 p20 from 1 h to 14 days after cortical impact-induced TBI in rats. Caspase 8 messenger RNA levels, estimated by semiquantitaive RT-PCR, were elevated from 1 h to 72 h in the traumatized cortex. Western blotting revealed increased immunoreactivity for procaspase 8 and the proteolytically active subunit of caspase 8, p20, in the ipsilateral cortex from 6 to 72 h after injury, with a peak at 24 h after TBI. Similar to our previous studies, immunoreactivity for the p18 fragment of activated caspase 3 also increased in the current study from 6 to 72 h after TBI, but peaked at a later timepoint (48 h) as compared with proteolyzed caspase 8 p20. Immunohistologic examinations revealed increased expression of caspase 8 in neurons, astrocytes and oligodendrocytes. Assessment of DNA damage using TUNEL identified caspase 8- and caspase 3-immunopositive cells with apoptotic-like morphology in the cortex ipsilateral to the injury site, and immunohistochemical investigations of caspase 8 and activated caspase 3 revealed expression of both proteases in cortical layers 2–5 after TBI. Quantitative analysis revealed that the number of caspase 8 positive cells exceeds the number of caspase 3 expressing cells up to 24 h after impact injury. In contrast, no evidence of caspase 8 and caspase 3 activation was seen in the ipsilateral hippocampus, contralateral cortex and hippocampus up to 14 days after the impact. Our results provide the first evidence of caspase 8 activation after experimental TBI and suggest that this may occur in neurons, astrocytes and oligodendrocytes. Our findings also suggest a contributory role of caspase 8 activation to caspase 3 mediated apoptotic cell death after experimental TBI in vivo.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.2001.00460.x
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  • 5
    Electronic Resource
    Electronic Resource
    Sequential Cleavage of Poly(ADP-Ribose)polymerase and Appearance of a Small Bax-Immunoreactive Protein Are Blocked by Bcl-XL and Caspase Inhibitors During Staurosporine-Induced Dopaminergic Neuronal Apoptosis (1999)
    Oxford UK : Blackwell Science Ltd.
    Journal of neurochemistry 72 (1999), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: To assess the role of Bcl-XL and its splicederivative, Bcl-Xs, in staurosporine-induced cell death, we used adopaminergic cell line, MN9D, transfected with bcl-xL(MN9D/Bcl-XL), bcl-xs (MN9D/Bcl-Xs),or control vector (MN9D/Neo). Only 8.6% of MN9D/Neo cells survived after 24 hof 1 μM staurosporine treatment. Caspase activity was implicatedbecause a caspase inhibitor,N-benzyloxycarbonyl-Val-Ala-Asp-fluoromethyl ketone (Z-VAD-fmk),attenuated staurosporine-induced cell death. Bcl-XL rescued MN9Dcells from death (89.4% viable cells), whereas Bcl-Xs had little orno effect. Bcl-XL prevented morphologically apoptotic changes aswell as cleavage of poly(ADP-ribose)polymerase (PARP) induced bystaurosporine. It is interesting that a small Bax-immunoreactive proteinappeared 4-8 h after PARP cleavage in MN9D/Neo cells. The appearance of thesmall Bax-immunoreactive protein, however, may be cell type-specific as it wasnot observed in PC12 cells after staurosporine treatment. The sequentialcleavage of PARP and the appearance of the small Bax-immunoreactive protein inMN9D cells were blocked either by Z-VAD-fmk or by Bcl-XL. Thus, ourpresent study suggests that Bcl-XL but not Bcl-Xs prevents staurosporine-induced apoptosis by inhibiting the caspase activation that may be directly or indirectly responsible for the appearance of the small Bax-immunoreactive protein in some types of neurons.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1999.0722456.x
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  • 6
    Electronic Resource
    Electronic Resource
    Cooperative Interception of Neuronal Apoptosis by BCL-2 and BAG-1 Expression: Prevention of Caspase Activation and Reduced Production of Reactive Oxygen Species (1997)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 69 (1997), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Neuronally differentiated PC12 cells undergo synchronous apoptosis when deprived of nerve growth factor (NGF). Here we show that NGF withdrawal induces actinomycin D- and cycloheximide-sensitive caspase (ICE-like) activity. The peptide inhibitor of caspase activity, N-acetyl-Asp-Glu-Val-Asp-aldehyde, was more potent than acetyl-Tyr-Val-Ala-Asp-chloromethyl ketone in preventing NGF withdrawal-induced apoptosis, suggesting an important role for caspase-3 (CPP32)-like proteases. We observed a peak of reactive oxygen species (ROS) 6 h after NGF withdrawal. ROS appear to be required for apoptosis, because cell death is prevented by the free radical spin trap, N-tert-butyl-α-phenylnitrone, and the antioxidant, N-acetylcysteine. ROS production was blocked by actinomycin D, cycloheximide, and caspase protease inhibitors, suggesting that ROS generation is downstream of new mRNA and protein synthesis and activation of caspases. Forced expression of either BCL-2 or the BCL-2-binding protein BAG-1 blocked NGF withdrawal-induced apoptosis, activation of caspases, and ROS generation, showing that they function upstream of caspases. Coexpression of BCL-2 and BAG-1 was more protective than expression of either protein alone.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1997.69052075.x
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  • 7
    Electronic Resource
    Electronic Resource
    Up-regulation of Bax Protein in Degenerating Retinal Ganglion Cells Precedes Apoptotic Cell Death after Optic Nerve Lesion in the Rat (1997)
    Oxford, UK : Blackwell Publishing Ltd
    European journal of neuroscience 9 (1997), S. 0 
    Details
    ISSN: 1460-9568
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Retrograde degeneration of retinal ganglion cells as a consequence of optic nerve lesion has been shown to fulfil the criteria of apoptosis. In the present study, we investigated the time course of ganglion cell apoptosis following intraorbital crushing of the optic nerve in adult rats using morphological criteria and applying a terminal transferase technique (TUNEL) for in situ detection of DNA strand breaks. In addition, we examined expression patterns of the anti-apoptotic proteins Bcl-2 and Bcl-X and the cell death-promoting protein Bax in retinae after crushing the optic nerve. Apoptotic nuclei were detected in the ganglion cell layer in the first 3 weeks after optic nerve crush, with a peak after 6 days. Bcl-2 and Bcl-X proteins were expressed in ganglion cells at low levels. Expression of Bcl-2 decreased further during the days following crush. Bcl-X expression was initially increased, followed by a decline over the following days. In contrast, Bax protein, which was expressed in most ganglion cells at moderate baseline levels, was sharply increased as early as 30 min after crush, reached peak levels after 3 days, and remained up-regulated for at least 1 week thereafter. Double labelling for Bax and TUNEL in retinal sections, however, did not reveal colocalization of the two signals in individual retinal ganglion cells, consistent with the idea that increases in Bax precede apoptosis after optic nerve lesion. Thus, retinal ganglion cell death might be prevented by ablation of Bax protein in these cells, or by up-regulation of Bax-antagonists such as Bcl-2 or Bcl-X.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1460-9568.1997.tb01534.x
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  • 8
    Electronic Resource
    Electronic Resource
    SPECIAL REGIONS (1973)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 216 (1973), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1973.tb41375.x
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  • 9
    Electronic Resource
    Electronic Resource
    An inhibitor of Bcl-2 family proteins induces regression of solid tumours (2005)
    [s.l.] : Macmillian Magazines Ltd.
    Nature 435 (2005), S. 677-681 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Proteins in the Bcl-2 family are central regulators of programmed cell death, and members that inhibit apoptosis, such as Bcl-XL and Bcl-2, are overexpressed in many cancers and contribute to tumour initiation, progression and resistance to therapy. Bcl-XL expression ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature03579
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  • 10
    Electronic Resource
    Electronic Resource
    Oncogenic potential of bcl -2 demonstrated by gene transfer (1988)
    [s.l.] : Nature Publishing Group
    Nature 336 (1988), S. 259-261 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] DNA sequences encoding the p26 bcl-2-a or p22 bcl-2-^ were subcloned in both orientations into the pSV2-CAT expression vector7 to yield plasmids, pSV2-bcl-2-a, pSV2-bcl-2-a-AS (anti-sense, reversed orientation), pSV2-bcl-2-p and pSV2-fcc/-2-/3- AS (Fig. 1). Plasmid DNAs were then cotransfected with ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/336259a0
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