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- Jacobsohn, L. G, et al.
(författare)
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Role of intericosahedral chains on hardness of sputtered boron carbide films
- 2004
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Ingår i: Applied Physics Letters. - : AIP Publishing. - 0003-6951 .- 1077-3118. ; 84:21, s. 4173-
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Tidskriftsartikel (refereegranskat)abstract
- The relationship between the structure and mechanical properties of sputter-deposited boron carbide films was investigated. Changes in the structure induced by annealing were characterized in terms of chemical composition, chemical bonding, and concentrations of defects and trapped impurities. The creation of intericosahedral chains for higher annealing temperatures was revealed by infrared and Raman measurements, and the intensity of the infrared band at 1500 cm–1 was found to be related to the hardness. The presence of residual trapped Ar atoms and of open-volume defects is insensitive to relatively high annealing temperatures and does not influence the recovery of the hardness. Our results suggest postdeposition annealing as a pathway to enhance the mechanical properties of boron carbide films.
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- Los, Marek Jan, et al.
(författare)
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Activation and caspase-mediated inhibition of PARP : A molecular switch between fibroblast necrosis and apoptosis in death receptor signaling
- 2002
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Ingår i: Molecular Biology of the Cell. - : American Society for Cell Biology. - 1059-1524 .- 1939-4586. ; 13:3, s. 978-988
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Tidskriftsartikel (refereegranskat)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-I mutant were more sensitive to TNF than wild-tvpe 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.
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- Los, Marek Jan, et al.
(författare)
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Functional characterization of DNase X, a novel endonuclease expressed in muscle cells
- 2000
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Ingår i: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 39:25, s. 7365-7373
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Tidskriftsartikel (refereegranskat)abstract
- The activation of endonucleases resulting in the degradation of genomic DNA is one of the most characteristic changes in apoptosis. Here, we report the characterization of a novel endonuclease, termed DNase X due to its X-chromosomal localization. The active nuclease is a 35 kDa protein with 39% identity to DNase I. When incubated with isolated nuclei, recombinant DNase X was capable of triggering DNA degradation at internucleosomal sites. Similarly to DNase I, the nuclease activity of DNase X was dependent on Ca2+ and Mg2+ and inhibited by Zn2+ ions or chelators of bivalent cations. Overexpression of DNase X caused internucleosomal DNA degradation and induction of cell death associated with increased caspase activation. Despite the presence of two potential caspase cleavage sites, DNase X was processed neither in vitro nor in vivo by different caspases. Interestingly, after initiation of apoptosis DNase X was translocated from the cytoplasm to the nuclear compartment and aggregated as a detergent-insoluble complex. Abundant expression of DNase X mRNA was detected in heart and skeletal muscle cells, suggesting that DNase X may be involved in apoptotic or other biological events in muscle tissues.
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