| 1. |
- Ghavami, S., et al.
(författare)
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Apoptosis and cancer : mutations within caspase genes
- 2009
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Ingår i: Journal of Medical Genetics. - : B M J Group. - 0022-2593 .- 1468-6244. ; 46:8, s. 497-510
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Forskningsöversikt (refereegranskat)abstract
- The inactivation of programmed cell death has profound effects not only on the development but also on the overall integrity of multicellular organisms. Beside developmental abnormalities, it may lead to tumorigenesis, autoimmunity, and other serious health problems. Deregulated apoptosis may also be the leading cause of cancer therapy chemoresistance. Caspase family of cysteinyl-proteases plays the key role in the initiation and execution of programmed cell death. This review gives an overview of the role of caspases, their natural modulators like IAPs, FLIPs, and Smac/Diablo in apoptosis and upon inactivation, and also in cancer development. Besides describing the basic mechanisms governing programmed cell death, a large part of this review is dedicated to previous studies that were focused on screening tumours for mutations within caspase genes as well as their regulators. The last part of this review discusses several emerging treatments that involve modulation of caspases and their regulators. Thus, we also highlight caspase cascade modulating experimental anticancer drugs like cFLIP-antagonist CDDO-Me; cIAP1 antagonists OSU-03012 and ME-BS; and XIAP small molecule antagonists 1396-11, 1396-12, 1396-28, triptolide, AEG35156, survivin/Hsp90 antagonist shephedrin, and some of the direct activators of procaspase-3.
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| 2. |
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| 3. |
- Abdi, Y., et al.
(författare)
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Light-emitting nano-porous silicon structures fabricated using a plasma hydrogenation technique
- 2005
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Ingår i: Materials Science and Engineering B: Solid-State Materials for Advanced Technology. - : Elsevier BV. - 0921-5107. ; 124-125:SUPPL., s. 483-487
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Tidskriftsartikel (refereegranskat)abstract
- The preparation of porous silicon films by DC-plasma hydrogenation and subsequent annealing of amorphous silicon films on silicon and glass substrates is reported for the first time. The effects of varying plasma power and annealing temperatures have been investigated and characterized by scanning-electron microscopy, transmission-electron microscopy, and photoluminescence. A plasma density of about 5.5 W/m2 and hydrogenation-annealing temperatures of about 400 °C was found to be suitable for the formation of nano-crystalline silicon films with grain diameters of the order of 3-10 nm. The intensity and wavelength of the emitted visible light were found to depend on the hydrogenation and annealing conditions, and patterning of the silicon films using standard lithography allowed the creation of light-emitting patterns.
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| 5. |
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| 6. |
- Ghavami, Saeid, et al.
(författare)
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S100A8/9 induces cell death via a novel, RAGE-independent pathway that involves selective release of Smac/DIABLO and Omi/HtrA2
- 2008
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Ingår i: Biochimica et Biophysica Acta. Molecular Cell Research. - : Elsevier. - 0167-4889 .- 1879-2596. ; 1783:2, s. 297-311
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Tidskriftsartikel (refereegranskat)abstract
- A complex of two S100 EF-hand calcium-binding proteins S100A8/A9 induces apoptosis in various cells, especially tumor cells. Using several cell lines, we have shown that S100A8/A9-induced cell death is not mediated by the receptor for advanced glycation endproducts (RAGE), a receptor previously demonstrated to engage S100 proteins. Investigation of cell lines either deficient in, or over-expressing components of the death signaling machinery provided insight into the S100A8/A9-mediated cell death pathway. Treatment of cells with S100A8/A9 caused a rapid decrease in the mitochondrial membrane potential (ΔΨm) and activated Bak, but did not cause release of apoptosis-inducing factor (AIF), endonuclease G (Endo G) or cytochrome c. However, both Smac/DIABLO and Omi/HtrA2 were selectively released into the cytoplasm concomitantly with a decrease in Drp1 expression, which inhibits mitochondrial fission machinery. S100A8/A9 treatment also resulted in decreased expression of the anti-apoptotic proteins Bcl2 and Bcl-XL, whereas expression of the pro-apoptotic proteins Bax, Bad and BNIP3 was not altered. Over-expression of Bcl2 partially reversed the cytotoxicity of S100A8/A9. Together, these data indicate that S100A8/A9-induced cell death involves Bak, selective release of Smac/DIABLO and Omi/HtrA2 from mitochondria, and modulation of the balance between pro- and anti-apoptotic proteins.
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| 7. |
- Ghavami, Saeid, et al.
(författare)
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S100A8/A9 at low concentration promotes tumor cell growth via RAGE ligation and MAP kinase-dependent pathway
- 2008
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Ingår i: Journal of Leukocyte Biology. - : eration of American Societies for Experimental Biology. - 0741-5400 .- 1938-3673. ; 83:6, s. 1484-1492
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Tidskriftsartikel (refereegranskat)abstract
- The complex formed by two members of the S100 calcium-binding protein family, S100A8/A9, exerts apoptosis-inducing activity against various cells, especially tumor cells. Here, we present evidence that S100A8/A9 also has cell growth-promoting activity at low concentrations. Receptor of advanced glycation end product (RAGE) gene silencing and cotreatment with a RAGE-specific blocking antibody revealed that this activity was mediated via RAGE ligation. To investigate the signaling pathways, MAPK phosphorylation and NF-κB activation were characterized in S100A8/A9-treated cells. S100A8/A9 caused a significant increase in p38 MAPK and p44/42 kinase phosphorylation, and the status of stress-activated protein kinase/JNK phosphorylation remained unchanged. Treatment of cells with S100A8/A9 also enhanced NF-κB activation. RAGE small interfering RNA pretreatment abrogated the S100A8/A9-induced NF-κB activation. Our data indicate that S100A8/A9-promoted cell growth occurs through RAGE signaling and activation of NF-κB.
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