Protein microarray analysis of apoptosis-related protein expression following heat shock in human tongue squamous cell carcinomas containing different p53 phenotypes. Int. J. Hyperthermia, 2008; 24(8), 605–612.
International Journal of Hyperthermia hereby notifies its readers that errors were published in the article listed above. The corrections are shown in bold face below:
p. 608, right column, 3rd paragraph:
In Table III, among the proteins which inhibit apoptosis, Bcl-2 (B–cell lymphoma/leukemia-2), COX (cyclooxygenase)-2, PKCα, PKCβ, DFF45 (DNA fragmentation factor-45), PKCθ, Bcl-xL (B-cell CLL/lymphoma × the long isoform), MDM2 (murine double minute 2), NF-κB (nuclear factor κB), Rb2 (retinoblastoma protein 2), STAT3 (signal transducer and activator of transcriptional 3), TRAF2 (tumor necrosis factor receptor associated factor 5), IL-6 (interleukin 6), PKCλ, PKCτ and IKK-α/1 (I-κ-B kinase-α/1) were up-regulated in SAS/mp53 cells. FADD/Mort-1, Ku70, PKCδ, PKCε and E2F-1 were up-regulated in SAS/mp53 cells as well as in SAS/neo cells. Other apoptosis-inducing proteins were also up-regulated in SAS/mp53 cells. These were Baxα (Bcl-2 associated × protein α), cRAF-1 (v-raf-1 murine leukemia vial oncogene homolog 1), TGF-β1(transforming growth factor β1), cytochrome c/Apaf-2 (apoptotic protease activating factor 2), c-Myc (cellular homologue of avian myelocytomatosis virus oncogene), Bak (Bcl-2 homologous antagonist/killer), DAP3 (death-associated protein kinase 3), Smad2 (Sma- and Mad-related protein 2) and Smad4/DPC4 (Sma- and Mad-related protein 4/deleted in pancreatic cancer locus 4). The level of induced Hsp90 (heat shock protein 90) in SAS/mp53 cells was higher than that induced in SAS/neo cells.
p. 611, left column, 1st paragraph:
The results reported here show that apoptosis-inhibitory proteins (such as Bcl-2, Bcl-xL, IL-6, and others) were strongly induced by heat treatment in SAS/mp53 cells when compared to SAS/neo cells containing a wtp53.