The dataset for the stages of concerns of public-school teachers towards the use of e-learning platform: Malaysian context.

This dataset contains demographic information of 355 respondents and a validated 32-items Stages of Concerns Questionnaire (SoCQ). The SoCQ questionnaire was developed based on the Concerns-Based Adoption Model (CBAM) which measures seven stages of concerns as the variables. They are unconcerned, informational, personal, management, consequence, collaboration and refocusing. The data was firstly tested with normality, followed by validity checking using confirmatory factor analysis (CFA). It is useful for policy makers and stakeholders to have a thorough understanding about teachers' concerns on the use of the e-learning platform and thus, design suitable interventions to smoothen the adoption process of using the technology. This set of data could be used in a multi-racial developing country for more complex analyses.

Emodin Induces Apoptosis of K562/Adr Cells Probably through Akt-Caspase 3 Signal Pathway / 中国实验血液学杂志

<p><b>OBJECTIVE</b>To investigate the apoptosis-inducing effects of emodin on multidrug resistant leukemia cell line K562/Adr, and to explore the role of Akt-Caspase 3 signal pathway in apoptosis of K562/Adr cells treated with emodin.</p><p><b>METHODS</b>K562/Adr cells were exposed to emodin of different doses. The ability of emodin to induce apoptosis of K562/Adr cells was detected by Annexin V/PI double labeled flow cytometry and DNA ploidy analysis, the expressions of procaspase-3, PARP, Akt, p-Akt protein were determined by Western blot.</p><p><b>RESULTS</b>Apoptosis in K562/Adr cells could be induced by emodin in a dose dependent manner, Western blot results showed that emodin down-regulated the expression levels of procaspase-3, Akt, p-Akt, PARA 116 KD in treated K562/Adr cells, up-regulated expressions leves of PARP 85 KD in a time-dependent manner.</p><p><b>CONCLUSION</b>The Akt-Caspase 3 signal pathway may be involved in these processes.</p>

Interleukin 8/KC enhances G-CSF induced hematopoietic stem/progenitor cell mobilization in Fancg deficient mice.

BACKGROUND: Fanconi anemia (FA) is a heterogeneous genetic disorder characterized by a progressive bone marrow aplasia, chromosomal instability, and acquisition of malignancies. Successful hematopoietic cell transplantation (HCT) for FA patients is challenging due to hypersensitivity to DNA alkylating agents and irradiation of FA patients. Early mobilization of autologous stem cells from the bone marrow has been thought to be ideal prior to the onset of bone marrow failure, which often occurs during childhood. However, the markedly decreased response of FA hematopoietic stem cells to granulocyte colony-stimulating factor (G-CSF) is circumventive of this autologous HCT approach. To-date, the mechanism for defective stem cell mobilization in G-CSF treated FA patients remains unclear. METHODS: Fancg heterozygous (Fancg (+/-)) mice utilized in these studies. Student's t-test and one-way ANOVA were used to evaluate statistical differences between WT and Fancg (-/-) cells. Statistical significance was defined as P values less than 0.05. RESULTS: Fancg deficient (Fancg (-/-)) mesenchymal stem/progenitor cells (MSPCs) produce significant lower levels of KC, an interleukin-8 (IL-8) related chemoattractant protein in rodents, as compared to wild type cells. Combinatorial administration of KC and G-CSF significantly increased the mobilization of hematopoietic stem/progenitor cells (HSPCs) in Fancg (-/-) mice. CONCLUSIONS: In summary, our results suggest that KC/IL-8 could be proved useful in the synergistic mobilization of FA HSPCs in combination with G-CSF.

Normal hematopoiesis and neurofibromin-deficient myeloproliferative disease require Erk.

Neurofibromatosis type 1 (NF1) predisposes individuals to the development of juvenile myelomonocytic leukemia (JMML), a fatal myeloproliferative disease (MPD). In genetically engineered murine models, nullizygosity of Nf1, a tumor suppressor gene that encodes a Ras-GTPase-activating protein, results in hyperactivity of Raf/Mek/Erk in hematopoietic stem and progenitor cells (HSPCs). Activated Erk1/2 phosphorylate kinases and transcription factors with myriad mitogenic roles in diverse cell types. However, genetic studies examining Erk1/2's differential and/or combined control of normal and Nf1-deficient myelopoiesis are lacking. Moreover, prior studies relying on chemical Mek/Erk inhibitors have reached conflicting conclusions in normal and Nf1-deficient mice. Here, we show that while single Erk1 or Erk2 disruption did not grossly compromise myelopoiesis, dual Erk1/2 disruption rapidly ablated granulocyte and monocyte production in vivo, diminished progenitor cell number, and prevented HSPC proliferation in vitro. Genetic disruption of Erk1/2 in the context of Nf1 nullizygosity (Mx1Cre(+)Nf1(flox/flox)Erk1(-/-)Erk2(flox/flox)) fully protects against the development of MPD. Collectively, we identified a fundamental requirement for Erk1/2 signaling in normal and Nf1-deficient hematopoiesis, elucidating a critical hematopoietic function for Erk1/2 while genetically validating highly selective Mek/Erk inhibitors in a leukemia that is otherwise resistant to traditional therapy.

Effect of emodin on proliferation inhibition and apoptosis induction in leukemic K562 cells / 中国实验血液学杂志

The study was aimed to investigate the effects of emodin on proliferation inhibition and apoptosis induction in human chronic myeloid leukemia cell line K562 cells, and to explore the role of P210 protein and activation of caspase 3 in these processes. K562 cells were exposed to emodin at different doses. The proliferation inhibition was detected by MTT assay and colony formation test. The ability of emodin to induce apoptosis and DNA fragmentation were examined by flow cytometry. The expressions of P210, procaspase-3 and PARP protein were determined by Western blot. The results indicated that the emodin remarkably inhibited the K562 cell proliferation, with IC(50) value of 38.25 micromol/L after treatment for 48 hours. Meanwhile induced apoptosis, Annexin V-FITC positive cells, sub-G(1) apoptotic peak and DNA fragmentation in K562 cells confirmed that emodin induced apoptosis in K562 cells in dose-dependent manner. Western blot results showed that emodin inhibited phosphorylation of P210 protein in K562 cells and down-regulated the expression levels of P210. The procaspase-3 level in treated K562 cells decreased with increased expressions of PARP in time-dependent manner. It is concluded that the emodin efficiently inhibits growth and induces apoptosis of K562 cells, while the inhibition of phosphorylation of P210 protein, down-regulation of P210 protein expression and activation of caspase-3 may be involved in these processes.

Inhibitory effects of emodin on drug-resistant HL-60/ADR cell proliferation and its induction of apoptosis / 中国实验血液学杂志

The study was aimed to investigate the effects of emodin on the proliferation and apoptosis of adriamycin-resistant HL-60/ADR cells, and to explore the underlying mechanism. The cell viability and colony formation were detected by MTT assay and colony formation assay respectively. Apoptotic cells were tested by means of cell cycle analysis, mitochondrial transmembrane potential levels, caspase-3 activity detection, Annexin V FITC/PI staining and TUNEL labeling. RT-PCR was used to analyze the bcl-2 and c-myc mRNA expressions. The protein expressions of Bcl-2, c-Myc and caspase-3 precursor were determined by Western blot. The results showed that HL-60/ADR cell growth was significantly inhibited by emodin in dose and time dependent manners. Cell colony formation obviously decreased with IC50 5.79 micromol/L. G0/G1 phase cell population increased while G2/M phase cells decreased in 40 and 80 micromol/L groups compared with control group (p < 0.01), and no significant difference of cell cycle was observed in 20 micromol/L group (p > 0.05). The typical hypo-diploid peak (apoptotic peak) appeared in each dose group. The levels of mitochondrial transmembrane potential of HL-60/ADR cells decreased and caspase-3 activity increased when incubated with emodin for 12 and 24 hours respectively. Apoptosis occurred in a dose-dependent manner, and its earlier and later stages were identified by Annexin-V FITC/PI staining and TUNEL labeling methods respectively. The expressions of bcl-2, c-myc mRNA and Bcl-2, c-Myc, caspase-3 precursor protein were all down-regulated in a time-dependent manner after treatment with emodin at different times. It is concluded that emodin efficiently inhibits growth and induces apoptosis on HL-60/ADR cells, which may be related with the down-regulation of mitochondrial transmembrane potential and expressions of bcl-2 and c-myc, as well as up-regulation of caspase-3 activity.

Emodin induces leukemic HL-60 cells apoptosis probably by inhibiting Akt signal pathway / 药学学报

This study is to investigate the effect of emodin on inducing human myeloid leukemia cell line HL-60 apoptosis and the role of Akt signal pathway in the apoptosis. HL-60 cells were exposed to various dosages of emodin. MTT assay was used to detect HL-60 cell proliferation. Distribution of HL-60 cells in cell cycle was analyzed by flow cytometry and cell apoptosis was observed by MitoCapture apoptosis detection. The protein expressions of Akt signal pathway were detected by Western blotting. The result showed that emodin remarkably inhibited the cell proliferation. The IC50 value for 48 h treatment was about 20 micromol x L(-1). Apoptosis in HL-60 cells could be efficiently induced by emodin in a dose dependent manner and cells were arrested at G0/G1. The expressions of Akt, p-Akt, IkappaB-alpha, p-IkappaB-alpha, p65, p-p65, mTOR and p-mTOR in Akt signal pathway were downregulated after emodin treatment. It can be concluded that emodin could efficiently induce growth inhibition and apoptosis in HL-60 cells. Akt signal pathway may be involved in this process.