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  • 1
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    Retraction: Depletion of pleckstrin homology domain leucine-rich repeat protein phosphatases 1 and 2 by Bcr-Abl promotes chronic myelogenous leukemia cell proliferation through continuous phosphorylation of Akt isoforms.
    Elsevier BV ; 2010
    In:  Journal of Biological Chemistry Vol. 285, No. 20 ( 2010-05), p. 15662-
    Details
    In: Journal of Biological Chemistry, Elsevier BV, Vol. 285, No. 20 ( 2010-05), p. 15662-
    Type of Medium: Online Resource
    ISSN: 0021-9258
    URL: Article
    DOI: 10.1074/jbc.A109.808182
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2010
    detail.hit.zdb_id: 2141744-1
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    SSG: 12
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  • 2
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    Etodolac inhibits EBER expression and induces Bcl‐2‐regulated apoptosis in Burkitt's lymphoma cells
    Wiley ; 2005
    In:  European Journal of Haematology Vol. 75, No. 3 ( 2005-09), p. 212-220
    Details
    In: European Journal of Haematology, Wiley, Vol. 75, No. 3 ( 2005-09), p. 212-220
    Abstract: Abstract:  Cyclooxygenase‐2 (COX‐2) is reported to be an important cellular target for therapy in malignancies. The growth inhibitory effects of COX‐2 inhibitors on malignancies have been demonstrated to be through not only COX‐2 dependent, but also independent mechanisms. In this study, we showed that etodolac, COX‐2 inhibitor, induced apoptosis via COX‐2 independent pathway, and investigated the molecular details of etodolac‐induced apoptosis in Burkitt's lymphoma cells. In Daudi and Raji Burkitt's lymphoma cell lines, which expressed no COX‐2 enzyme, etodolac more strongly induced apoptosis compared to meloxicam. Moreover, etodolac did not induce apoptosis to normal B‐lymphocytes. For the pathway of etodolac‐induced apoptosis, reduction of anti‐apoptotic bcl‐2 mRNA and Bcl‐2 protein, activation of Caspase‐9 and ‐3, down‐regulation of caspase inhibitors, c‐IAP‐1 and Survivin were involved. Moreover, EBER‐1 and ‐2 expression in Epstein–Barr virus positive Daudi and Raji cells were reduced to result in down‐regulation of Bcl‐2 by treatment with etodolac. It has been reported that etodolac has stereoisomers, R‐ and S‐etodolac. We found that racemate of etodolac more strongly induced apoptosis in Daudi and Raji cells compared to R‐ or S‐etodolac. In conclusion, our findings indicated etodolac inhibited EBERs expression and induced apoptosis via a Bcl‐2‐regulated pathway. Moreover, racemate of etodolac more effectively induced apoptosis than R‐ and/or S‐etodolac. Therefore, these activities of etodolac potentially extend to the treatment of patients with Burkitt's lymphoma resistant to chemotherapy.
    Type of Medium: Online Resource
    ISSN: 0902-4441 , 1600-0609
    URL: Issue
    URL: Article
    DOI: 10.1111/ejh.2005.75.issue-3
    DOI: 10.1111/j.1600-0609.2005.00498.x
    Language: English
    Publisher: Wiley
    Publication Date: 2005
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  • 3
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    Depletion of PHLPP1 and 2 by Bcr-Abl Promotes CML Cell Proliferation through the Continuous Phosphorylation of Akt.
    American Society of Hematology ; 2009
    In:  Blood Vol. 114, No. 22 ( 2009-11-20), p. 2182-2182
    Details
    In: Blood, American Society of Hematology, Vol. 114, No. 22 ( 2009-11-20), p. 2182-2182
    Abstract: Abstract 2182 Poster Board II-159 Objective PHLPP1 and 2 (pleckstrin homology (PH) domain leucine-rich repeat protein phosphatase 1 and 2) is identified as the dephosphorylation enzyme of Akt, the same as that of PP2A of the dephosphorylation enzyme of Akt, and regulate the cell-growth signal of Akt through a dephosphorylation of the phosphorylated Akt (p-Akt). Previously, we reported the expression of PHLPP1 and 2 were suppressed in CML cell lines. In this study, we investigated the the CML and its progenitor cell proliferation through the phosphorylation of Akt by depletion of PHLPP1 and 2. Method CML cell lines (K562, Meg01, SHG3) and the CML clinical specimen (n= 10) were used for this research. The changes in the expression of PHLPP1 and 2 by treatment with Abl kinase inhibitors (STI571, AMN107 and BMS354825) or knock down with Bcr-Abl gene were evaluated by RT-PCR method. The influence on the expression of PHLPP1 and 2 in AML cell line transfected with Bcr-Abl also evaluated. CML progenitor cells derived from CML patients separated by ALDH activity, and the expression of PHLPP1 and 2 were investigated by quantitative RT-PCR method. p-Ser473 Akt1, 2 and 3 by Abl kinase inhibitor or knock down with PHLPP1 and 2 were measured, and the influence on the effect of cell growth inhibition by MTT assay. The expression of PHLPP1 and 2 and colony formation in colony forming unit-granulocyte, erythroid, macrophage, megakaryocyte (CFU-GEMM), colony forming unit-granulocyte, macrophage (CFU-GM) and burst forming unit-erythroid (BFU-E) derived from Bcr-Abl positive hematopoietic progenitor cells also evaluated. Result The expression of mRNA and protein of PHLPP1 and 2 were increased by treatment with Abl kinase inhibitor or Bcr-Abl knock down by siRNA in CML cell lines and AML cell line trasfected with Bcr-Abl gene. Moreover, p-Ser473 Akt 2 and 3 were decreased according to the expression of PHLPP1, and also p-Ser473 Akt1 and 3 according to the expression of PHLPP2. The Abl kinase inhibitors induced the expression of PHLPP1, 2 and the reduction of p-Ser473 Akt isoforms. The Abl kinase inhibitors inhibited the CML cell proliferation via the depletion of PHLPP1 and 2. In Bcr-Abl positive progenitor cells, the expression of PHLPP1 and 2 was increased, and colony formation was suppressed by Abl kinase inhibitor and by Bcr-Abl siRNA. The colony formation in progenitor cells knocked down PHLPP1 and 2 were decreased when treated with Abl kinase inhibitors. Conclusion These results suggest that Bcr-Abl might promote CML cell proliferarion through continuous phosphorylation of p-Ser473 Akt1, 2 and 3 by suppression of PHLPP1 and 2, and that the induction of PHLPP1 and 2 may be effective to regulate the cell proliferation in CML cells. It may be also that the induction of expression of PHLPPs has the potential possibility as the targets on the regulation of cell proliferation in Bcr-Abl positive progenitor cells. Disclosures: No relevant conflicts of interest to declare.
    Type of Medium: Online Resource
    ISSN: 0006-4971 , 1528-0020
    URL: Article
    DOI: 10.1182/blood.V114.22.2182.2182
    RVK:
    XA 33000
    RVK:
    XA 10000
    Language: English
    Publisher: American Society of Hematology
    Publication Date: 2009
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  • 4
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    Etodolac Induces Apoptosis and Inhibits Cell Adhesion to Bone Marrow Stromal Cells in Human Myeloma Cells.
    American Society of Hematology ; 2004
    In:  Blood Vol. 104, No. 11 ( 2004-11-16), p. 4836-4836
    Details
    In: Blood, American Society of Hematology, Vol. 104, No. 11 ( 2004-11-16), p. 4836-4836
    Abstract: Cyclooxygenase-2 (COX-2) is reported to regulate apoptosis and to be an important cellular target for therapy. In this study, we demonstrated that etodolac, a COX-2 inhibitor, inhibited proliferation and induced apoptosis in myeloma cell lines (RPMI 8226 and MC/CAR cells), expressing the COX-2 enzyme. In both cell lines, etodolac more strongly induced apoptosis compared with thalidomide or meloxicam. Etodolac induced down-regulation of bcl-2 protein and mRNA, activation of caspase-9, -7 and -3, down-regulation of caspase inhibitors, cIAP-1 and survivin, and loss of mitochondrial membrane potential in a dose-dependent manner. In addition, our data demonstrated that when myeloma cells were coincubated with 50 mM etodolac on bone marrow stromal cells (BMSC), myeloma cell adhesion to BMSC was significantly inhibited compared with thalidomide or meloxicam coincubation, and the adhesion molecules VLA-4, LFA-1 (CD11a), CXCX4, and CD44 were suppressed on myeloma cells treated with etodolac. Moreover, we found that 100 mM R-etodolac, S-etodolac, and the combination of R- and S-etodolac, which are the stereoisomers of etodolac, slightly inhibited the proliferation of myeloma cells, while 50 to 100 mM etodolac significantly inhibited the proliferation of myeloma cells. In conclusion, our findings indicate that etodolac induced apoptosis via a bcl-2 dependent pathway, suppressed the expression of adhesion molecules, and inhibited myeloma cell adhesion to BMSC compared with thalidomide or meloxicam. Thus, the activities of etodolac potentially extend to the treatment of patients with myeloma resistant to standard chemotherapy, including thalidomide.
    Type of Medium: Online Resource
    ISSN: 0006-4971 , 1528-0020
    URL: Article
    DOI: 10.1182/blood.V104.11.4836.4836
    RVK:
    XA 33000
    RVK:
    XA 10000
    Language: English
    Publisher: American Society of Hematology
    Publication Date: 2004
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  • 5
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    Elevation of Kinase Interacting with Stathmin (KIS) and Promotion of Cellcycle Progression by KIS in Leukemia Cells.
    American Society of Hematology ; 2005
    In:  Blood Vol. 106, No. 11 ( 2005-11-16), p. 1365-1365
    Details
    In: Blood, American Society of Hematology, Vol. 106, No. 11 ( 2005-11-16), p. 1365-1365
    Abstract: Purpose: The protein p27 is an important regulator of cell cycle. An increase in p27 causes proliferation of cells, while a decrease in p27 induces quiescence of cells. p27 is regulated by transcriptional, translational and proteolytic mechanisms. Among them, an importnant mechanism in the regulation of p27 is proteolysis. Kinase interacting with stathmin, KIS, is a serine / threonine kinase, and regulates cell cycle progression through the phosphorylation of p27 on serine 10. The S10 phosphorylation on p27 plays an important role in p27 degradation. KIS that phosphorylates p27 on S10 and its role in the regulation of cell cycle progression have not been defined in leukemia cells. In this study, we investigated the role of KIS in leukemia cells. Materials and Methods: We examined the biological significance of KIS expression in K562, NB4, U937, CEM, MOLT4, and SUP-B15 leukemia cells and relationship with the G1 regulaters, such as p27. Moreover, we generated the lentivirus vector inserted with the dsDNA of KIS small interfering RNA (siRNA), and effects of down-regulation of KIS by siRNA transfection were investigated in leukemia cells. Results: RT-PCR and western blot analysis showed high KIS expression in all leukemia cells. The p27 phosphorylation on S10 was significantly lower in the leukemia cells transduced with KIS siRNA and depletion of KIS enhanced growth arrest. The down-regulation of KIS induced G1 arrest in cell cycle, but not apoptosis. In cell cycle analysis, control leukemia cells showed 42.3 ± 1.8 %, but leukemia cells transfected with KIS siRNA showed 67,1 ± 2.1 % in G1 fraction. Moreover, these cells significantly showed small population in S ansd G2 fractions compared compared with controls. Conclusion: These findings suggest KIS expression promotes cell cycle progression in leukemia cells. Depletion of KIS using siRNA in leukemia cells induced cell cycle arrest in G1 phase compared with control cells. In this study, we showed that KIS might be the target for the molecular therapy.
    Type of Medium: Online Resource
    ISSN: 0006-4971 , 1528-0020
    URL: Article
    DOI: 10.1182/blood.V106.11.1365.1365
    RVK:
    XA 33000
    RVK:
    XA 10000
    Language: English
    Publisher: American Society of Hematology
    Publication Date: 2005
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  • 6
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    Development as Anti-Leukemic Agents, a Novel Synthesis of Phospha Sugar Derivatives in Therapy for Leukemias, and Analysis of Their Characterizations.
    American Society of Hematology ; 2007
    In:  Blood Vol. 110, No. 11 ( 2007-11-16), p. 4174-4174
    Details
    In: Blood, American Society of Hematology, Vol. 110, No. 11 ( 2007-11-16), p. 4174-4174
    Abstract: [Background] Sugar derivatives whose oxygen atom in the hemiacetal ring is replaced by a carbon, nitrogen, sulfur atom, and etc., are celled as pseudo sugars. The synthesis and bioassay of these pseudo sugars are well investigated and are known as potential bioactive materials. Phospha sugar, which is one of pseudo sugars, having a phosphorus atom instead of the oxygen atom in the hemiacetal ring, is little known. The synthesis and bioassay of phospha sugars are not well studied in detail. We synthesized the 2, 3, 4-tribromo-3-methyl-1-phenyl phospholane 1-oxide (TMPP) and 2, 3-dibromo-3-methyl-1-phenyl phospholane 1-oxide (DMPP) by the nucleophilic substitution reactions, and found their anti-leukemic activities. [Purpose] The aims of the present study were to evaluate the inhibition of proliferation and induction of apoptosis in leukemia cell treated with TMPP or DMPP, and define the target molecules for TMPP in leukemia cells. [Methods] The cells used in this study were human leukemia cell lines, K562, U937, and YRK2 cells. For proliferation analysis, MTT assays were performed in leukemia cells treated with TMPP. For cell cycle analysis, flow cytometory analysis was performed in leukemia cells treated with TMPP or DMPP by PI staining. For analysis of mitotic regulatory proteins (p27, p21, Skp2, Cdc25B, Cyclin D1, Survivin, and Aurora kinase B), Western blotting was perfo rmed in leukemia cells treated with TMPP. [Results] In leukemia cell lines, DMPP and TMPP significantly inhibited the cell proliferation, and TMPP more strongly inhibited the cell proliferation than DMPP. 10 μM TMPP significantly induced G2/M phase arrest, and 25 μM TMPP induced apoptosis in leukemia cells. In leukemia cells, 10 μM TMPP reduced protein of Aurora kinase B, Survivin, Cyclin D1, Skp2 KIS, and FoxM1, while increased protein expression of p21and p27 by western blot analysis. Moreover, 25 μM TMPP activated caspase-3 and caspase-9, cleaved PARP, and reduced Bcl-2. [Conclusions] In this study, we report in the first time the possibility of phospha sugar derivatives as anti-leukemic agents in therapy for leukemias, and analysis of their characterizations. DMPP significantly inhibited the proliferation, and induced apoptosis of leukemia cells. These results demonstrated that the FoxM1, which is an essential transcription factor for cell growth and regulates expression of the mitotic regulators, is one of the targets for DMPP. Therefore, DMPP or TMPP has possibility as new agents for FoxM1 in leukemia therapy.
    Type of Medium: Online Resource
    ISSN: 0006-4971 , 1528-0020
    URL: Article
    DOI: 10.1182/blood.V110.11.4174.4174
    RVK:
    XA 33000
    RVK:
    XA 10000
    Language: English
    Publisher: American Society of Hematology
    Publication Date: 2007
    detail.hit.zdb_id: 1468538-3
    detail.hit.zdb_id: 80069-7
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  • 7
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    Bcr-Abl Inhibitors Induce Expression of HoxA10, Playing a Role as an Inhibitor of the Proliferation through PI3K/PKB Pathway in Chronic Myelogenous Leukemia Cells.
    American Society of Hematology ; 2006
    In:  Blood Vol. 108, No. 11 ( 2006-11-16), p. 1363-1363
    Details
    In: Blood, American Society of Hematology, Vol. 108, No. 11 ( 2006-11-16), p. 1363-1363
    Abstract: [Background] Homeobox (Hox) genes are grouped together in 4 clusters, A to D. Recent studies has shown that the Hox proteins are important in the control of differentiation and proliferation in hematopoietic cells. It is reported that HoxA10 has been expressed in all types acute myeloid leukemias (except for APL) but not in acute lymphoid leukemias, implicating an important role as a regulator of myeloid progenitors. Moreover, overexpression of HoxA10 induses the proliferation of early progenitor cells and leads to the development of myeloid leukemias. However, we found that Bcr-Abl inhibitors increased the expression of HoxA10 gene in CML cells. In this study, we investigated the mechanism controlling HoxA10 in CML cells treated with Bcr-Abl inhibitors. [Methods] The cells used in this study were Ph1 positive CML cells, K562 and Meg01, and U937 cells for a Ph1 negative cell. We used AMN107 and BMS354825 for Bcr-Abl inhibitors, LY294002 for a PI3K inhibitor, PP2 for a Src kinase inhibitor, and SB203580 for a p38 MAP kinase inhibitor. For analysis of HoxA10 mRNA and protein, RT-PCR and western blot were performed in K562, Meg-01 and U937 cells, which untreated or treated with AMN107, BMS354825, LY294002, PP2, or SB203580 respectively. We then attempted to localize the intracellular locations of HoxA10 in K562 and Meg01, which untreated or treated with AMN107, BMS354825, or LY294002 by using conforcal fluorescence microscopy. Finally, for analysis of proliferation in K562, Meg-01 and U937 transfected with siRNA HoxA10, MTT assays were performed in untransfected or transfected K562, Meg-01 and U937 treated with or without AMN107, BMS354825, orLY294002. [Results] Both K562 and Meg01 cells expressed HoxA10 mRNA and protein at lower level compared to U937 cells. Interestingly, treatment with AMN107, BMS354825, or LY294002 increased the expression of HoxA10 mRNA and protein in both K562 and Meg01 cells. In contrast, treatment with PP2 or SB203580 did not affect the expression of HoxA10 mRNA and protein in both K562 and Meg01 cells. The fluorescence of HoxA10 was more strongly observed in the area corresponding to the cell’s cytoplasm than nucleus, and the treatment with AMN107, BMS354825, or LY294002 increased the fluorescence in nucleus of K562 and Meg01 cells in a time-dependent manner. In K562 and Meg01 cells transfected with the siRNA HoxA10, treatment with AMN107 or BMS354825 slightly inhibited the proliferation compared to K562 and Meg01 transfected with control siRNA. [Conclusions] In this study, we showed that Bcr-Abl inhibitors induced the expression of HoxA10, and HoxA10 was regulated by PI3K/P[Kappa[B pathway in CML cells. This finding indicates a new insight in the regulation of cell proliferation via the PI3K/PKB signal pathway in CML cells.
    Type of Medium: Online Resource
    ISSN: 0006-4971 , 1528-0020
    URL: Article
    DOI: 10.1182/blood.V108.11.1363.1363
    RVK:
    XA 33000
    RVK:
    XA 10000
    Language: English
    Publisher: American Society of Hematology
    Publication Date: 2006
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  • 8
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    CMC‐544 (inotuzumab ozogamicin) shows less effect on multidrug resistant cells: analyses in cell lines and cells from patients with B‐cell chronic lymphocytic leukaemia and lymphoma
    Wiley ; 2009
    In:  British Journal of Haematology Vol. 146, No. 1 ( 2009-07), p. 34-43
    Details
    In: British Journal of Haematology, Wiley, Vol. 146, No. 1 ( 2009-07), p. 34-43
    Abstract: The effect of CMC‐544, a calicheamicin‐conjugated anti‐CD22 monoclonal antibody, was analysed in relation to CD22 and P‐glycoprotein (P‐gp) in B‐cell chronic lymphocytic leukaemia (CLL) and non‐Hodgkin lymphoma (NHL) in vitro . The cell lines used were CD22‐positive parental Daudi and Raji, and their P‐gp positive sublines, Daudi/MDR and Raji/MDR. Cells obtained from 19 patients with B‐cell CLL or NHL were also used. The effect of CMC‐544 was analysed by viable cell count, morphology, annexin‐V staining, and cell cycle distribution. A dose‐dependent, selective cytotoxic effect of CMC‐544 was observed in cell lines that expressed CD22. CMC‐544 was not effective on Daudi/MDR and Raji/MDR cells compared with their parental cells. The MDR modifiers, PSC833 and MS209, restored the cytotoxic effect of CMC‐544 in P‐gp‐expressing sublines. In clinical samples, the cytotoxic effect of CMC‐544 was inversely related to the amount of P‐gp ( P  = 0·003), and to intracellular rhodamine‐123 accumulation ( P   〈  0·001). On the other hand, the effect positively correlated with the amount of CD22 ( P  = 0·010). The effect of CMC‐544 depends on the levels of CD22 and P‐gp. Our findings will help to predict the clinical effectiveness of this drug on these B‐cell malignancies, suggesting a beneficial effect with combined use of CMC‐544 and MDR modifiers.
    Type of Medium: Online Resource
    ISSN: 0007-1048 , 1365-2141
    URL: Issue
    URL: Article
    DOI: 10.1111/bjh.2009.146.issue-1
    DOI: 10.1111/j.1365-2141.2009.07701.x
    RVK:
    XA 34100
    Language: English
    Publisher: Wiley
    Publication Date: 2009
    detail.hit.zdb_id: 1475751-5
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  • 9
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    Spicamycin and KRN5500 Induce Apoptosis in Myeloid and Lymphoid Cell Lines with Down-regulation of Bcl-2 Expression and Modulation of Promyelocytic Leukemia Protein
    Wiley ; 2000
    In:  Japanese Journal of Cancer Research Vol. 91, No. 6 ( 2000-06), p. 604-611
    Details
    In: Japanese Journal of Cancer Research, Wiley, Vol. 91, No. 6 ( 2000-06), p. 604-611
    Type of Medium: Online Resource
    ISSN: 0910-5050
    URL: Issue
    URL: Article
    DOI: 10.1111/cas.2000.91.issue-6
    DOI: 10.1111/j.1349-7006.2000.tb00988.x
    Language: English
    Publisher: Wiley
    Publication Date: 2000
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  • 10
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    Role for Interleukin-6 and Insulin like Growth Factor-I Via PI3-K/Akt Pathway in the Proliferation of CD56-Negative and Positive Multiple Myeloma Cells.
    American Society of Hematology ; 2004
    In:  Blood Vol. 104, No. 11 ( 2004-11-16), p. 3365-3365
    Details
    In: Blood, American Society of Hematology, Vol. 104, No. 11 ( 2004-11-16), p. 3365-3365
    Abstract: Several studies including ours have suggested that lack of CD56 expression in multiple myeloma (MM) defines a unique patient subset with poorer prognosis. However, the mechanism underlying this aggressive behavior of CD56− MM has not been well elucidated. In this study, we sorted out both CD56− and CD56+ fractions from MM cell lines or patients with MM, and investigated their different responsiveness to interleukin-6 (IL-6) or insulin like growth factor-I (IGF-I), and tried to clarify the course of action in cell cycle distribution. After stained with PE-CD56, CD56− and CD56+ fractions in KMS-21-BM and U-266 cell lines were isolated by the cell sorter, and cultured separately either in the presence or absence of IL-6 (2 ng/ml and 10 ng/ml, respectively). Although CD56− cells in both KMS-21-BM and U-266 cell lines responded significantly to IL-6 (P=0.001 and 0.009, respectively), CD56+ cells did not. Ki-67+ cells in CD56− KMS-21-BM cells, that were significantly fewer than that in CD56+ ones (P=0.0003), increased significantly upon 24-hour incubation with IL-6 (P 〈 0.0001). Western blotting analysis showed that the level of cyclin D1 and p27 protein in CD56− KMS-21-BM cells were up- and down-regulated by IL-6 in a time dependent manner, respectively. IL-6 also brought phosphorylation of Akt (ser473) in the CD56− cells. LY-294002 completely blocked these effects of IL-6. On the other hand, Ki-67+ cells in the CD56+ cells did not respond to IL-6. Although IGF-I did not increase Ki-67+ cells either in the CD56− and CD56+ cells from KMS-21-BM, anti-IGF-I mAb significantly reduced Ki-67+ cells only in the CD56+ cells (P=0.006). IGF-I up-regulated the level of cyclin D1 and phosphorylated Akt in CD56+ KMS-21-BM cells. LY294002 completely blocked these effects of IGF-I. Same results were obtained in the analysis of U-266 cell lines. The MM cells sorted from 17 patients with MM were also examined for CD56 and Ki-67 expression. Four and 13 patients were distributed to the CD56− and CD56+ group, respectively. These MM cells from the patients were cultured with or without IL-6 (10 ng/ml) or IGF-I (500ng/ml) for 24 hours. IL-6 increased the percentage of Ki-67+ cells in the CD56− group more than those in the CD56+ group (P=0.007). Although MM cells did not respond to IL-6, IGF-I significantly increased Ki-67+ cells in the CD56+ group (P=0.005). These results suggest that CD56− and CD56+ MM cells could be stimulated by different cytokines. We here found that CD56− MM cells were proliferated more than CD56+ MM cells in the presence of IL-6, and that this effect of IL-6 was mainly mediated by the activation of PI3-K/Akt pathway. In addition, our results suggest that IGF-I play an important role in the proliferation of CD56+ MM cells via PI3-K/Akt pathway.
    Type of Medium: Online Resource
    ISSN: 0006-4971 , 1528-0020
    URL: Article
    DOI: 10.1182/blood.V104.11.3365.3365
    RVK:
    XA 33000
    RVK:
    XA 10000
    Language: English
    Publisher: American Society of Hematology
    Publication Date: 2004
    detail.hit.zdb_id: 1468538-3
    detail.hit.zdb_id: 80069-7
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