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Article type: Cover
1999 Volume 30 Issue 4 Pages
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Article type: Cover
1999 Volume 30 Issue 4 Pages
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Akio NOGUCHI
Article type: Article
1999 Volume 30 Issue 4 Pages
471-484
Published: December 31, 1999
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Cells exogenously expressing p16^<INK4a> reduce proliferative activity by suppressing cyclin dependent kinase activity. However it remains unclear how phenotypic changes are associated with exogenous p16 expression. The human glioblastoma cell line U87MG was doubly transfected with plasmids pVgRXR and pIND horboring the wild-type p16 gene. The cells that express p16 protein in an eckdysoneinducible manner were used in this study. Phenotypic changes of cell characteristics associated with p16 expression such as cell shapes and cell adhesion on extracellular matrix (ECM) proteins were studied microscopically. Furthermore, the cell responses for extra-cellular growth stimuli such as EGF were also studied. In this study, changes in cell characteristics were observed as follows ; (1) The cells expressing p16 protein became larger and flatter than p16-negative cells; (2) these p16 protein showed an increased formation of actin-stress fibers, a finding assessed by TRITC-labeled phalloidin staining and vinculin accumulation in the focal adhesion contacts ; (3) cell adhesion to ECM proteins such as laminin, fibronectin, and type IV collagen significantly increased, and an increased expression of integrin α5 and αv was observed in the p16 positive cell, and p16 expression was also associated with a decrease in Rac protein ; (4) phosphorylation of ERK and expression of c-fos following the of EGF-stimulation was significantly reduced in the p16 positive cell, compared with that of p16-negative cells. The results suggest that the deletion or mutation of p16 gene during malignant progression of glioma may induce histopathological changes since changes in integrins may modulate cell adhesion and crosstalk between various surrounding cells and tumor cells in vivo. Additionally, mutational change in the p16 gene may result in an increased response to extracellular growth stimuli such as EGF.
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Nobuyuki ITOH
Article type: Article
1999 Volume 30 Issue 4 Pages
485-496
Published: December 31, 1999
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Sodium butyrate (NaBu) has been shown to arrest the cell-cycle in the G1 phase and cellular differentiation in many cell lines. However, the molecular mechanisms of this remain to be clarified. In this communication, the effects of NaBu on cell proliferation and invasiveness in extracellular matrix proteins, such as fibronectin and laminin, were examined using cultured human glioma cell lines. The changes of cell-cycle regulatory proteins induced by the addition of NaBu were studied. In addition, morphological changes including actin organization by NaBu were also studied. This study shows that 1) NaBu reduced cell proliferation and invasiveness, 2) NaBu increased the expression of p21 (WAF1), 3) the increased expression of p21 (WAF1) may be independent of the p53 gene status, and 4) actin-stress fibers are increased by NaBu and these changes in F-actin distribution may correlate to reduced invasiveness of human glioma cells. These results suggest that NaBu is a promising candidate compound for treating patients with malignant gliomas.
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Article type: Appendix
1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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Article type: Article
1999 Volume 30 Issue 4 Pages
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Article type: Article
1999 Volume 30 Issue 4 Pages
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Article type: Article
1999 Volume 30 Issue 4 Pages
499-500
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Article type: Article
1999 Volume 30 Issue 4 Pages
500-
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Article type: Article
1999 Volume 30 Issue 4 Pages
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Article type: Article
1999 Volume 30 Issue 4 Pages
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Article type: Article
1999 Volume 30 Issue 4 Pages
500-501
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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Article type: Article
1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
507-508
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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1999 Volume 30 Issue 4 Pages
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