Role of Protein Kinase C Isoforms in Phorbol Ester-induced Vascular Endothelial Growth Factor Expression in Human Glioblastoma Cells

Shih, Shu Ching; Mullen, Andrew R.; Abrams, Kristin; Mukhopadhyay, Debabrata; Claffey, Kevin P.

doi:10.1074/jbc.274.22.15407

Cited by 98 publications

(88 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Phosphorothioate derivatives of antisense and sense oligonucleotides of PKC were designed against the translation start site of the PKC isoform (Shih et al, 1999) and obtained from GenoTech (Taejon, Korea). For transient transfection with the antisense oligonucleotides, about 1 × 10 5 BEAS-2B cells were Figure 1.…”

Section: Transfection With Antisense Pkcα Oligonucleotidesmentioning

confidence: 99%

PMA-induced up-regulation of MMP-9 is regulated by a PKCα-NF-κB cascade in human lung epithelial cells

Shin

Yoon²,

Choe³

et al. 2007

Exp Mol Med

View full text Add to dashboard Cite

Expression of matrix metalloproteinase-9 (MMP-9) is associated with airway remodeling and tissue injury in asthma. However, little is known about how MMP-9 is up-regulated in airway epithelial cells. In this study, we show that phorbol myristate acetate (PMA) induces MMP-9 expression via a protein kinase Cα (PKCα)-dependent signaling cascade in BEAS-2B human lung epithelial cells. Pretreatment with either GF109203X, a general PKC inhibitor, or Gö6976, a PKCα/β isozyme inhibitor, inhibited PMA-induced activation of the MMP-9 promoter, as did transient transfection with PKCα antisense oligonuclotides. PMA activated NF-κB by phosphorylating IκB in these cells and this was also inhibited by GF109203X and Gö6976, suggesting that PKCα acts as an upstream regulator of NF-κB in PMA-induced MMP-9 induction. Our results indicate that a "PKCα-NF-κB"-dependent cascade is involved in the signaling leading to PMA-induced MMP-9 expression in the lung epithelium.

show abstract

Section: Transfection With Antisense Pkcα Oligonucleotidesmentioning

confidence: 99%

PMA-induced up-regulation of MMP-9 is regulated by a PKCα-NF-κB cascade in human lung epithelial cells

Shin

Yoon²,

Choe³

et al. 2007

Exp Mol Med

View full text Add to dashboard Cite

show abstract

“…A construct containing the VEGF promoter containing 1.5 kb from Ϫ1226 to ϩ298 with respect to the transcription start site was followed by a luciferase reporter gene (Shih et al, 1999). The vector was transfected into 80% confluent Balb/c 3T3 cells using Lipofectamine (Gibco/ BRL) reagent, according to the manufacturer's instructions, for 6 hours followed by 16 hours' recovery in complete media.…”

Section: Cell Culture Conditions Cytokine Treatment and Transient Tmentioning

confidence: 99%

“…RNA isolation and Northern blot analyses were performed as described previously (Shih et al, 1999). Probes used were the mouse VEGF cDNA (Claffey et al, 1992) and the ribosome associated protein, 36B4, as control (Masiakowski et al, 1982).…”

Section: Rna Isolation and Northern Blot Analysismentioning

confidence: 99%

“…Transient transfection analysis of VEGF-dependent transcription in Balb/c 3T3 cells was performed as described previously (Shih et al, 1999). A construct containing the VEGF promoter containing 1.5 kb from Ϫ1226 to ϩ298 with respect to the transcription start site was followed by a luciferase reporter gene (Shih et al, 1999).…”

Section: Cell Culture Conditions Cytokine Treatment and Transient Tmentioning

confidence: 99%

“…Neovascularization was confirmed with immunohistochemical analysis with antimouse collagen type IV (Biodesign International, Kennebunk, Maine) to stain basement membrane or antimouse PECAM-1 (PharMingen, San Diego, California), which stains neovascular and precursor endothelial cells (DeLisser et al, 1997). A chicken anti-hVEGF 165 polyclonal antibody, described previously (Shih et al, 1999), was used to detect mouse VEGF with immunohistochemistry. In situ hybridization was performed for mouse VEGF and VEGF receptors, flk-1(KDR/VEGF-R2), and flt-1(VEGF-R1), as described previously .…”

Section: Matrigel Angiogenesis In Athymic Nude Micementioning

confidence: 99%

See 2 more Smart Citations

Fibroblast Growth Factor 2 Activation of Stromal Cell Vascular Endothelial Growth Factor Expression and Angiogenesis

Claffey

Abrams²,

Shih

et al. 2001

Laboratory Investigation

Self Cite

View full text Add to dashboard Cite

Fibroblast growth factor-2 (FGF-2) increases N-cadherin expression through protein kinase C and Src-kinase pathways in human calvaria osteoblasts

et al. 2001

View full text Add to dashboard Cite

Fibroblast growth factors (FGFs) are important factors regulating osteogenesis. However, the early mechanisms and signaling pathways involved in FGF actions in osteoblasts are unknown. We investigated the effects of FGF-2 on cell-cell adhesion and cadherin expression and the underlying signaling pathways in immortalized human neonatal calvaria (IHNC) cells. These cells express E- and N-cadherins, as shown by immunocytochemical and Western blot analyses. rhFGF-2 increased cell-cell adhesion at 24-72 h, as measured in a cell aggregation assay, and this effect was blocked by specific neutralizing anti-N-cadherin, but not anti-E-cadherin antibodies. Accordingly, ELISA and Western blot analyses showed that rhFGF-2 (10-100 ng/ml) dose dependently increased N-cadherin but not E-cadherin protein levels. RT-PCR analysis showed that rhFGF-2 transiently increased N-cadherin mRNA levels in IHNC cells. The RNA polymerase II inhibitor 5,6-dichloro-1-beta-D-ribofuranosyl benzimidazole prevented the rhFGF-2-induced up-regulation of N-cadherin mRNA, suggesting that transcription is necessary for this effect. Analysis of signaling molecules showed evidence that PLCgamma-PKC, Src, Erk 1/2 and p38 MAPK pathways are activated by rhFGF-2 in IHNC cells. The selective PKC inhibitors calphostin C, Ro-31-8220, Gö6976 and Gö6983 abrogated the stimulatory effect of rhFGF-2 on N-cadherin mRNA levels. The src-family tyrosine kinase inhibitor PP1 also blocked rhFGF-2-promoted N-cadherin expression. In contrast, the p38 MAP kinase inhibitor SB 203580 or the MEK inhibitor PD98059 had no effect on rhFGF-2-induced N-cadherin mRNA levels. Our data indicate that FGF-2 increases N-cadherin expression and function in human calvaria osteoblasts via activation of PKC and src-kinase pathways. This study identifies N-cadherin as a previously unrecognized target gene for FGF-2 signaling pathway that regulates cell-cell adhesion in human osteoblasts.

show abstract

Role of Protein Kinase C Isoforms in Phorbol Ester-induced Vascular Endothelial Growth Factor Expression in Human Glioblastoma Cells

Cited by 98 publications

References 31 publications

PMA-induced up-regulation of MMP-9 is regulated by a PKCα-NF-κB cascade in human lung epithelial cells

PMA-induced up-regulation of MMP-9 is regulated by a PKCα-NF-κB cascade in human lung epithelial cells

Fibroblast Growth Factor 2 Activation of Stromal Cell Vascular Endothelial Growth Factor Expression and Angiogenesis

Fibroblast growth factor-2 (FGF-2) increases N-cadherin expression through protein kinase C and Src-kinase pathways in human calvaria osteoblasts

Contact Info

Product

Resources

About