Activation of Protein Kinase C<i>δ</i>Induces Growth Arrest in NPA Thyroid Cancer Cells Through Extracellular Signal-Regulated Kinase Mitogen-Activated Protein Kinase

Koike, Kazuo; Fujii, Teruhiko; Nakamura, Anna; Yokoyama, Goro; Yamana, Hideaki; Kuwano, Michihiko; Shirouzu, Kazuo

doi:10.1089/thy.2006.16.333

Cited by 23 publications

(23 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In FTC-133 cells, PKC activation by PMA increased cell invasion (Hoelting et al 1997). Others, however, have found a negative correlation between PKC activation and cell proliferation in human thyroid cancer cells (Koike et al 2006, Afrasiabi et al 2008. In our study we found a higher pPKC protein expression in FTC-238 compared to FTC-133 cells.…”

Section: Discussioncontrasting

confidence: 47%

The impact of CLAUDIN-1 on follicular thyroid carcinoma aggressiveness

Zwanziger¹,

Badziong²,

Ting³

et al. 2015

Endocrine-Related Cancer

View full text Add to dashboard Cite

CLAUDIN-1 belongs to the family of transmembrane tight junction proteins tightening the paracellular cleft of epithelial cells. In human malignancies, CLAUDIN-1 is often dysregulated and located in subcellular compartments, particularly in the nucleus where it may influence cellular behaviour. Here, we studied CLAUDIN-1 in relation to the biological characteristics of follicular thyroid carcinoma (FTC). CLAUDIN-1 immuno-staining showed loss of membrane expression and increased nuclear CLAUDIN-1 localization in FTC metastases. CLAUDIN-1 function was further investigated in two different follicular thyroid carcinoma cell lines: FTC-133 isolated from a regional lymph node metastasis and FTC-238 derived from a lung metastasis. In both cell lines CLAUDIN-1 expression was demonstrated in the cell nuclei with a significantly higher protein expression in FTC-238 compared to FTC-133 cells. Interestingly, in vitro scratch assay revealed enriched nuclear CLAUDIN-1 expression near the scratch. Furthermore, the increase of the pathogenic character of FTC-133 cells by RASV12 transfection was associated with elevated CLAUDIN-1 expression and enhanced cell migration, invasion and proliferation. Likewise over-expression of nuclear CLAUDIN-1 in FTC-133 cells resulted in increased cell migration and invasion. Conversely, CLAUDIN-1 downregulation in FTC-238 cells by siRNA resulted in decreased cell migration and invasion and was accompanied by reduced phosphoPKC expression. Moreover, activation and inhibition of PKC resulted in CLAUDIN-1 up-and downregulation in FTC cells respectively. These data suggest an impact of CLAUDIN-1 on follicular thyroid carcinoma aggressiveness, which could potentially be influenced by PKC activity.

show abstract

Section: Discussioncontrasting

confidence: 47%

The impact of CLAUDIN-1 on follicular thyroid carcinoma aggressiveness

Zwanziger¹,

Badziong²,

Ting³

et al. 2015

Endocrine-Related Cancer

View full text Add to dashboard Cite

show abstract

“…Rottlerin has been reported to antagonize the growth arrest induced by PMA in thyroid cancer cells [Koike et al, 2006], to inhibit ionizing radiation-induced JNK activation in thyrocytes [Mitsutake et al, 2001], and to suppress cisplatin-provoked ERK phosphorylation in transformed thyroid cells [Urso et al, 2005]. Our study is the first to define the migration-inhibitory effects of rottlerin in thyroid cancer cells.…”

Section: Discussionmentioning

confidence: 64%

“…Since activated PKCd translocates to the cell membrane [Kikkawa et al, 2002], we prepared membrane fractions from the rottlerin and/or PMA-treated cells described below and assayed the relative abundance of active membrane-bound phospho-PKCd (pPKCd). CGTH W-2 cells were incubated with rottlerin or solvent vehicle for 0, 0.5, or 1 h before co-treatment with 200 nM PMA, a well-known activator of PKC [Koike et al, 2006]. All groups were harvested 1 h after PMA addition.…”

Section: Inhibition Of Migration By Rottlerin Is Independent Of Pkcmentioning

confidence: 99%

Rottlerin inhibits migration of follicular thyroid carcinoma cells by PKCδ‐independent destabilization of the focal adhesion complex

Lin¹,

Lin²,

Chen³

et al. 2010

J of Cellular Biochemistry

View full text Add to dashboard Cite

This study examined the effect of rottlerin on the focal adhesion-mediated cell migration of CGTH W-2 human follicular thyroid carcinoma cells. Rottlerin (10 microM) resulted in decreased adhesion of CGTH W-2 cells to matrix substance, which was correlated with metastatic potential. Rottlerin treatment also resulted in a marked reduction in the migration of CGTH W-2 cells. Protein levels of integrin beta1, FAK, and paxillin were decreased by rottlerin. Consistent with this, immunostaining of FAK, vinculin, and paxillin revealed disassembly of the focal adhesions. Disruption of actin stress fibers was noted, which was compatible with reduced expression levels and activities of Rac-1 and Rho. The effect of rottlerin on cell migration was not attributable to inhibition of PKCdelta activity since siRNA knockdown of PKCdelta did not recapitulate the effects of rottlerin on cell adhesion and migration. Furthermore, activation of PKCdelta by phorbol esters failed to restore the rottlerin-inhibited migratory ability. The mitochondrial uncoupler, carbonylcyanide-4-(trifluoromethoxy)-phenylhydrazone, was able to mimic several rottlerin's effects. In summary, we demonstrated that rottlerin inhibits the migration of CGTH W-2 cells by disassembly of focal adhesion complexes in a PKCdelta-independent manner, and might play as a mitochondrial uncoupler role in these events.

show abstract

“…Kip1 /cyclin E/pRb pathway [497] as well as antiproliferative effects in the anaplastic (FRO and ARO) and follicular (ML-1) thyroid cancer cell lines through MAPK/Akt and FOXO signaling [498]. Enhanced FRO cell migration through phosphorylation of Bcl-2 associated athanogene 3 (BAG3) was also observed in some cases [498,499].…”

Section: Thyroidmentioning

confidence: 99%

Protein Kinase C (PKC) Isozymes and Cancer

Kang

2014

New Journal of Science

View full text Add to dashboard Cite

Protein kinase C (PKC) is a family of phospholipid-dependent serine/threonine kinases, which can be further classified into three PKC isozymes subfamilies: conventional or classic, novel or nonclassic, and atypical. PKC isozymes are known to be involved in cell proliferation, survival, invasion, migration, apoptosis, angiogenesis, and drug resistance. Because of their key roles in cell signaling, PKC isozymes also have the potential to be promising therapeutic targets for several diseases, such as cardiovascular diseases, immune and inflammatory diseases, neurological diseases, metabolic disorders, and multiple types of cancer. This review primarily focuses on the activation, mechanism, and function of PKC isozymes during cancer development and progression.

show abstract

Activation of Protein Kinase CδInduces Growth Arrest in NPA Thyroid Cancer Cells Through Extracellular Signal-Regulated Kinase Mitogen-Activated Protein Kinase

Cited by 23 publications

References 36 publications

The impact of CLAUDIN-1 on follicular thyroid carcinoma aggressiveness

The impact of CLAUDIN-1 on follicular thyroid carcinoma aggressiveness

Rottlerin inhibits migration of follicular thyroid carcinoma cells by PKCδ‐independent destabilization of the focal adhesion complex

Protein Kinase C (PKC) Isozymes and Cancer

Contact Info

Product

Resources

About