PKCδ-mediated phosphorylation of BAG3 at Ser187 site induces epithelial−mesenchymal transition and enhances invasiveness in thyroid cancer FRO cells

N, Li; Zx, Du; Zong, Zhi‐Hong; Bq, Liu; C, Li; Q, Zhang; Hq, Wang

doi:10.1038/onc.2012.466

Cited by 38 publications

(36 citation statements)

References 43 publications

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“…Enhanced FRO cell migration through phosphorylation of Bcl-2 associated athanogene 3 (BAG3) was also observed in some cases [498,499].…”

Section: Thyroidmentioning

confidence: 93%

Protein Kinase C (PKC) Isozymes and Cancer

Kang

2014

New Journal of Science

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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.

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“…Enhanced FRO cell migration through phosphorylation of Bcl-2 associated athanogene 3 (BAG3) was also observed in some cases [498,499].…”

Section: Thyroidmentioning

confidence: 93%

Protein Kinase C (PKC) Isozymes and Cancer

Kang

2014

New Journal of Science

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“…Importantly, BAG3 function and levels can also be regulated by posttranslational modification. For example, phosphorylation of Ser187 of BAG3 by protein kinase C delta (PKCΔ) leads to increased epithelial-mesenchymal transition, motility and invasiveness of cancer cells [69, 70]. Expression of exogenous Tat, a protein expressed by the HIV virus, in glioblastoma cell lines enhances BAG3 protein but not mRNA levels [71].…”

Section: Bag3 Mutants Myofibrillar Myopathy and Dilated Cardiomyopathymentioning

confidence: 99%

BAG3: a new player in the heart failure paradigm

et al. 2015

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BAG3 is a cellular protein that is expressed predominantly in skeletal and cardiac muscle but can also be found in the brain and in the peripheral nervous system. BAG3 functions in the cell include: serving as a co-chaperone with members of the heat-shock protein family of proteins to facilitate the removal of misfolded and degraded proteins, inhibiting apoptosis by interacting with Bcl2 and maintaining the structural integrity of the Z-disk in muscle by binding with CapZ. The importance of BAG3 in the homeostasis of myocytes and its role in the development of heart failure was evidenced by the finding that single allelic mutations in BAG3 were associated with familial dilated cardiomyopathy. Furthermore, significant decreases in the level of BAG3 have been found in end-stage failing human heart and in animal models of heart failure including mice with heart failure secondary to trans-aortic banding and in pigs after myocardial infarction. Thus, it becomes relevant to understand the cellular biology and molecular regulation of BAG3 expression in order to design new therapies for the treatment of patients with both hereditary and non-hereditary forms of dilated cardiomyopathy.

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“…In embryonic tissues, it is reported that HMGA2 plays an important role in triggering embryonic cardiogenesis [8] and activating the self-renewal in peripheral neural system [9], by which HMGA2 modulates stem cell proliferaiton and differentiation. Most importantly, HMGA2 is demonstrated to be highly expressed in most tumors [10,11] and portends a poor prognosis for cancer patients like lung cancer [12], oral squamous cell carcinoma [13,14], and breast cancer [15]. However, it is not clear whether HMGA2 overexpression is related with the progression of EOC.…”

Section: Introductionmentioning

confidence: 96%

The critical role of HMGA2 in regulation of EMT in epithelial ovarian carcinomas

et al. 2015

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The high mobility group A2 (HMGA2), an oncofetal protein, was shown to play a role in tumor development and progression. However, the molecular and clinical role of HMGA2 in epithelial ovarian carcinomas (EOCs) is still unknown. In the present study, EOC cell line SKOV3 was subjected to in vitro assays. Here, our findings showed that HMGA2 was highly expressed in EOC cell line SKOV3. HMGA2 knockdown promoted cell apoptosis and the cleavage of caspase 3, and decreased the B cell lymphoma 2 (Bcl-2)/Bax ratio in SKOV3. Functionally, HMGA2 knockdown resulted in reduction of SKOV3 cell migration and invasion. Mechanically, HMGA2 knockdown affected the occurrence of EMT by increasing E-cadherin gene and protein expression and decreasing the gene and protein expression of N-cadherin, slug, and vimentin. At the same time, HMGA2 also repressed the expression of matrix metalloproteinase 2 (MMP2) and matrix metalloproteinase 9 (MMP9), which was consistent with the decreased invasion capacity. In conclusion, HMGA2 is associated with migration and invasiveness and regulates the progression of EMT in the development of EOC, and HMGA2 gene and protein may be a novel therapeutic target against EOC in the clinical practice.

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PKCδ-mediated phosphorylation of BAG3 at Ser187 site induces epithelial−mesenchymal transition and enhances invasiveness in thyroid cancer FRO cells

Cited by 38 publications

References 43 publications

Protein Kinase C (PKC) Isozymes and Cancer

Protein Kinase C (PKC) Isozymes and Cancer

BAG3: a new player in the heart failure paradigm

The critical role of HMGA2 in regulation of EMT in epithelial ovarian carcinomas

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