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Fisciano, Italy

Gupta N.,Fortis Hospital | Sanchety N.,Fortis Hospital | Verma P.S.,Fortis Hospital | Verma G.,srl
Indian Journal of Pathology and Microbiology | Year: 2015

Malignant granular cell tumor (MGCT) is rare tumors that comprise 1-2% of all granular cell tumors. They commonly arise on lower extremity, nuchal region, chest wall, gastrointestinal tract, head, and neck but very rarely in breast. We report a case of a MGCT of breast with review of literature. The patient had noticed a breast mass 4 years back which was operated, and wide local excision was done. The tumor was diagnosed as MGCT. The tumor fulfilled 3 of the 6 criteria of Fanburg-Smith et al. The patient received 8 cycles of chemotherapy thereafter with 4 cycles of antharacycline and 4 of taxanes. However, the tumor reoccurred 4 years after resection and grew rapidly. Contrast-enhanced computed tomography done showed a large lobulated breast mass with axillary lymph node metastasis. She underwent Modified Radical Mastectomy with axillary clearance. The histopathology this time also revealed similar malignant tumor. To the best of our knowledge, only 7 cases have been reported in indexed English literature occurring primarily in breast. Source

Basile A.,University of Salerno | Basile A.,srl | Pascale M.,University of Salerno | Pascale M.,srl | And 7 more authors.
Journal of Cellular Physiology | Year: 2012

Cystic fibrosis transmembrane conductance regulator (CFTR) is a cAMP-dependent Cl- channel located in the plasma membrane, and its malfunction results in cystic fibrosis (CF), the most common lethal genetic disease in Caucasians. Most CF patients carry the deletion of Phe508 (ΔF508 mutation); this mutation prevents the delivery of the CFTR to its correct cellular location, the apical (lumen-facing) membrane of epithelial cells. Molecular chaperones play a central role in determining the fate of ΔF508-CFTR. In this report, we show that the Matrine, a quinolizidine alkaloid, downregulates the expression of the molecular chaperone HSC70 and increases the protein levels of ΔF508-CFTR in human alveolar basal epithelial cells (A549 cell line), stably transfected with a ΔF508-CFTR-expressing construct. Moreover, Matrine induced ΔF508-CFTR release from endoplasmic reticulum to cell cytosol and its localization on the cell membrane. Interestingly, downregulation of HSC70 resulted in increased levels of ΔF508-CFTR complexes with the co-chaperone BAG3 that in addition appeared to co-localize with the mutated protein on the cell surface. These results shed new light on ΔF508-CFTR interactions with proteins of the chaperones/co-chaperones system and could be useful in strategies for future medical treatments for CF. © 2011 Wiley Periodicals, Inc. Source

Konishi Y.,srl | Hayashi H.,srl | Suzuki H.,Sapporo Medical University | Yamamoto E.,Sapporo Medical University | And 2 more authors.
Analytical Biochemistry | Year: 2015

Quantifying levels of DNA methylation in tumors is a useful approach for the identification of potential tumor suppressors and to find biomarkers that can be used as prognostic or therapeutic indicators. In the current study, we compared three methods commonly used for quantifying DNA methylation - bisulfite pyrosequencing, quantitative methylation-specific PCR (Q-MSP), and MethyLight - by focusing on the CpG island of the gene encoding the microRNA-34b and microRNA-34c (miR-34b/c); aberrant regulation of this miR is associated with various human malignancies, including gastric cancer. Standard curve analysis using control DNA samples demonstrated the highest quantitative accuracy in Q-MSP analysis. We also carried out methylation analysis using gastric mucosa specimens obtained from gastric cancer patients. We found a high correlation between methylation levels determined by Q-MSP and those determined by MethyLight (R2 = 0.952), whereas the results of bisulfite pyrosequencing and the other two methods were less well correlated (R2 = 0.864 and R2 = 0.804 for Q-MSP and MethyLight, respectively). This may reflect possible PCR bias in the pyrosequencing technique, which we show can be corrected for by applying a cubic approximate equation to the original data. Thus, although results obtained by the different DNA methylation analysis techniques are largely comparable, an appropriate correction may be necessary for stringent comparison. © 2015 Elsevier Inc. All rights reserved. Source

Rosati A.,University of Salerno | Rosati A.,srl | Graziano V.,University of Chieti Pescara | De Laurenzi V.,srl | And 5 more authors.
Cell Death and Disease | Year: 2011

Bcl2-associated athanogene 3 (BAG3) protein is a member of BAG family of co-chaperones that interacts with the ATPase domain of the heat shock protein (Hsp) 70 through BAG domain (110-124 amino acids). BAG3 is the only member of the family to be induced by stressful stimuli, mainly through the activity of heat shock factor 1 on bag3 gene promoter. In addition to the BAG domain, BAG3 contains also a WW domain and a proline-rich (PXXP) repeat, that mediate binding to partners different from Hsp70. These multifaceted interactions underlie BAG3 ability to modulate major biological processes, that is, apoptosis, development, cytoskeleton organization and autophagy, thereby mediating cell adaptive responses to stressful stimuli. In normal cells, BAG3 is constitutively present in a very few cell types, including cardiomyocytes and skeletal muscle cells, in which the protein appears to contribute to cell resistance to mechanical stress. A growing body of evidence indicate that BAG3 is instead expressed in several tumor types. In different tumor contexts, BAG3 protein was reported to sustain cell survival, resistance to therapy, and/or motility and metastatization. In some tumor types, down-modulation of BAG3 levels was shown, as a proof-of-principle, to inhibit neoplastic cell growth in animal models. This review attempts to outline the emerging mechanisms that can underlie some of the biological activities of the protein, focusing on implications in tumor progression. © 2011 Macmillan Publishers Limited All rights reserved. Source

Basile A.,University of Salerno | Basile A.,srl | Zeppa R.,University of Salerno | Pasquino N.,University of Naples Federico II | And 12 more authors.
Journal of Cellular Physiology | Year: 2011

The expression of the anti-apoptotic protein BAG3 is induced in several cell types by exposure to high temperature, oxidants, and other stressful agents. We investigated whether exposure to 50Hz electromagnetic fields raised BAG3 levels in the human melanoma cell line M14, in vitro and in orthotopic xenografts. Exposure of cultured cells or xenografts for 6h or 4 weeks, respectively, produced a significant (P<0.01) increase in BAG3 protein amounts. Interestingly, at the same times, we could not detect any significant variation in the levels of HSP70/72 protein or cell apoptosis. These results confirm the stressful effect of exposure to ELF in human cells, by identifying BAG3 protein as a marker of ELF-induced stress. Furthermore, they suggest that BAG3 induction by ELF may contribute to melanoma cell survival and/or resistance to therapy. © 2011 Wiley-Liss, Inc. Source

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