Intramuscular hemangioma originated in chest wall is a rare benign tumor, with no relevant reports in Korea. In most cases, the tumor is discovered before the age of 30 years and it is reported that trauma operates as the initiation factor. It is essential to concern the clinical suspicion and conduct a CT scan for diagnosis. The principle of treatment is surgical excision with clear resection margin. The authors of this study report a case of surgical excision for post-traumatic intramuscular hemangioma of the chest wall with review of literature.
Hemangioma ; Korea ; Peptide Initiation Factors ; Thoracic Wall ; Thorax

High glucose leads to physio/pathological alterations in diabetes patients. We investigated collagen production in human gingival cells that were cultured in high concentrations of glucose. Collagen synthesis and secretion were increased when the cells were exposed to high concentrations of glucose. We examined endoplasmic reticulum (ER) stress response because glucose metabolism is related to ER functional status. An ER stress response including the expression of glucose regulated protein 78 (GRP78), C/EBP homologous protein (CHOP), inositol requiring enzyme alpha (IRE-1alpha) and phosphoreukaryotic initiation factor alpha (p-eIF-2alpha) was activated in the presence of high glucose. Activating transcription factor 4 (ATF-4), a downstream protein of p-eIF-2alpha as well as a transcription factor for collagen, was also phosphorylated and translocalized into the nucleus. The chemical chaperone 4-PBA inhibited the ER stress response and ATF-4 phosphorylation as well as nuclear translocation. Our results suggest that high concentrations of glucose-induced collagen are linked to ER stress and the associated phosphorylation and nuclear translocation of ATF-4.
Activating Transcription Factor 4 ; Butylamines ; Collagen ; Endoplasmic Reticulum ; Fibroblasts ; Glucose ; Humans ; Inositol ; Peptide Initiation Factors ; Phenylbutyrates ; Phosphorylation ; Transcription Factors

OBJECTIVETo detect the expression of eukaryotic translation initiation factor 5A2(EIF5A2) in pancreatic adenocarcinoma and its correlation with the clinicopathological characteristics and prognosis.

METHODSA total of 73 patients who were treated in our hospital from March 2007 to December 2008 were enrolled in this study. The expression of EIF5A2 in the surgical samples was detected using immunohistochemical staining. Complete clinicopathological data were obtained from all the patients. The potential correlation between EIF5A2 expression and the clinicopathological features, particularly its role in prognosis, were analyzed.

RESULTSOf these 73 patients, 43 had a high EIF5A2 expression. EIF5A2 expression was significantly correlated with the pathological T stage(P<0.001), N stage(P=0.004), M stage(P=0.039), and TNM stage(P=0.005). Kaplan-Meier method demonstrated that the survival was significantly longer in the low EIF5A2 expression group than in the high EIF5A2 expression group(P=0.003). Cox's hazard model showed EIF5A2 was a significant predictor of overall survival in patients with pancreatic adenocarcinoma.

CONCLUSIONEIF5A2 may be a potential predictor of the poor prognosis in patients with pancreatic adenocarcinoma.

Adenocarcinoma ; diagnosis ; metabolism ; Humans ; Neoplasm Staging ; Pancreatic Neoplasms ; diagnosis ; metabolism ; Peptide Initiation Factors ; metabolism ; Prognosis ; RNA-Binding Proteins ; metabolism

Due to advances in omics technologies, numerous genome-wide studies on human samples have been published, and most of the omics data with the associated clinical information are available in public repositories, such as Gene Expression Omnibus and ArrayExpress. While analyzing several public datasets, we observed that errors in gender information occur quite often in public datasets. When we analyzed the gender description and the methylation patterns of gender-specific probes (glucose-6-phosphate dehydrogenase [G6PD], ephrin-B1 [EFNB1], and testis specific protein, Y-linked 2 [TSPY2]) in 5,611 samples produced using Infinium 450K HumanMethylation arrays, we found that 19 samples from 7 datasets were erroneously described. We also analyzed 1,819 samples produced using the Affymetrix U133Plus2 array using several gender-specific genes (X (inactive)-specific transcript [XIST], eukaryotic translation initiation factor 1A, Y-linked [EIF1AY], and DEAD [Asp-Glu-Ala-Asp] box polypeptide 3, Y-linked [DDDX3Y]) and found that 40 samples from 3 datasets were erroneously described. We suggest that the users of public datasets should not expect that the data are error-free and, whenever possible, that they should check the consistency of the data.
Dataset* ; DNA Methylation ; Ephrin-B1 ; Gender Identity ; Gene Expression ; Humans ; Methylation ; Microarray Analysis ; Oxidoreductases ; Peptide Initiation Factors ; Testis

BACKGROUND: beta-cell death due to endoplasmic reticulum (ER) stress has been regarded as an important pathogenic component of type 2 diabetes. The possibility has been suggested that sulfonylurea, currently being used as one of the main oral hypoglycemic agents of type 2 diabetes, increases ER stress, which could lead to sulfonylurea failure. The authors of the present study examined ER stress of beta-cells in a glucolipotoxic condition using glyburide (GB) in an environment mimicking type 2 diabetes. METHODS: Apoptosis was induced by adding various concentrations of GB (0.001 to 200 microM) to a glucolipotoxic condition using 33 mM glucose, and the effects of varied concentrations of palmitate were evaluated via annexin V staining. The markers of ER stress and pro-apoptotic markers were assessed by Western blotting and semi-quantitative reverse transcription-polymerase chain reaction. Additionally, the anti-apoptotic markers were evaluated. RESULTS: Addition of any concentration of GB in 150 microM palmitate and 33 mM glucose did not increase apoptosis. The expression of phosphorylated eukaryotic initiation factor (eIF-2alpha) was increased and cleaved caspase 3 was decreased by adding GB to a glucolipotoxic condition. However, other ER stress-associated markers such as Bip-1, X-box binding protein-1, ATF-4 and C/EBP-homologous protein transcription factor and anti-apoptotic markers phosphor-p85 phosphatidylinositol 3-kinase and phosphorylation of Akt did not change significantly. CONCLUSION: GB did not show further deleterious effects on the degree of apoptosis or ER stress of INS-1 cells in a glucolipotoxic condition. Increased phosphorylation of eIF-2alpha may attenuate ER stress for adaptation to increased ER protein load.
Annexin A5 ; Apoptosis ; Blotting, Western ; Caspase 3 ; Endoplasmic Reticulum ; Endoplasmic Reticulum Stress ; Eukaryotic Initiation Factor-2 ; Glucose ; Glyburide ; Hypoglycemic Agents ; Insulin-Secreting Cells ; Peptide Initiation Factors ; Phosphatidylinositol 3-Kinase ; Phosphorylation ; Transcription Factors

PURPOSE: The pathophysiological mechanisms of the bladder dysfunction in postmenopausal state are not well understood especially in moleclular level. Therefore we investigated the changes of bladder in female rat following bilateral ovariectomy by proteomic approach. MATERIALS AND METHODS: A total 10 female Sprague-Dawley rats were obtained at 8 weeks of age and randomly divided into 2 groups in each 5 rats; sham operation group as the control group and the bilateral ovariectomy group. Whole urinary bladders of the rats were excised 4 weeks after the beginning of the experiment. Conventional proteomics was performed with high resolution 2-D gel electrophoresis followed by computational image analysis and protein identification using mass spectrometry. RESULTS: Bladder weight was not changed by oophorectomy. A comparison of bladder of ovariectomy group with control showed that 8 proteins; Eukaryotic translation initiation factor 5A was over-expressed, and chaperone grp 75 precursor, guanine deaminase, keratin complex 2, Gelsolin precursor, peroxiredoxin 2, Enol protein and contrapsin-like inhibitor 1 precursor were under-expressed in the oophorectomy group. CONCLUSION: These data suggested that the bilateral oophorectomy might make a bladder to have a cellular apoptosis and a change of contractility in the rat bladder. However more information is needed in human bladder tissue for clinical usage and long-term proteomic changes are needed.
Animals ; Apoptosis ; Electrophoresis, Gel, Two-Dimensional ; Female ; Female* ; Gelsolin ; Guanine Deaminase ; Humans ; Mass Spectrometry ; Ovariectomy* ; Peptide Initiation Factors ; Peroxiredoxins ; Proteomics ; Rats* ; Rats, Sprague-Dawley ; Urinary Bladder*

Identifying a target molecule that is crucially involved in pancreatic tumor growth and metastasis is necessary in developing an effective treatment. The study aimed to investigate the role of the eukaryotic translation initiation factor 3a (eIF3a) in the cell proliferation and motility in pancreatic cancer. Our data showed that the expression of eIF3a was upregulated in pancreatic ductal adenocarcinoma as compared with its expression in normal pancreatic tissues. Knockdown of eIF3a by a specific shRNA caused significant decreases in cell proliferation and clonogenic abilities in pancreatic cancer SW1990 and Capan-1 cells. Consistently, the pancreatic cancer cell growth rates were also impaired in xenotransplanted mice. Moreover, wound-healing assay showed that depletion of eIF3a significantly slowed down the wound recovery processes in SW1990 and Capan-1 cells. Transwell migration and invasion assays further showed that cell migration and invasion abilities were significantly inhibited by knockdown of eIF3a in SW1990 and Capan-1 cells. Statistical analysis of eIF3a expression in 140 cases of pancreatic ductal adenocarcinoma samples revealed that eIF3a expression was significantly associated with tumor metastasis and TNM staging. These analyses suggest that eIF3a contributes to cell proliferation and motility in pancreatic ductal adenocarcinoma.
Adenocarcinoma ; Animals ; Cell Movement ; Cell Proliferation* ; Mice ; Neoplasm Metastasis ; Neoplasm Staging ; Pancreatic Ducts ; Pancreatic Neoplasms* ; Peptide Initiation Factors* ; RNA, Small Interfering ; Wounds and Injuries

Viruses initiate a number of cellular stress responses and modulate gene regulation and compartmentalization of RNA upon infection to be successful parasites. Virus infections may induce or impair stress granule (SG) formation to maximize replication efficiency. SGs and processing bodies (PBs) are the RNA granules, which contain translationally inactive pool of transcripts as the mRNA silencing foci. PBs and SGs, the highly conserved macromolecular aggregates, can release mRNAs to allow their translations. Unlike constitutively existing PBs that can respond to stimuli and affect mRNA translation and decay, SGs are specifically induced upon cellular stress and can triggers a global translational silencing by several pathways, including phosphorylation of the key translation initiation factor eIF2alpha, tRNA cleavage, and sequestration of cellular components and so on. The dynamics of PBs and SGs are regulated by several signaling pathways, including histone deacetylase 6, and depend on microfilaments and microtubules, and the cognate molecular motors myosin, dynein, and kinesin. SGs share features with aggresomes and related aggregates of unfolded proteins and may play a role in the pathology. The recent advances in understanding the relationship between viruses and mRNA stress granules are summarized.
Actin Cytoskeleton ; Dyneins ; Histone Deacetylases ; Kinesin ; Microtubules ; Myosins ; Parasites ; Peptide Initiation Factors ; Phosphorylation ; Protein Biosynthesis ; Proteins ; RNA ; RNA, Messenger ; RNA, Transfer ; Translations ; Viruses

BACKGROUNDHypertrophic scar is one of the most common complications and often causes the disfigurement or deformity in burn or trauma patients. Therapeutic methods on hypertrophic scar treatment have limitations due to the poor understanding of mechanisms of hypertrophic scar formation. To throw light on the molecular mechanism of hypertrophic scar formation will definitely improve the outcome of the treatment. This study aimed to illustrate the negative role of eukaryotic initiation factor 6 (eIF6) in the process of human hypertrophic scar formation, and provide a possible indicator of hypertrophic scar treatment and a potential target molecule for hypertrophic scar.

METHODSIn the present study, we investigated the protein expression of eIF6 in the human hypertrophic scar of different periods by immunohistochemistry and Western blot analysis.

RESULTSIn the hypertrophic scar tissue, eIF6 expression was significantly decreased and absent in the basal layer of epidermis in the early period, and increased slowly and began to appear in the basal layer of epidermis by the scar formation time.

CONCLUSIONSThis study confirmed that eIF6 expression was significantly related to the development of hypertrophic scar, and the eIF6 may be a target molecule for hypertrophic scar control or could be an indicator of the outcomes for other treatment modalities.

Adult ; Blotting, Western ; Cicatrix, Hypertrophic ; metabolism ; Female ; Gene Expression Regulation ; genetics ; Humans ; Immunohistochemistry ; Male ; Middle Aged ; Peptide Initiation Factors ; metabolism ; Pregnancy ; Retrospective Studies ; Young Adult

Escherichia coli ; genetics ; metabolism ; Escherichia coli Proteins ; genetics ; Gene Knockout Techniques ; Hydrogen-Ion Concentration ; Peptide Initiation Factors ; genetics ; Polyribosomes ; metabolism ; Protein Biosynthesis ; Stress, Physiological