OBJECTIVETo analyze the expression of MAP2K4 and vimentin in human endometrial carcinoma (EC) and their association with the clinicopathological features and prognosis of the patients.

METHODSMAP2K4 and vimentin expressions were detected immunohistochemically in paraffin-embedded tissue sections from 128 patients with EC, and the correlation of MAP2K4 and vimentin expressions with the clinicopathological factors of the patients was analyzed.

RESULTSMAP2K4 and vimentin proteins were positively expressed in 49 (38.3%) and 83 (64.8%) of the patients, respectively. A positive expression of MAP2K4 was negatively correlated with FIGO stage of the tumor (P=0.010) and lymph node status (P=0.016); a positive expression of vimentin was positively correlated with FIGO stage of the tumor (P=0.025), histological grades (P=0.017), depth of myometrial invasion (P=0.044) and lymph node status (P=0.032). MAP2K4 was inversely associated with vimentin expression in EC(r=-0.598, P<0.001). Patients positive for MAP2K4 tended to have a higher overall survival rate (P=0.002), and those positive for vimentin tended to have a lower overall survival rate (P=0.007); patients positive for MAP2K4 but negative for vimentin had the longest survival time, while those negative for MAP2K4 and positive for vimentin had lowest survival rate (P=0.004).

CONCLUSIONDetection of MAP2K4 and vimentin might help in early diagnosis and prognostic evaluation of patients with EC.

Endometrial Neoplasms ; metabolism ; pathology ; Female ; Humans ; MAP Kinase Kinase 4 ; metabolism ; Prognosis ; Survival Rate ; Vimentin ; metabolism

OBJECTIVETo study the clinicopathologic characteristics, immunophenotypes and differential diagnosis of primitive myxoid mesenchymal tumor of infancy (PMMTI).

METHODSThe clinical data, histological features and immunohistochemic results of 3 cases of PMMTI were reviewed.

RESULTSThere were 2 males and 1 female aged 4 years, 2 days and 3 months respectively. The tumor occurred in the head and neck (n = 2), and lumbar regions (n = 1).Histologically, they were composed of ovoid, short spindled to polygonal mesenchymal cells with less eosinophilic cytoplasm, or vacuolated cytoplasm. There was mild nuclear atypia with mitotic activity of 0-2/10 HPF.In most areas, the neoplastic cells showed a diffuse growth pattern, whereas in some areas, they formed a vaguely nodular pattern with peripheral collagenized stroma. They were embedded in a myxoid stroma that contained a rich delicate vascular network. Besides, small cyst-like spaces were also present in one case. The tumor cells expressed vimentin, but not alpha smooth muscle actin, desmin, myogenin, S-100 protein, CD34 and cytokeratin. The patients underwent surgery.One patient had local recurrences twice and died 2 years later. Compared with the primary tumor, the recurrent lesions exhibited increased cellularity, marked cellular atypia and mitotic activity (10/10 HPF). The other two patients remained well with no evidence of disease at last during follow-up.

CONCLUSIONSPMMTI is a rare soft tissue tumor of infancy, composed of primitive mesenchymal cells and myxoid stroma.It occurs mainly in the somatic soft tissues of the trunk, head and neck region, and the extremities, and is characterized by a high rate of local recurrence if incompletely excised. Metastasis and tumor related death may occur, albeit very rarely.Increased awareness of this novel entity will help avoid misinterpreting the lesion as a variety of other infantile mesenchymal neoplasms, including congenital fibrosarcoma and lipoblastoma.

Child, Preschool ; Female ; Humans ; Infant ; Infant, Newborn ; Male ; Soft Tissue Neoplasms ; metabolism ; pathology ; Vimentin ; metabolism

Adult ; Antigens, CD34 ; metabolism ; Humans ; Male ; Neoplasms, Fibrous Tissue ; metabolism ; pathology ; surgery ; Prostatectomy ; Prostatic Neoplasms ; metabolism ; pathology ; surgery ; Vimentin ; metabolism

Actins ; metabolism ; Adult ; Glomus Tumor ; metabolism ; pathology ; surgery ; Humans ; Male ; Trachea ; pathology ; Tracheal Neoplasms ; metabolism ; pathology ; surgery ; Tracheotomy ; Vimentin ; metabolism

Actins ; metabolism ; Female ; Glomus Tumor ; metabolism ; pathology ; surgery ; Humans ; Skin Neoplasms ; metabolism ; pathology ; surgery ; Thigh ; Vimentin ; metabolism ; Young Adult

Actins ; metabolism ; Bone Neoplasms ; metabolism ; pathology ; surgery ; Desmin ; metabolism ; Diagnosis, Differential ; Fibrosarcoma ; metabolism ; pathology ; Humans ; Leiomyosarcoma ; metabolism ; pathology ; surgery ; Male ; Middle Aged ; Neurilemmoma ; metabolism ; pathology ; Tibia ; Vimentin ; metabolism

Actins ; metabolism ; Arm ; Diagnosis, Differential ; Fibrosarcoma ; metabolism ; pathology ; Hamartoma ; metabolism ; pathology ; surgery ; Humans ; Infant ; Lipoma ; metabolism ; pathology ; Male ; Myofibromatosis ; metabolism ; pathology ; S100 Proteins ; metabolism ; Vimentin ; metabolism

OBJECTIVEThe conversion of arginine into citrulline, termed citrullination, has important consequences for the structure and function of proteins. The present study aimed to identify novel citrullinated proteins in 10 tumor cell lines by 2-D Western blotting (2-D WB).

METHODSTwo identical two-dimensional electrophoresis (2-DE) gels were prepared using extracts from ten cultured human tumor cell lines: ECA(esophageal cancer cells), HEPG2 (hepatocellular carcinoma cells), SKOV3 (ovarian cancer cells), MCF-7 (breast cancer cells), H292 (lung mucoepidermoid carcinoma cells), HeLa (cervical cancer cells), Lovo (colon cancer cells), OS-RC (renal cell carcinoma cells), PANC-1 (pancreatic cancer cells), and SGC (gastric cancer cells). The expression profiles on one 2-DE gels were trans-blotted to PVDF membranes, and the blots were then probed with an anti-citrulline antibody. By comparing the 2-DE profile with the parallel 2-D WB profile at a global level, protein spots with immuno-signals were collected from the second 2-DE gel and identified using mass spectrometry. Immunoprecipitation was used to verify the expression and citrullination of the targeted proteins in the tumor cell lines.

RESULTS2-D WB and mass spectrometry identified citrullinated ENO1 (α-enolase), HSP60 (heat shock protein 60), KRT8 (keratin 8), TUBB (tubulin beta), TCRβ (T cell receptor β chain), VIME (vimentin) and PDI in these cell lines. Immunoprecipitation analyses verified the expression and citrullination of ENO1, HSP60, KRT8, and TUBB in the total protein lysates of the tumor cell lines.

CONCLUSIONThe citrullination of proteins ENO1, HSP60, KRT8, and TUBB suggests a new mechanism in the tumorigenic process.

Blotting, Western ; Cell Line, Tumor ; Citrulline ; metabolism ; Female ; Humans ; Immunoprecipitation ; Mass Spectrometry ; Phosphopyruvate Hydratase ; Vimentin

OBJECTIVETo evaluate the effects of early tangential excision on the prevention of the progression of deep partial thickness burn wound.

METHODSTwelve burn patients with deep partial thickness burn wound were enrolled and received tangential excision of the burn wound within 24 postburn hours (PBHs). The histological samples were harvested from the wound before and 5 - 7 postoperative days (PODs) after the operation and the wound without operation 5 - 7 postburn days (PBDs). The samples were observed by means of HE staining, Masson's staining and the labelling of Vimentin antigen positive cells by immunohistological skill.

RESULTSThe inflammatory reaction of the burn wound without operation aggravated progressively along with that of disease and the tissue necrosis area enlarged. And the residual skin appendages disappeared due to the enhanced inflammatory reaction. The brown area expanded and light green area shrinked by Masson's staining. The Vimentin antigen positive cell count decreased significantly. But in the burn wound being performed tangential excision within 24 PBHs, focal inflammatory reaction exhibited evident ligher than that in burn wound without operation. Moreover, there appeared fresh granulation formation and partial epithelial coverage with no enlarged necrotic tissue area in the operated wound when compared with that in non-operated wound (P < 0.05). Furthermore, the light green area exhibited no obvious shrinking by Masson's staining and the Vimentin antigen positive cell count was much more in the operation area than that in non-operative area (P < 0.05).

CONCLUSIONIt might be beneficial to the host to perform tangential excision within 24 PBHs, which could remove burn wound necrotic tissue in time and hamper the progression of tissue degenerative injury. The healing process of deep partial thickness burn wound was therefore accelerated.

Adult ; Burns ; complications ; metabolism ; pathology ; Female ; Humans ; Male ; Necrosis ; Vimentin ; analysis ; Wound Healing

OBJECTIVETo observe the expression profiles between two metastasis-associated proteins in different prostate cancer cell lines and explore the molecular mechanisms of bone metastatic potentials.

METHODSExpressions of E-cadherin and vimentin in two prostate cancer cell lines (LNCaP and IA8) with different metastatic potentials were detected by Western blotting.

RESULTSThere was remarkable difference in the expressions of E-cadherin and vimentin between the highly metastatic cell line and the lowly one. As one of the adhesion associated proteins, E-cadherin was detected with high level of expression in LNCaP cell line, which was well known as low metastatic potential. However, E-cadherin did not expressed in IA8 with high metastatic potential. And as one of the cytoskeleton proteins, vimentin expression was high in IA8, but not in LNCaP.

CONCLUSIONThere is definitely difference in the metastatic phenotypes (E-cadherin and vimentin) among cell lines with different metastatic potentials. The expressions of E-cadherin and vimentin proteins may play important roles in promoting and inhibiting the metastasis of prostate cancer respectively, and may be considered to be valuable in evaluating the malignant degree, predictable metastasis and prognosis of prostate cancers.

Cadherins ; biosynthesis ; Cell Line, Tumor ; Humans ; Male ; Neoplasm Metastasis ; Prognosis ; Prostatic Neoplasms ; metabolism ; pathology ; Vimentin ; biosynthesis