OBJECTIVE: The aim of this study was to investigate the genetic association of the FAT gene with schizophrenia in the Korean population, as well as analyzing the association of FAT gene with clinical variables. METHODS: Four variants within the FAT gene were investigated in 189 patients with schizophrenia and 119 healthy controls (rs2306987 A/C, rs2306990 T/C, rs2637777 G/T, and rs2304865 G/C). RESULTS: Significant association at the rs273777 with schizophrenia was observed; however, rs2306987, rs2306990, and rs2304865 were not associated with schizophrenia. Haplotype analyses revealed that the haplotype A/T/T/G was associated with a significantly protective effect. Sliding window analysis (rs2637777 G/T and rs2304865 G/C) revealed the more common T/G haplotype, included in the A/T/T/G protective combination, showed a small protective effect, in particular the effect was due to the rs273777 T variant (minor allele). CONCLUSION: The present finding suggests that FAT polymorphism may play a putative role in the susceptibility to schizophrenia in the Korean population. Further studies using a larger number of subjects should be performed to determine whether the FAT gene polymorphism may be truly involved in the development of schizophrenia.
Cadherins ; Haplotypes ; Humans ; Schizophrenia

No abstract available.
Cadherins* ; Carcinogenesis* ; Urinary Bladder*

OBJECTIVE: To investigate the expression of E-cadherin in benign, borderline, and malignant ovarian tumors. METHODS: An immunohistochemical technique was applied to formalin-fixed paraffin-embedded samples of 20 benign cystic ovarian tumors, 14 borderline ovarian tumors and 13 ovarian carcinomas. Expressions of E-cadherin immunostaining in three histological types were compared, and the survival rate in malignant ovarian cancer according to E-cadherin expression was also assessed. RESULTS: E-cadherin was positively or heterogeneously expressed in both benign and borderline ovarian tumors. But it was negatively, heterogeneously, or positively expressed in malignant ovarian tumors. The difference of expression of E-cadherin between borderline and malignant ovarian tumors was statisticaIly significant (p<0.05). In ovarian carcinoma, there was difference between negative and positive group in survival (p<0.05). CONCLUSION: Our results suggest that alterations in E-cadherin seem to occur at a later stage of the ovarian carcinogenesis, and may have some prognostic value in malignant ovarian tumor.
Cadherins* ; Carcinogenesis ; Ovarian Neoplasms ; Survival Rate

The usefulness of E-cadherin immunostaining as a marker of malignancy in the body fluids was investigated in the present study. Thirty-three histologically proven cases of cell blocks from the pleural, peritoneal, and pericardial fluids were studied by immunocytochemistry for E-cadherin antibody using LSAB method. These cases were cytologically diagnosed as adenocarcinoma (25 cases) and atypical cells (8 cases). Tumor cells showed strong positive membranous staining for E-cadherin antibody in 21 out of 25 cases (84%) of adenocarcinoma. E-cadherin staining was not found in 6 of 8 cases of suspicious maligancy. The sensitivity and specificity were 84% and 75%, respectively. Reactive mesothelial cells and inflammatory cells scattered were all negative. In conclusion, E-cadherin is an useful adjunctive marker to distinguish reactive mesothelial cells from the carcinoma cells in the body fluids.
Adenocarcinoma ; Body Fluids ; Cadherins* ; Immunohistochemistry ; Sensitivity and Specificity

PURPOSE: We investigated whether the loss of E-cadherin function was related to the peritoneal seeding in colorectal carcinomas. METHODS: Eleven patients who had undergone a palliative resection for a colorectal carcinoma, with peritoneal seeding, were enrolled onto the study. The primary tumors and seeding nodules were analyzed with regarded to mutations in the expressions of the CDH1 and protein of E-cadherin using SSCP, direct sequencing and immunohistochemical staining. RESULTS: In the primary tumors, the E-cadherin was normally expressed in 9 of the 11 cases, with 2 cases showing a reduced expression. In the seeding nodules, the E-cadherin was normally expressed in 6 of the 11 cases, with 5 cases showing a reduced expression. The degree of E-cadherin expression in the seeding nodules was significantly decreased comparing to that in the primary tumors (P<0.001). In the mutational analysis, there were no pathogenic mutations in either the primary tumors or the seeding nodules, with the exception of two silent changes in the ctgggt>ctaggt (intron 2) and GTG>GTA (codon 782). CONCLUSION: The loss of E-cadherin expression might be related to peritoneal seeding. The functional derangement of E-cadherin in peritoneal seeding could possibly be caused by a mechanism, such as promoter methylation, rather than the mutation of the CDH1.
Cadherins* ; Colorectal Neoplasms* ; Humans ; Methylation ; Polymorphism, Single-Stranded Conformational

PURPOSE: We examined the expressions of claudin-4 and E-cadherin, which are known as cell adhesion-associated proteins, in stomach cancer. The relationship of their expression with the clinicopathologic factors was examined to investigate the roles of these proteins in the invasion or metastasis of stomach adenocarcinoma. METHODS: The expressions of claudin-4 and E-cadherin were examined in 73 cases of adenocarcinoma of the stomach by performing immunohistochemical staining. RESULTS: The expressions of claudin-4 and E-cadherin in the stomach adenocarcinoma were both correlated with the histologic grade, the T-stage and nodal metastasis, respectively (P<0.05). The expression of claudin-4 was significantly associated with the expression of E-cadherin. CONCLUSION: Our data suggests that claudin-4 and E-cadherin are involved in the processes of histologic differentiation, invasion and metastasis of stomach adenocarcinoma.
Adenocarcinoma ; Cadherins* ; Claudin-4* ; Neoplasm Metastasis ; Stomach Neoplasms* ; Stomach*

BACKGROUND: The activation of phospholipase C(PLC) is one of the early cellular events in various growth process, including malignant transformation. PLC-gamma1 is activated through direct interaction with growth factor receptor tyrosine kinase. MATERIAL AND METHODS: Using immunoblot assay, we evaluated overexpression of PLC-gamma1 expression in twenty human breast cancer tissues. It was also determined whether there was any connection between other prognostic factors(numbers of metastatic axillary nodes, nuclear and histological grade, c-erbB2, p53 and E-cadherin) and the overexpression of PLC-gamma1 protein. RESULTS: Seventeen of 20 breast cancer tissues showed overexpression of PLC-gamma1, which was corresponded to that seen on the immunohistochemistry( kappa= 0.8275, p = 0.003). Of 3 tumor markers, immunohistochemically determined, positive expression of E-cadherin only was associated with PLC-gamma1 protein overexpression in a range of statistical significance (p=0.045, kappa=0.607). CONCLUSION: PLC-gamma1 overexpression might be pathogenic trigger involved in breast cancer and the relationship between expression of E-cadherin and PLC-gamma1 would require further elucidation.
Breast Neoplasms ; Cadherins ; Humans ; Phospholipases* ; Protein-Tyrosine Kinases ; Biomarkers, Tumor

PURPOSE: We investigated the expressions of E- Cadherin and p53 in soft tissue tumors to determine their significance in sarcoma development and/or progression and to assess their potential correlation with epithelial features. MATERIALS AND METHODS: A total of 79 soft tissue sarcomas, including 10 tumors comprising epithelial components, were studied immunohistochemically in paraffin-embedded tissue sections. Further analysis was performed on 61 tumors by the application of a polymerase chain reaction technique and a direct sequence analysis procedure applied to exons 5 through 8 in the p53 gene. RESULTS: E-Cadherin was expressed at the cell-cell boundaries in 8 (10%) tumors: 5 of grade 2 and 3 of grade 3. Of these, six (being 60% of the total of 10 tumors containing epithelial elements) contained and two did not contain histologic evidence of epithelial differentiation. Overexpression of p53 was detected in 26 (33%) samples, 7 of which demonstrated mutations in the p53 gene. No association was established between E-Cadherin immunoreactivities and p53 abnormalities. Tumor grade was found to be strongly correlated with p53 alterations (p=0.01) but not with E-Cadherin expression (p=0.09). CONCLUSION: These data confirm a role for altered p53 in the pathogenesis of soft tissue sarcomas and suggest a possible role for E-Cadherin in the maintenance of epithelial architecture in these tumors regardless of p53 status.
Cadherins* ; Exons ; Genes, p53 ; Polymerase Chain Reaction ; Sarcoma* ; Sequence Analysis

E-cadherin (ECD) is a Ca++ -dependent adhesion molecule which plays a major role in the maintenance of intercellular adhesion in epithelial tissues. The expression pattern of ECD in 77 surgically resected gastric adenocarcinomas was examined by immunohistochemistry, using a rat monoclonal antibody raised against murine E-cadherin (DECAM-1). ECD was strongly expressed uniformly at cell to cell borders in normal gastric epithelium without exception. But, various staining patterns were observed in the cancer tissues. The frequency of tumors with preserved ECD expression (Pre-type) and reduced ECD expression (Rd-type) was 44% and 56%, respectively. Using Lauren's classification, the high frequency of the Pre-type expression in adenocarcinoma of the intestinal type was significantly higher than that in adenocarcinoma of the diffuse type (p<0.05). But, no significant correlation between the ECD expression and the gross type, invasion depth, growth pattern or metastasis was observed. These results suggest that ECD might play a key role in the morphogenesis of gastric adenocarcinoma.
Adenocarcinoma* ; Animals ; Cadherins* ; Classification ; Epithelium ; Immunohistochemistry ; Morphogenesis ; Neoplasm Metastasis ; Rats

BACKGROUND: Pemphigus foliaceus(PF) and pemphigus vulgaris(PV) have different target antigens which belong to the desmoglein(DG) subfamily of the desmosomal cadherins; DG in the case of PF and PV antigen(PVA) in the case of PV. OBJECTIVE: Because DG is also a normal major component of the intercellular adhesive core, we investigated the immunohistochemical distribution of DG in PF to compare and contrast the findings with those of PV. METHODS: Immunohistochemical analysis using streptavidin-biotin complex method with anti-DG monoclonal antibody was done in six cases of PF and six cases of PV, as well as two samples of normal skin as control. RESULTS: Both disorders showed abnormal intense diffuse cytoplasmic staining patterns in the lesional skin. Contrary to PF, showing complete loss of normal, rim-like, membranous staining, two of six cases of PV showed the relatively well preserved normal staining pat-terns in the upper epidermis. CONCLUSION: The differences in the expression of DG in the lesional skins between PF and PV suggest that PVA is distinct from DG, although an overlapping of antigens between PF and PV could exist.
Adhesives ; Cytoplasm ; Desmogleins* ; Desmosomal Cadherins ; Epidermis ; Methods ; Pemphigus* ; Skin