Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0220723 (PCA)
 4,687 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The immunological reactivity of serous ovarian tumor cells was evaluated, taking into account their density and morphological features. Discontinuous density gradient centrifugation was applied to fractionate cell subpopulations from cystic fluids of patients with ovarian serous carcinomas, cystadenomas and benign serous cysts. For phenotypic characterization of tumor cell subpopulations the immune sera against perchloric acid extracts of ovarian serous (anti-PCA-CaOs) and mucinous (anti-PCA-CaOm) carcinomas were used. The expression of carcinoembryonic antigen (CEA) and nonspecific cross-reacting antigen (NCA) on tumor cell fractions was also checked. Some relationship between immunological reactivity, cell morphology and cell density was found; however, individual patient-to-patient variations in cellular composition and antigenic expression were also observed. The presence of ovarian serous carcinoma-associated antigen (CaOs-Ag) was related mainly to frankly malignant cells. Neither CEA nor NCA were constant and characteristic markers for serous ovarian neoplasms. These neoplasms were unreactive with anti-PCA-CaOm serum. Our results indicate the possibility of correlation between morphological features, density distribution and immunological phenotypes of ovarian tumor cell populations.
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PMID:Density distribution and antigenic characterization of cell subpopulations isolated from cystic fluids of ovarian serous neoplasms. 270 45

By fusion of C3H mouse spleen cells, immunized with a PCA extract from liver metastases of a colon tumor, and Sp2/O-Ag14 myeloma cells, we produced several clones secreting monoclonal antibodies (MAb) with reactivity against carcinoembryonic antigen (CEA). For the screening of the different MAb, an ELISA technique with PCA extract and highly purified CEA coupled with alkaline phosphatase was employed. The specificities of the MAb prescreened with the ELISA technique were analyzed further by immunoprecipitation and separation on SDS-PAGE, followed by enzyme digestion and thin-layer chromatography for fingerprint analysis. The MAb recognized (a) an antigenic determinant present only on CEA, (b) common determinants present on CEA and at least six other molecules separated by SDS-PAGE and (c) antigenic determinants not present on CEA. The fingerprint analysis showed the relationship of the molecules on the basis of protein chemistry.
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PMID:Monoclonal antibodies against CEA. Comparison of the immunoprecipitates by fingerprint analysis. 618 85

Some properties and kinetics of synthesis of the carcinoembryonic antigen (CEA-LoVo) produced by an established human colon carcinoma cell line were analyzed. CEA-LoVo was assayed by the method of Chu and Reynoso which was standardized against the activity of the First British Standard for CEA. CEA-LoVo was stable at -20 and 4 degrees C. At 37 degrees C, CEA-LoVo degraded at the rate of 1.4%/day in cell-free supernatants, and at the rate of 6.6%/day in the supernatants of monolayer cultures. CEA-LoVo was sensitive to enzymatic treatment with trypsin (approximately 55% loss)) and extraction of PCA (> 70% loss). The elution profile of CEA-LoVo in Concanavalin A-Sepharose B coincided with that of the First British Standard for CEA. No A or B blood group antigenic activity was noted. Studies employing immunofluorescent and horseradish peroxidase-labeled antibody techniques demonstrated heavy membrane and moderate intracytoplasmic localization. The greatest amount of net synthesis occurred for cells in the stationary phase while CEA-LoVo release occurred maximally in the lag phase.
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PMID:Observations on the synthesis of carcinoembryonic antigen by an established human colonic carcinoma cell line. 625 89

Some properties and kinetics of synthesis of the carcinoembryonic antigen (CEA-LoVo) produced by an established human colon carcinoma cell line were analyzed. CEA-LoVo was assayed by the method of Chu and Reynoso which was standardized against the activity of the First British Standard for CEA. CEA-LoVo was stable at -20 and 4 degrees C. At 37 degrees C, CEA-LoVo degraded at the rate of 1.4%/day in cell-free supernatants, and at the rate of 6.6%/day in the supernatants of monolayer cultures. CEA-LoVo was sensitive to enzymatic treatment ( approximately 55% loss) and extraction of PCA (greater than 70% loss). The elution profile of CEA-LoVo in concanavalin A-Sepharose B coincided with that of the First British Standard for CEA. No A or B blood group antigenic activity was noted. Studies employing immunofluorescent and horseradish peroxidase-labeled antibody techniques demonstrated heavy membrane and moderate intracytoplasmic localization. The greatest amount of net synthesis occurred for cells in stationary phase while CEA-LoVo release occurred maximally in lag phase.
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PMID:Observations on the synthesis of carcinoembryonic antigen by an established human colonic carcinoma cell line. 736 Apr 84

CD66a is a member of the carcinoembryonic antigen family and has been suggested to function as an intercellular adhesion molecule and cell growth regulator. Expression of CD66a in myeloma cells was examined with mAb TS135 against CD66a transfectants of murine-transformed fibroblasts. The reactivity of mAb TS135 with CD66a, CD66c, and CD66e was revealed. CD66a in myeloma cells was considered to be detectable with this mAb, since CD66c and CD66e are not expressed in them. CD66a was detected in three myeloma cell lines and an IgM-producing B-cell line. In clinical bone marrow specimens, including 18 multiple myeloma, two primary macroglobulinemia, and a case of CLL-like chronic lymphoproliferation with monoclonal IgG production, CD66a and three conventional myeloma cell markers (PCA-1, CD38, and CD56) were examined by indirect immunofluorescence assay. The results showed that 18 out of 21 cases (86%) were CD66a+, and PCA-1 showed the highest correlation with CD66a among conventional markers. Primary macroglobulinemia and chronic lymphoproliferation were also CD66a+. Two-dimensional flow cytometry with mAbs TS135 and CD38 confirmed the reactivity of TS135 with myeloma cells in those bone marrow specimens. The findings suggest that CD66a is expressed in multiple myeloma with high frequency.
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PMID:Expression of CD66a in multiple myeloma. 1194 96

Background Serum tumor markers are ubiquitously used in the clinic for cancer screening. However, the mechanisms accounting for the elevated levels of the serum tumor markers remain to be explored. Methods We performed a pan-cancer analysis of serum alpha-fetoprotein (AFP), carcinoembryonic antigen (CEA) and prostate-specific antigen (PSA). The relation between concentration of serum tumor markers and the expression of their coding genes was assessed. Then the expression of AFP and its genomic background in hepatocellular carcinoma (liver cancer) was studied. Results High expression of AFP mRNA was found mainly in liver cancer. In gastric cancer, breast cancer and lung cancer, high AFP mRNA expression was also discovered occasionally. In liver cancer patients, serum AFP levels correlated significantly with AFP mRNA expression in cancer tissues (r = 0.72, p = 1.6e-45). Whole transcriptome analysis revealed that serum AFP levels clearly separated liver cancer into two classes with distinct expression profiles according to PCA analysis. Gene co-expression analysis revealed that AFP expression was connected to a module enriched with genes accounting for cell cycle and cell proliferation regulation. In addition, high AFP expression was associated with the molecular classification of liver cancer, including iCluster (Chi-square: 16.86, P = 0.0002). Methylation analysis revealed de-methylation of AFP promoter occurred in some liver cancer tissues, which was significantly related to AFP mRNA expression. Survival analysis indicated high serum AFP levels was prognostic of poorer survival of the liver cancer patients (Log-rank test: p = 0.046). This was confirmed by an independent dataset in which liver cancer patients with high serum AFP also had poorer survival (Log-rank test: p = 0.024). Conclusion High expression of AFP defined a subtype of liver cancer with distinct gene expression profiles and clinical features. De-methylation of cytosine from CpG di-nucleotides in AFP promoter may be the cause of AFP re-expression in adult human liver cancer tissue.
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PMID:Aberrant AFP expression characterizes a subset of hepatocellular carcinoma with distinct gene expression patterns and inferior prognosis. 3189 35