Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.3.1 (alkaline phosphatase)
47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Combinations of carcinoembryonic antigen (CEA), gamma glutamyl transpeptidase (GGT), pregnancy-associated macroglobulin (PAM) and placenta-like alkaline phosphatase (PLAP) were studied in groups of patients with ovarian and cervical cancer. In ovarian cancer, only CEA and PLAP levels appeared to reflect tumor burden and were complementary in detecting active disease. In cervical cancer, CEA and GGT reflected tumor burden, while PLAP showed just the reverse--the highest degree of positivity being present in minimal disease. PLAP positivity was even more pronounced in patients with cervical dysplasia and carcinoma in situ while CEA and GGT were negative. The data indicate that the use of marker combinations can improve our capacity to detect minimal disease and provide information regarding tumor biology that may not be available by studying individual markers or by other means. It remains to be determined whether the use of tumor markers can influence existing therapy sufficiently to alter the outcome in cancers which are notoriously difficult to treat.
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PMID:Carcinoembryonic antigen (CEA) and other tumor markers in ovarian and cervical cancer. 3 May 36

The localization of alkaline phosphatase in HeLa cells was examined by electron microscopic histochemistry and subcellular fractionation techniques. Two monophenotypic sublines of HeLa cells which respectively produced Regan and non-Regan isoenzymes of alkaline phosphatase were used for this study. The electron microscopic histochemical results showed that in both sublines the major location of alkaline phosphatase is in the plasma membrane. The enzyme reaction was occasionally observed in some of the dense body lysosomes. This result was supported by data obtained from a subcellular fractionation study which showed that the microsomal fraction rich in plasma membrane fragments had the highest activity of alkaline phosphatase. The distribution of this enzyme among the subcellular fractions closely paralleled that of the 5'-nucleotidase, a plasma membrane marker enzyme. Characterization of the alkaline phosphatase present in each subcellular fraction showed identical enzyme properties, which suggests that a single isoenzyme exists among fractions obtained from each cell line. The results, therefore, confirm the reports suggesting that plasma membrane is the major site of alkaline phosphatase localization in HeLa cells. The absence of any enzyme reaction in the perimitochondrial space in these cultured tumor cells also indicates that the mitochondrial localization of the Regan isoenzyme reported in ovarian cancer may not be a common phenomenon in Regan-producing cancer cells.
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PMID:Plasma membrane localization of alkaline phosphatase in HeLa cells. 5 27

Histaminase has been shown to be associated with several types of human cancer. In the present study, we examined the activity of histaminase and its relationship with Regan isoenzyme of alkaline phosphatase in ascitic fluids obtained from patients with ovarian and several other types of cancer. We have found that about 44% of the ovarian cancer patients had elevated levels of histaminase in the ascitic fluid, whereas a less frequent incidence was observed in fluids obtained from other types of cancer. There was concurrence in the elevation of histaminase activity with the appearance of Regan isoenzyme in most of the samples examined. Of the 10 patients who showed elevated histaminase, 9 had high Regan isoenzyme activity; whereas in 9 patients with normal levels of histaminase, all except 1 had low or moderate levels of Regan isoenzyme activity. These results, therefore, confirm the observation of an association of histaminase with human cancer and suggest the possibility for the utilization of histaminase, in conjunction with Regan isoenzyme and cancer-associated proteins, for cancer diagnosis and clinical evaluation of tumor progression and regression during therapy.
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PMID:Elevation of histaminase and its concurrence with Regan isoenzyme in ovarian cancer. 80 68

Among 833 cancer patients whose sera were investigated for Regan isoenzyme and among 1,319 cancer patients from a different population whose sera were assayed for human chorionic gonadotropin (HCG), those patients with neoplasms of the testis or ovary showed the highest frequency of both placental proteins. Among another 22 patients with ovarian cancer, for whom both placental proteins were measured, 59% showed Regan isoenzyme and 68% showed HCG in ascitic fluids, whereas the figures were 65% and 30%, respectively, for sera. In 55% of both fluids and sera, there was a positive correlation of Regan isoenzyme with HCG (positive or negative). Almost invariably, the ascitic fluid was richer in Regan isoenzyme and HCG than the serum when both were collected on the same day. Progressively increasing levels of each placental protein generally correlated with the spread of the disease, though there were instances when only one was expressed. Evidence indicated the existence of two forms of alkaline phosphatase in ovarian cancer, Regan and non-Regan; the latter was assumed to be of fetal origin. Ultrastructural studies of one ovarian cancer revealed a morphologic entity, i.e., mitochondria enveloped by inverted tubules of endoplasmic reticulum.
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PMID:Regan isoenzyme and human chorionic gonadotropin in ovarian cancer. 123 37

A number of chemical agents have been found to influence the proliferation, morphology, enzymatic activity, and antigen expression of neoplastic cells toward a more differentiated phenotype. We studied the effects of differentiating agents retinoic acid, sodium butyrate, and dibutyryl cyclic AMP on the expression of the tumor-associated antigen CA 125 and several biochemical markers of differentiation in cultured OVCA 433 ovarian cancer cells. Treatment of OVCA 433 cells with these agents for 96 hr reduced cellular proliferation and altered cellular morphology. Quantitation of cell surface CA 125 using flow cytometry revealed that CA 125 expression was reduced by 35-50%. The amount of CA 125 antigen shed into the culture media was reduced to a similar degree. In addition, differentiation inducers markedly enhanced cellular alkaline phosphatase activity and induced the expression of a 65-67-kDa cytokeratin. These findings provide support for the induction of a more differentiated phenotype by these agents.
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PMID:Effect of differentiation agents on expression of CA 125, alkaline phosphatase, and cytokeratins in human ovarian adenocarcinoma cells (OVCA 433). 172 Jan 10

The molecular nature and possible presence of a glycan-phosphatidylinositol anchor (GPI-anchor) in CA125 molecules was investigated. Serial lectin affinity chromatography and N- or O-glycanase treatment to reduce antigenicity showed that CA125 contained certain N- and O-glycosylated sugar chains in the molecule, like a glycoprotein. CA125 released from ovarian cancer tissues increased time-dependently following phosphatidylinositol-specific phospholipase C (PI-PLC) treatment, concomitant with the release of tissue-unspecific alkaline phosphatase. Western blotting of CA125 treated by PI-PLC showed a single band of 90 kD instead of the 162- and 76-kD bands of the native antigen. Further, ovarian cancer tissues subjected to PI-PLC treatment lost the immunohistochemical localization of CA125 with OC125 antibody. Consequently, it is strongly suggested that CA125 is a glycoprotein that has both N- and O-linked sugar chains and a membranous GPI-anchoring moiety, and further, that its 90-kD form is the antigen without the GPI-anchor.
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PMID:Molecular nature and possible presence of a membranous glycan-phosphatidylinositol anchor of CA125 antigen. 196 50

The significance of the PLAP (Placental alkaline phosphatase)/PLAP-like isozyme as tumour marker in relation to CA 125 and TPA for the monitoring of patients with malignant ovarian epithelial tumours was evaluated. Of all patients (n = 85), 40% had all three markers elevated. CA 125 being the most sensitive (60%), and the PLAP/PLAP-like isozyme and TPA both 40%. A tendency to certain tumour marker patterns of these three antigens in serum can be seen with regard to histopathology. Serous and anaplastic adenocarcinomas usually have all three markers moderately elevated, mucinous and mesonephric adenocarcinomas both have low incidences and low average levels of all three markers. Endometrioid and non-mucinous adenocarcinomas are often associated with high levels of the PLAP/PLAP-like isozyme and CA 125, while TPA shows moderate elevation. The PLAP/PLAP-like isozyme is positively correlated to tumour burden and the outcome of the disease. It may provide additional information on CA 125 in the monitoring of patients with ovarian cancer.
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PMID:Placental alkaline phosphatase (PLAP)/PLAP-like alkaline phosphatase as tumour marker in relation to CA 125 and TPA for ovarian epithelial tumours. 209 51

Placental-like alkaline phosphatase (PLAP) was measured by its catalytic activity (CA), using an amplified enzyme-linked immunoassay, and by its immunologic activity (IA), using an enzyme-linked immunosorbent assay. In both assays the same monoclonal anti-PLAP antibody was used as the primary reagent. This antibody reacts with the main epitope on PLAP that is common to PLAP of ovarian and testicular origin, as well as of PLAP that is induced by smoking. Determinations of CA and IA of PLAP were carried out in serum samples from 101 patients with epithelial ovarian cancer (49 patients with progressive or recurrent disease, 52 patients with no evidence of disease), 20 patients with testicular cancer (8 non-seminoma testis, 12 seminoma testis) and 61 healthy controls. Smoking status was taken into consideration. The main findings from this study are: 1. In prolonged follow-up of patients who were treated for ovarian cancer, progressive or recurrent disease was never accompanied by rising values of CA or IA of PLAP. Therefore in this study, PLAP was not a good monitor for this disease. 2. In all instances where expression of PLAP was reflected by raised serum levels of these antigens, the measurement of the catalytic activity proved to be a more sensitive parameter than that of the immunologic activity. The value of PLAP measurements in the follow-up of patients with testicular cancer remains to be elucidated.
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PMID:Catalytic and immunologic activities of placental-like alkaline phosphatase in clinical studies. The value of PLAP in follow-up of ovarian cancer. 244 78

1. Two monoclonal antibodies, MA54 and MA61, were established by immunizing with culture medium supernatants of a lung adenocarcinoma cell line, and a double determinants sandwich enzyme immunoassay system (MKS-15) was developed by using these two monoclonal antibodies. The antigen recognized by this assay (CA54/61) was found in the sera of 54% of all ovarian cancer cases and 55% of mucinous cystoadenocarcinoma cases, but in 4% of benign ovarian cystoadenoma cases: 85% of ovarian cancers were positive by the combination assay of MA 54/61 and CA125, indicating the clinical usefulness of CA54/61. 2. Galactosyl transferase isozyme II (GT-II) was assayed by a newly developed system, and it was found that 74% of ovarian cancers were positive and the value GT-II was very high in 6 of 9 mesonephroid cases, indicating its histological type specificity. 3. Placental alkaline phosphatase (PLAP) was assayed by two kinds of newly developed EIA kits, and it was found that PLAP was high in more than 50% of serous cystoadenocarcinomas, but in 7% of benign ovarian tumors, indicating its cancer specificities.
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PMID:[The usefulness and limitation of sugar antigen in ovarian cancers--with special reference to a new tumor marker, CA54/61]. 249 63

A permanent human neoplastic cell line, DO-s, was established from ascites of a patient with a well-differentiated mucinous cyst-adenocarcinoma of the ovary. This cell line grew as vermiform, floating colonies of epithelial cells in culture. The karyotype of DO-s was of a human female; the chromosome number ranged from 54 to 66 with several abnormalities, mainly trisomy. Epithelial-like character was confirmed by transmission electron microscopy and by the presence of cytokeratin. Inoculation of DO-s cells i.p. or s.c. in athymic nude mice resulted in, respectively, ascites and xenografts. Light and electron microscopical analysis of cultured cells and xenografts demonstrated that the cell line was derived of a mucinous adenocarcinoma biopsy. Tumor-associated antigens, cancer antigen 125 (CA 125), human milk fat globulin, and human placental alkaline phosphatase were expressed by cells in culture and in xenografts. Modulation of the antigens, CA 125 and human milk fat globulin, occurred in DO-s cells growing in athymic mice. Biochemical, immunohistochemical, and histochemical analysis showed that more than 50% of the alkaline phosphatase isoenzymes present in DO-s cells had the characteristics of human placental alkaline phosphatase and placental alkaline phosphatase-like alkaline phosphatase (AP), but fractions of intestinal AP and nonspecific AP (bone-liver-kidney) were also present. The expression of AP isoenzymes could be induced by an enhancement of the serum supplement in the culture media, and by dexamethasone, sodium butyrate, and bromodeoxyuridine. This line will be a valuable tool in studying the therapeutic effects of antibodies to tumor-associated antigens or other agents for ovarian cancer.
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PMID:Establishment and characterization of a human ovarian neoplastic cell line, DO-s. 254 14


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