Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The highest prevalence of testicular cancer occurs in young men with high androgen activity. The presence and distribution of androgen receptors (ARs) was therefore investigated in germ cell neoplasia, using two specific monoclonal antibodies. Tissue samples from 18 patients with seminoma and/or carcinoma-in-situ (CIS) of the testis were examined. An indirect immunohistochemical method with a biotin-streptavidin-peroxidase or an alkaline phosphatase detection system was used. 45% of seminoma samples and 42% of CIS samples were AR-positive with antibody AN 1-15. The values obtained using antibody F 39.4.1 were 44 and 40% respectively. Some differences in specificity between the two antibodies were observed. Unusual granular staining of germ cells in normal testes, also present in malignant germ cells, was noted when antibody F39.4.1 was used. The presence of AR protein immunoreactivity in neoplastic germ cells suggests that androgens may be involved in the pathogenesis of the disease.
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PMID:Immunohistochemical identification of androgen receptors in germ cell neoplasia. 147 24

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

An alkaline phosphatase (EC 3.1.3.1) of the placental type was isolated from a seminoma type of human testicular cancer tissue and was purified to homogeneity by sulfate-mediated chromatography on a column of Cibacron Blue Sepharose 4B. The purified enzyme had a specific activity of 40.6 kU per gram of protein and was obtained in a yield of 37%. The purification procedure used was simple and economical, and may be used to purify alkaline phosphatase isoenzymes from other cancer tissues. This is the first report of the purification of the enzyme in seminoma. Inhibition studies suggest that this enzyme is a Nagao variant rather than the Regan type reported in several cancer tissues.
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PMID:Isolation and purification of placental type alkaline phosphatase from a seminoma. 310 Jan 1

Using a solid-phase monoclonal antibody enzyme immuno-assay, we evaluated in a multicenter study (18 laboratories) the utility of evaluating catalytic activity of human placental alkaline phosphatase (hPLAP, EC 3.1.3.1) in serum as a potential tumor marker. We determined hPLAP in serum samples from 130 patients with ovarian cancer, 79 patients with testicular cancer (53 seminoma testis, 26 nonseminoma testis), 537 patients with various other malignant diseases (95 lung, 39 gastrointestinal, 195 breast, 208 others), 291 patients with benign diseases, and 213 healthy controls. To assess the influence of smoking on hPLAP activity in serum, we evaluated 79 serum samples from patients with noncancerous diseases for whom smoking habits had been recorded. Our main findings are: (a) hPLAP activity is frequently increased (greater than 100 mU/L) in pre-operative serum samples from ovarian cancer patients (49%) and from testicular cancer patients (59% overall; 72% seminoma, 35% nonseminoma); (b) heavy smoking may increase hPLAP activity; (c) excluding heavy smokers, a 96% specificity for cancerous lesions was observed; (d) in patients with ovarian malignancies, CA 125 and hPLAP may behave as independent markers; and (e) in patients with seminoma, hPLAP is clearly more frequently increased than is beta-choriogonadotropin.
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PMID:Multicenter evaluation of human placental alkaline phosphatase as a possible tumor-associated antigen in serum. 316 10

Despite the apparent link between the presence of alkaline phosphatase (ALP) and various cancers, it has so far been difficult to determine distinct differences between seminoma-derived ALP and placental ALP (PLAP). In order to determine specificity, we purified ALP from a seminoma type of human testicular cancer tissue and compared its biochemical and immunological properties with those of PLAP. The purified ALP had a specific activity of 66 units per mg of protein, and it was possible to obtain 169 microg of purified preparation from 60 g of tissue. The molecular weight of the purified seminoma enzyme was approximately 500 kDa. We found that a novel type of ALP from human testicular cancer tissue exists, with a high molecular weight and differing in degree, from the seminoma ALP previously reported.
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PMID:Purification and characterization of alkaline phosphatase from human seminomas. 1035 11

Placement alkaline phosphatase (PLAP) is one of the cellular phosphatases (ALP) expressed in patients with testis cancers, particularly in seminomas. Using various techniques including Western blot and high-performance liquid chromatography (HPLC) systems and ATC2, a newly developed specific anti-PLAP monoclonal antibody (Mab), the presence of active form of PLAP in lysates prepared from testis tumour fragment and tumour cell lines, was studied. This was carried out following isolation of PLAP from biological samples using CNBr Sepharose-conjugated ATC2 beads. The results showed that: (1) The target for the newly developed Mab ATC2 was PLAP. (2) The ATC2-conjugated bead system was an efficient method for isolating pure PLAP. (3) Diethylamine (DEA), in contrast to urea and glycine, was the most efficient for separation of PLAP from ATC2-conjugated beads, as the isolated molecule did not lose any phosphatase activity and there was very little uncoupling of the ATC2 Mab from the beads. (4) ATC2-conjugated CNBr beads could pick up PLAP from a solution containing standard PLAP and lysates prepared from tumour cell lines or testis tissue fragments positive for the PLAP. (5) HPLC profile of testis tumour lines and testis tumours showed two distinct peaks with ALP activity, one at retention time 7-8 min (corresponding to 95 kDa molecule) and one at 12-13 min corresponding to 70 kDa molecule). These data demonstrated the potential use of various biochemical methods in combination with HPLC for isolation of the fully functional molecules with ALP activity from different samples including lysates prepared from patients with testis cancer. The nature of ALP activity at 95 kDa is being investigated as no such molecule has been reported previously. These techniques might have an important implication for an early detection of germ cell tumours, particularly in patients with equivocal ultrasound.
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PMID:Standardization and potential use of HPLC for detection of cellular placental alkaline phosphatase using established tumour cell lines and fresh tumour biopsies. 1074 1

It has long been thought that mammalian Sertoli cells are terminally differentiated and nondividing postpuberty. For most previous in vitro studies immature rodent testes have been the source of Sertoli cells and these have shown little proliferative ability when cultured. We have isolated and characterized Sertoli cells from human cadaveric testes from seven donors ranging from 12 to 36 years of age. The cells proliferated readily in vitro under the optimized conditions used with a doubling time of approximately 4 days. Nuclear 5-ethynyl-2'-deoxyuridine (EdU) incorporation confirmed that dividing cells represented the majority of the population. Classical Sertoli cell ultrastructural features, lipid droplet accumulation, and immunoexpression of GATA-4, Sox9, and the FSH receptor (FSHr) were observed by electron and fluorescence microscopy, respectively. Flow cytometry revealed the expression of GATA-4 and Sox9 by more than 99% of the cells, and abundant expression of a number of markers indicative of multipotent mesenchymal cells. Low detection of endogenous alkaline phosphatase activity after passaging showed that few peritubular myoid cells were present. GATA-4 and SOX9 expression were confirmed by reverse transcription polymerase chain reaction (RT-PCR), along with expression of stem cell factor (SCF), glial cell line-derived neurotrophic factor (GDNF), and bone morphogenic protein 4 (BMP4). Tight junctions were formed by Sertoli cells plated on transwell inserts coated with fibronectin as revealed by increased transepithelial electrical resistance (TER) and polarized secretion of the immunoregulatory protein, galectin-1. These primary Sertoli cell populations could be expanded dramatically in vitro and could be cryopreserved. The results show that functional human Sertoli cells can be propagated in vitro from testicular cells isolated from adult testis. The proliferative human Sertoli cells should have important applications in studying infertility, reproductive toxicology, testicular cancer, and spermatogenesis, and due to their unique biological properties potentially could be useful in cell therapy.
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PMID:Characterization and functionality of proliferative human Sertoli cells. 2105 48