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)

The mesodermal clone C1 was derived from the multipotent embryonal carcinoma 1003 cell line transformed with the plasmid pK4 carrying SV40 oncogenes under the control of the adenovirus E1A promoter. We have shown that the C1 clone becomes committed to the osteogenic pathway when cultured in aggregates in the presence of mediators of the osteogenic differentiation. To further validate C1 as a model with which to study osteogenesis in vitro the kinetics of its differentiation was studied, focusing on the histology of the aggregates and on the expression of a set of genes corresponding to representative bone matrix proteins. The presence of ascorbic acid and beta- glycerophosphate specifically leads to mineralization in almost 100% of the aggregates. Transcription of the above genes, silent in exponentially growing cells, specifically occurred with the establishment of cell-cell contacts independently of the presence of ascorbic acid and inorganic phosphate. The latter, however, were absolutely required for matrix deposition and mineralization. In their presence, one observed an overall decline in type I collagen and alkaline phosphatase transcripts while osteocalcin and osteopontin transcripts preferentially accumulated in cells lining the mineralizing foci. Concomitantly, type I collagen and osteocalcin became extracellularly deposited. The osteogenic differentiation of C1 occurred while cells were still proliferating. The C1 clone thus behaves as a mesodermal stem cell, becoming committed to the osteogenic pathway upon: firstly, establishment of cellular contacts; and secondly, addition of ascorbate and beta-glycerophosphate. It therefore appears to be a promising in vitro system for deciphering the molecular basis of osteoblast ontogeny.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Commitment of the teratocarcinoma-derived mesodermal clone C1 towards terminal osteogenic differentiation. 828 57

An immunohistopathological study using monoclonal antibodies for alkaline phosphatases demonstrated placental alkaline phosphatase (PLAP)-like substance in the tumor cells of 11 pure seminomas, 1 seminoma with embryonal carcinoma and 1 seminoma metastasis. Liver alkaline phosphatase (LAP) could also be demonstrated in all seminomas but a third intestinal alkaline phosphatase (IAP) was not demonstrable in any tumor. The PLAP-like substance and LAP had considerable enzyme activities. This provides two tumor markers of seminomas detectable in histopathological specimens.
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PMID:Immunopathology of alkaline phosphatase isozymes in seminoma. 843 23

Osteogenic protein-1 (OP-1, BMP-7), a bone morphogenetic protein in the transforming growth factor-beta superfamily, induces endochondral bone formation in vivo, but the mechanism of action of OP-1 in osteogenesis is not yet established. Three murine clonal cell lines in different stages of differentiation exhibit graded responses to recombinant human OP-1: the mouse embryonal carcinoma ATDC5 cell, with potential for chondroblastic differentiation; the osteoblast-like MC3T3-E1 cell derived from mouse calvaria; and the multipotent fibroblastic C3H10T1/2 cell derived from mouse embryo connective tissue. We show that OP-1 acts on early stage mesenchymal progenitor cells (ATDC5, C3H10T1/2) to induce chondroblastic differentiation, while OP-1 strongly enhances the osteoblastic phenotype of committed osteoblasts (MC3T3-E1), possibly explaining its induction of the endochondral ossification cascade in vivo. Markers of osteoblastic, chondroblastic, and adipocytic differentiation are compared. OP-1 is strongly mitogenic for ATDC5, showing dose-dependent (2.5-80 ng/ml) induction of Alcian blue staining, alkaline phosphatase activity, and mRNA expression for collagen types II and IX, and matrix Gla protein. MC3T3-E1 cells do not proliferate or stain with Alcian blue in response to OP-1, but express elevated levels of alkaline phosphatase and osteocalcin. While low-dose OP-1 treatment of C3H10T1/2 induces only adipocyte-like cells filled with lipid droplets, a high dose (500 ng/ml) causes the same cells to also exhibit chondrocytic properties. Thus, OP-1 can induce differentiation along elements of the endochondral ossification pathway according to the stage and potential of the target cell.
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PMID:Human osteogenic protein-1 induces chondroblastic, osteoblastic, and/or adipocytic differentiation of clonal murine target cells. 854 71

The pattern of cell surface antigen expression of a set of cell lines derived from human germ cell tumours and corresponding to various cell phenotypes found within these tumours was studied using immunofluorescence. Twenty-two different antibodies were used. Many of these antibodies have been noted to recognise epitopes that are either preferentially expressed by embryonal carcinoma (EC) cells, or by more differentiated cell types. Using scatter plots and rank correlations, 6 groups of antibodies were distinguished with respect to their staining patterns on the cell lines tested. Several antibodies showed a specific staining pattern in relation to the differentiation state of the cells. Two groups of antibodies included those recognising high m.w. glycoproteins (antibodies TRA-1-60, TRA-1-81, GCTM2, 3-177, K4 and K21) and the ganglioseries glycolipid antigens SSEA-3 and -4 (antibodies MC631 and MC813-70). These antibodies mostly stained EC cells but not other cell types, confirming previously published data. However, one of these groups, comprising antibodies K4 and MC631, was more exclusively associated with the EC cell phenotype than was the other group. Antibodies recognising the liver isozyme of alkaline phosphatase (TRA-2-49 and TRA-2-54) also reacted strongly with most EC cell lines, although they reacted significantly with a number of other cell lines as well, whereas antibodies to the placental isozyme tended to react only weakly with EC cells. The antibodies recognising the ganglioseries glycolipids GD2 and GD3 (VIN2PB22 and VINIS56) preferentially stained cells with neuroectodermal characteristics. Other antibodies showed a heterogeneous staining pattern for the cell lines with different phenotypes. The data obtained from the cell lines were, in general, similar to data obtained from immunohistochemical studies on tissue sections of primary germ cell tumours of the adult testis, including carcinoma in situ.
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PMID:Comparative analysis of cell surface antigens expressed by cell lines derived from human germ cell tumours. 864 54

Four examples of spermatocytic seminoma with a predominant anaplastic component occurred in men 33 to 43 years of age, without histories of cyptorchidism. The seminomas presented with painless testicular masses recognized 3 to 18 months before orchiectomy. Preoperative serum measurements of human chorionic gonadotropin and alpha-fetoprotein were negative. All tumors contained areas (10% to 30% of the tumor) in which the three cell types characteristic of conventional spermatocytic seminoma could be identified under light microscopy. The predominant anaplastic component also contained the three cell types, but the nuclei had prominent nucleoli with granular and filamentous chromatin. In addition, sheets of cells with vesicular nuclei and prominent nucleoli superficially resembling embryonal carcinoma were found. There were numerous large mononuclear and multinucleated giant cells with bizarre nuclei and prominent nucleoli, but no sarcomatous elements. Many normal and abnormal mitotic figures were present. Tunical and vascular invasion and extensive necrosis were constant features. Immunohistochemistry documented p53 protein overexpression in two tumors, but neoplastic cells were negative with immunostains for placenta-like alkaline phosphatase, leukocyte common antigen, neuron-specific enolase, alpha-fetoprotein, human chorionic gonadotropin, vimentin, and cytokeratins. Ultrastructural examination of the anaplastic component showed large rope-like nucleoli, but the cytoplasmic features were similar to those of conventional spermatocytic seminoma. Despite the presence of a major anaplastic component, no patient has developed metastasis. Larger series and longer follow-up are needed to understand the natural history of these neoplasms.
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PMID:Anaplastic variant of spermatocytic seminoma. 869 7

We report the derivation of eight pluripotent cell lines from common marmoset (Callithrix jacchus) blastocysts. These cell lines are positive for a series of markers (alkaline phosphatase, SSEA-3, SSEA-4, TRA-1-60, and TRA-1-81) that characterize undifferentiated human embryonal carcinoma cells and rhesus embryonic stem cells. All eight cell lines had a modal chromosome number of 46; seven cell lines were XX and one was XY. Two cell lines (Cj11 and Cj62) were cultured continuously for over a year and remained undifferentiated and euploid. In the absence of fibroblast feeder layers, these cell lines differentiated to multiple cell types, even in the presence of leukemia inhibiting factor. Differentiated cells secreted bioactive CG into the culture medium and expressed alpha-CG, beta-CG, and alpha-fetoprotein mRNA, indicating trophoblast and endoderm differentiation. Bioactive CG secretion in differentiating cells was increased substantially in the presence of GnRH agonist D-Trp6-Pro9-NHEt. When grown at high densities, these cells formed embryoid bodies with a close resemblance to early postimplantation embryos, including the formation of a yolk sac, amnion, and an embryonic disc with an early primitive streak. These results make these pluripotent cells strong candidates for marmoset embryonic stem cells.
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PMID:Pluripotent cell lines derived from common marmoset (Callithrix jacchus) blastocysts. 882 27

Tumor and surrounding testicular tissue from six seminomas and one combined seminoma/embryonal carcinoma were examined for the expression of ICAM-1, VCAM-1 and ELAM-1. This was done by immunohistochemical staining of frozen samples using monoclonal antibodies and the avidin-biotin/ peroxidase or alkaline phosphatase staining method. ICAM-1 was expressed by Sertoli cells of intratubular germ cell neoplasia, but not by any of the cells in normal seminiferous epithelium, or by neoplastic germ cells whether invading or not. In addition inflammatory cells and endothelium expressed ICAM-1. VCAM-1, and also occasionally ELAM-1, was expressed only on endothelial cells in and outside the tumors. These results are discussed in relation to lymphocytic infiltration and immune surveillance of seminomas and T-cell tolerance to the antigens of the immunologically privileged seminiferous epithelium.
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PMID:Sertoli cells, but not tumor cells, of seminoma in situ express ICAM-1. 898 45

We have developed a reverse transcription-PCR method that clearly distinguishes between the RNA transcripts of all four alkaline phosphatase (AP) genes. If compared to the methods used up to the present, the main advantages of the reverse transcription-PCR method presented are its specificity and high sensitivity. The germ cell AP and the placental AP, which are the two most closely related AP isoenzymes (98% homology), can clearly be distinguished without any interference by other AP isoenzymes. An enhanced expression of AP isoenzymes has been reported for various tumors. The examination of the pattern of AP isoenzyme expression in a specific tumor and the corresponding tissue of origin enables discrimination between eutopically and ectopically expressed isoenzymes and thus represents an important tool in the elucidation of AP isoenzymes as potential tumor markers. The pattern of AP expression in 15 germ cell tumors, 2 germinal epithelia adjacent to seminoma, 2 cell lines of germ cell tumor origin (Tera-1 and BeWo), and 5 normal testes was studied. In comparison to normal testes, in all seminomatous germ cell tumors eutopic expression of germ cell AP and ectopic expression of tissue-nonspecific AP were demonstrated. In both samples of pure embryonal carcinoma and in the embryonal carcinoma cell line, the transcription of all four mRNAs was shown. These results indicate that the expression of the isoenzymes depends on the degree of differentiation of a tumor and that a simultaneous up-regulation of all AP isoenzymes in all types of germ cell tumors does not exist.
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PMID:Simultaneous detection of all four alkaline phosphatase isoenzymes in human germ cell tumors using reverse transcription-PCR. 928 97

The growth-arrest genes (gas and gadd) are widely expressed during mammalian embryogenesis and may be useful as markers of nutritional stress in the embryo. F9 embryonal carcinoma cells have been used to characterize the effect of serum or amino acid deficiency on growth-arrest gene expression in a differentiating embryonic cell. The differentiation markers, homeobox B2 (HoxB2), collagen type IV and laminin B2, were not induced by growth arrest. Treatment with all-trans retinoic acid (RA) produced a dose-dependent increase in alkaline phosphatase activity, which was unchanged in lysine-deficient medium and reduced in low-serum medium. Low-serum medium also reduced HoxB2 expression. There was a transient 2-6-fold increase in mRNAs for C/EBP-beta, gadd153/CHOP-10 and gas5 genes 24 h after transfer to amino-acid-deficient media. The mRNAs for the gas2 and gas6 genes began to rise slowly by 5-10-fold after a delay of approx. 24 h. The transient increases did not occur in low-serum medium where there was a much smaller and slower increase. Differentiation caused 1-2-fold increases in gas2, gas3 and gas6 mRNA levels. The transient overexpression of gas5, gadd153/CHOP-10 and CCAAT-enhancer-binding protein-beta, and the later expression of gas6 mRNAs in response to amino acid deficiency, were not affected by differentiation. RA treatment increased the expression of gas3 and caused gas2 to be transiently overexpressed in amino-acid-deficient medium. Differentiation in serum-deficient medium did not significantly alter the levels of the growth-arrest gene mRNAs. These results show that in F9 cells the growth-arrest genes are expressed sequentially as a result of nutrient stress.
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PMID:Effects of nutrient deprivation and differentiation on the expression of growth-arrest genes (gas and gadd) in F9 embryonal carcinoma cells. 946 58

Activin A and osteogenic protein-1 (OP-1) exerted antagonistic effects on each other's responses on the human Tera-2 embryonal carcinoma cell line. OP-1 dose dependently inhibited activin A-induced activation of p3TP-Lux transcriptional reporter, containing part of the human plasminogen activator inhibitor-1 (PAI-1) promoter, while activin A inhibited OP-1-mediated alkaline phosphatase induction. Approximately equimolar concentrations of both growth factors resulted in 50% inhibition of the respective biological responses. Affinity cross-linking studies using 125I-activin A or 125I-OP-1 followed by receptor-immunoprecipitations revealed that both ligands bound to the activin type II receptor (ActR-II), but recruited different type I receptors. In addition, OP-1 competed with binding of 125I-activin A, and activin A competed with binding of 125I-OP-1 to ActR-II. Transient transfection studies showed that competition between activin A and OP-1 also occurred at the type I receptor (ActR-1) level; constitutively active (CA)-ActR-I inhibited CA-ActR-IB-mediated p3TP-Lux reporter induction. There was no competition between activin A and OP-1 for availability of Smad4, indicating that the concentration of this common signal transducer is not limiting for generating the observed biological responses. Overexpression of ActR-II abolished the inhibitory effect of OP-1 on activin A-induced p3TP-Lux activation and, surprisingly, led to OP-1-induced transcriptional reporter activity. Whereas the exact mechanism of competition is unclear, the role of ActR-II in the competition between activin A and OP-1 is discussed in light of the observed interference in downstream signaling by CA-ActR-I and CA-ActR-IB.
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PMID:Functional antagonism between activin and osteogenic protein-1 in human embryonal carcinoma cells. 1039 83


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