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)

Dunn osteosarcomas synthesize 2 times more alkaline phosphatase than do Ridgeway osteosarcomas, 3 times more than do HeLa cells, and 4 to 5 times more than do rat or mouse fibroblast cell cultures. Implants of killed freeze-dried Dunn cell cultures into the thigh muscles are resorbed and replaced by normal cartilage, bone, and bone marrow tissue, while implants of freeze-dried Ridgeway cells are resorbed and replaced by fibrous tissue only. Outgrowths of normal muscle septum connective tissue cells onto the stroma of Ridgeway tumors differentiate into fibrous tissue. Cultures of either tumor on a substratum of bone matrix stroma prepared from normal bone proliferate, assume a spherical shape, and perpetuate the transformed osteoblast-like cell without forming attachments or adapting to the contour of the substratum. Outgrwoths of muscle mesenchymal cells on the Dunn tumor stroma differentiate into cartilage. Dunn osteosarcoma cell cultures proliferate on the inside and produce deposits of normal bone (not tumorous bone) on the outside of diffusion chambers. Killed freeze-dried cell cultures produce transfilter deposits of normal bone and bone marrow, but the quantity is significantly lower. On a substratum of cellulose acetate, outgrowths of muscle connective tissue will differentiate into cartilage when cell-free Dunn stroma is present under the organ culture grid. Tumorigenesis and normal cartilage and bone morphodifferentiation are antithetic, but tumor cells transfer a bone morphogen similar to the bone morphogenetic protein (BMP) of normal bone matrix. BMP recruits mesenchymal cells to proliferate and differentiate into cartilage and bone.
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PMID:Osteogenesis and chondrogenesis in transplants of Dunn and Ridgway osteosarcoma cell cultures. 27 82

Serum levels of alkaline phosphatase (AP) have been used in the clinical evaluation of numerous diseases, including malignancies, for half a century. The aberrant expression of AP genes in cancer cells has led to the suggestion that APs are oncofetal proteins and thus, could be involved in tumorigenesis. Tumors which express these AP isozymes can be broadly divided into two groups: (a) those with an enhanced production of an isozyme normally expressed in the tissue (eutopic expression) and (b) those showing expression of one or more isozymes not identified in the normal tissue (ectopic expression). Moreover, many tumors show simultaneous expression of two or more different AP isozymes. In the absence of known biological functions of the AP isozymes several different mechanisms underlying their expression in tumor cells could explain the findings. In an attempt to clarify the function of APs, this laboratory is engaged in the study of unique properties of the mammalian APs as possible clues to their function, i.e., (a) the phosphatidylinositol glycan attachment of APs to the cytoplasmic membrane, (b) the uncompetitive inhibition properties of APs and (c) the extracellular matrix binding domain of APs. This laboratory is also undertaking the task of targeting each of the mouse AP isozymes by homologous recombination to generate mouse models of hypophosphatasia to analyze in detail the in vivo consequences of AP isozyme deficiencies.
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PMID:Alkaline phosphatase as a reporter of cancerous transformation. 139 34

The influence of sodium chloride (NaCl), miso (Japanese soybean paste) and ethanol on development of intestinal metaplasia was examined. Five-week-old male CD(SD): Crj rats were treated with two 10 Gy doses of X-rays to the gastric region at a 3-day interval (total 20 Gy). After irradiation, the rats received supplementation with NaCl (1% or 10% in diet), miso (10% in diet) or ethanol (10% in drinking water) for 12 months. The number of alkaline phosphatase-positive foci of intestinal metaplasia in rats given 1% NaCl diet (Group 3) after X-rays was significantly elevated as compared to that in rats given X-rays alone (Group 1) (P < 0.01) or X-rays with 10% NaCl (Group 2) (P < 0.01). In the pyloric gland mucosae, the total numbers of metaplastic foci in rats of Group 3 were much higher than in Group 2, or after miso diet (Group 4) or ethanol supplementation (Group 5) (P < 0.01), but no difference was found between Group 2, 4 or 5 and Group 1. Atypical hyperplasia only appeared at incidences of less than 6% in Groups 1-3 and no promoting effect on gastric tumorigenesis was evident in Group 2. The present results thus showed that the occurrence of intestinal metaplasia induced by X-irradiation can be significantly increased by administration of 1% NaCl and decreased by 10% NaCl and ethanol, but this is not associated with any influence on gastric neoplasia.
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PMID:The effects of sodium chloride, miso or ethanol on development of intestinal metaplasia after X-irradiation of the rat glandular stomach. 148 41

Alveolar type II cells were isolated from fetal mouse lung by differential adherence and obtained in monolayer culture. Cultures display a high degree of purity as shown by histochemical and immunocytochemical staining procedures. Seventy-five percent of cells stained positive with specific anti-lavage serum mouse (SALS-M), an antiserum specific for (pre)alveolar type II cells of the mouse, and osmiophilic bodies were present in 82% of cells. These and other characteristics of type II cells in culture correspond to those of alveolar type II cells in fetal mouse lung. The pattern of reactivity of these cells with various anti-cytokeratin antibodies is described, and we show that, in contrast to rat type II cells, they do not exhibit alkaline phosphatase activity. Identity of the type II cell cultures was shown by their specific phospholipid composition and surfactant protein A (SP-A) content. The fetal alveolar type II cells in culture were found to synthesize and express class I but not class II major histocompatibility complex (MHC) antigens. The possibility to culture fetal alveolar type II cells of the mouse and the availability of genetically well-defined inbred and transgenic mouse strains opens ways to study the genetics of type II cell differentiation and function. Also, the in vitro availability of alveolar type II cells, the progenitor cells of mouse lung tumors, will enable us to study in vitro several of the processes involved in lung tumorigenesis in the mouse.
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PMID:Fetal mouse alveolar type II cells in culture express several type II cell characteristics found in vivo, together with major histocompatibility antigens. 169 1

An improved method for in situ hybridization was developed in order to identify the tissue-specific expression of messenger RNA (mRNA) for the novel extracellular matrix glycoprotein, tenascin, during mouse development. Non-radioactive RNA probes were generated by incorporating digoxigenin-11-UTP instead of conventional isotopic labels. Hybridization of anti-sense probes to complementary mRNAs was detected by a chromogenic staining reaction catalyzed by an anti-digoxigenin antibody-alkaline phosphatase conjugate. Markedly improved enhancement of staining was achieved by expanding the complexity of probes and strictly controlling the degree of proteolytic digestion of paraformaldehyde-fixed tissue sections. Six different complementary RNA (cRNA) probes representing most of the tenascin mRNA sequence were prepared. Very weak signals were obtained after single applications of each probe, but strong specific signals were present when all six probes were mixed together. In either case, no signal was found without prior proteolytic digestion of tissue sections with proteinase K. Treatment with increasing concentrations of proteinase K initially resulted in increased sensitivity of signal detection, but extensive digestion resulted in histological sections of poor quality for light microscopy. Optimal conditions varied according to the tissue type examined. In lung, in situ hybridization detected tenascin mRNA in the relatively large cells lining alveolar walls adjacent to type I pneumocytes. In cerebellum, glial cells of the Purkinje cell layer contained tenascin mRNA, but Purkinje cells did not. In both cases, hybridization signals were confined to the cytoplasm of cells, and no extracellular staining was observed. This method provides a promising new tool for analysis of spatio-temporal regulation of tenascin gene expression during embryogenesis and oncogenesis.
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PMID:In situ hybridization with non-radioactive digoxigenin-11-UTP-labeled cRNA probes: localization of developmentally regulated mouse tenascin mRNAs. 171 91

Ornithine decarboxylase (ODC) was separated, using diethylamino-ethyl ion-exchange chromatography, into multiple peaks of activity. We investigated the isoforms of ODC during 1,2-dimethylhydrazine-induced colon carcinogenesis and in human colon tumors. ODC in both mouse and human normal-appearing colonic mucosa was consistently separated into two active peaks by diethylaminoethyl-Sepharose CL-6B column chromatography. The major peak (Peak I) contained about 75% of the mouse and 72% of the human colonic mucosal ODC activity. During and after 10 weekly injections of 1,2-dimethylhydrazine (20 mg/kg, i.p.), colonic ODC activity was significantly enhanced with induction of both peaks but with a more significant increase in Peak II. ODC activity in both 1,2-dimethylhydrazine-induced and human colon tumors was significantly higher compared with the normal colon mucosa. The chromatographic profile of tumors showed the predominance of the second peak. Furthermore, the chromatographic profile of ODC after alkaline phosphatase treatment yielded an elution of only one peak coincident with the Peak I and the disappearance of Peak II. The second peak of ODC (the phosphorylated form) may be a specific isoform associated with colon tumorigenesis and tumor growth.
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PMID:Heterogenicity of ornithine decarboxylase during mouse colon carcinogenesis and in human colon tumors. 200 26

The activities of alkaline phosphatase and phosphoamino acid phosphatases were measured in normal and cancerous regions of the human larynx. For each larynx, alkaline phosphatase and phosphotyrosine phosphatase activities were higher in the tumor than in the corresponding normal tissue. Phosphothreonine and phosphoserine phosphatase activities were relatively low and there were no consistent trends. The increased alkaline phosphatase activity in the tumors supports histological observations that ossification of cartilage seems to occur at the site of invasion; the phosphatase acting on phosphotyrosine could serve as a regulator of cell differentiation during tumorigenesis.
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PMID:Alkaline phosphatase and phosphoamino acid phosphatases in normal and cancerous tissues of the human larynx. 231 Jun 11

Binding of fibronectins to gangliosides was tested directly using several different in vitro models. Using an enzyme-linked immunoabsorbent assay (ELISA), gangliosides were immobilized on polystyrene tubes and relative binding of fibronectin was estimated by alkaline phosphatase activity of conjugated second antibody. Above a critical ganglioside concentration, the gangliosides bound the fibronectin (GT1b congruent to GD1b congruent to GD1a greater than GM1 much greater than GM2 congruent to GD3 congruent to GM3) in approximately the same order of efficiency as they competed for the cellular sites of fibronectin binding in cell attachment assays (Kleinman et al., Proc natl acad sci US 76 (1979) 3367). Alternatively, these same gangliosides bound to immobilized fibronectin. Rat erythrocytes coated with gangliosides GM1, GD1a or GT1b bound more fibronectin than erythrocytes not supplemented with gangliosides. Using fibronectin in which lysine residues were radioiodinated, an apparent Kd for binding to mixed rat liver gangliosides of 7.8 X 10(-9) M was determined. This value compared favorably with the apparent Kd for attachment of fibronectin to isolated plasma membranes from rat liver of 3.7 X 10(-9) M for fibronectin modified on the tyrosine residue, or 6.4 X 10(-9) M for fibronectin modified on lysine residues. As shown previously by Grinnell & Minter (Biochem biophys acta 550 (1979) 92), fibronectin modified on tyrosine residues did not promote spreading and attachment of CHO cells. It did, however, bind to cells. In contrast, lysine-modified fibronectin both bound to cells and promoted cell attachment. Plasma membranes isolated from hepatic tumors in which the higher gangliosides that bind fibronectin were depleted bound 43-75% less [125I]fibronectin than did plasma membranes from control livers. The findings were consistent with binding of fibronectins to gangliosides, including the same gangliosides depleted from cell surfaces during tumorigenesis in the rat.
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PMID:Fibronectin binding to gangliosides and rat liver plasma membranes. 394 47

The in vitro effects of dimethyl sulfoxide (DMSO) on MGC 80-3 cells were studied by light microscopy, transmission electron microscopy and biochemical methods. The results indicated that the inhibitory effects of DMSO on the growth of MGC 80-3 cells was concentration dependent and 1.5% DMSO was suitable in the present study. The growth rate, mitotic index, colony forming efficiency and Con A-aggregation of the cells treated with 1.5% DMSO in vitro for 7 days was reduced respectively by 35.15%, 18/1000, 90% and 55.8%. It was remarkable that the activity of membrane-associated alkaline phosphatase, which is not presented in normal human gastric mucosa, was decreased by 90% in the treated cells. There was a 75% decrease of the rate of tumorigenesis in the treated cells as compared with the tumorigenic rate of the untreated MGC 80-3 cells inoculated into nude mice. Gross morphological changes of MGC 80-3 cells treated with 1.5% DMSO were evident including enlargement and flatness of the cells, stumpy microvillies instead of long and rigid ones, and extremely well-developed Golgi apparatus and rough endoplasmic reticulum. This data indicated that DMSO was able to induce differentiation of MGC 80-3 cells and change their malignant phenotypes.
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PMID:[DMSO induced differentiation of human gastric adenocarcinoma cell line MGC 80-3]. 780 21

Although the majority of genes required for the transfer of T-DNA from Agrobacterium tumefaciens to plant nuclei are located on the Ti plasmid, some chromosomal genes, including the recently described acvB gene, are also required. We show that AcvB shows 50% identity with the product of an open reading frame, designated virJ, that is found between the virA and virB genes in the octopine-type Ti plasmid pTiA6. This reading frame is not found in the nopaline-type Ti plasmid pTiC58. acvB is required for tumorigenesis by a strain carrying a nopaline-type Ti plasmid, and virJ complements this nontumorigenic phenotype, indicating that the products of these genes have similar functions. A virJ-phoA fusion expressed enzymatically active alkaline phosphatase, indicating that VirJ is at least partially exported. virJ is induced in a VirA/VirG-dependent fashion by the vir gene inducer acetosyringone. Primer extension analysis and subcloning of the virJ-phoA fusion indicate that the acetosyringone-inducible promoter lies directly upstream of the virJ structural gene. Although the roles of the two homologous genes in tumorigenesis remain to be elucidated, strains lacking acvB and virJ (i) are proficient for induction of the vir regulon, (ii) are able to transfer their Ti plasmids by conjugation, and (iii) are resistant to plant wound extracts. Finally, mutations in these genes cannot be complemented extracellularly.
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PMID:The octopine-type Ti plasmid pTiA6 of Agrobacterium tumefaciens contains a gene homologous to the chromosomal virulence gene acvB. 786 May 97


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