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: UMLS:C0027651 (tumor)
685,946 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Five out of eight consecutive cases with initial symptoms of a 'midline granuloma' were identified as malignant histiocytosis (histiocytic sarcoma) which within 5 months to 4 years led to generalization and death. The three remaining cases also fulfilled the morphological criteria of this type of neoplasia, though these patients are still alive 1/2 to 8 years after diagnosis, possibly as a result of local radiotherapy. The age of the individuals ranged from 18 to 71 years and there was a male preponderance of 7:1. The histiocytic nature of the atypical cells was primarily documented by intense activity of NaF-inhibitable non-specific esterase, of acid phosphatase and of beta-glucuronidase as demonstrated in cryostat sections of formaldehyde-saccharose-fixed fresh biopsy specimens and by the detection of alpha-1-antichymotrypsin, alpha-1-antitrypsin, and lysozyme antigens, in that order of constancy (immunohistochemical examination of formaldehyde-fixed paraffin sections, using the avidin-biotin-peroxidase complex method). There was among the reported cases a considerable heterogeneity with regard to these 'markers'. We conclude that malignant histiocytosis is a (the?) major cause of the 'midline granuloma syndrome'.
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PMID:Malignant histiocytosis (histiocytic sarcoma). A (the?) major cause of the 'midline granuloma syndrome'. 351 40

Since it has been demonstrated that a high level of fat is a dietary factor in the etiology of colon cancer, the effect of carrageenan, a polysaccharide extracted from the red seaweeds, on 1,2-dimethylhydrazine-induced colonic tumors in rats fed a semipurified control diet containing an ordinary level of fat was studied. Nevertheless, the enhancing effect of carrageenan on colonic tumors was observed. The rats fed a carrageenan diet had approximately twice the fecal weight compared to the rats fed a control diet. While no significant differences were found in beta-glucuronidase activities in colonic mucosa, liver or plasma in the carrageenan-fed rats and controls, the activity in feces was significantly lower in the carrageenan-fed rats. At least, no beta-glucuronidase activity seemed to be related to the tumor-enhancing effect of carrageenan.
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PMID:Enhancing effect of carrageenan on the induction of rat colonic tumors by 1,2-dimethylhydrazine and its relation to beta-glucuronidase activities in feces and other tissues. 355 59

The isolated rat urinary bladder was used to study this organ's capacity to metabolize chemical carcinogens. In our experimental conditions, the urinary bladder carcinogen N-nitrosobutyl(4-hydroxybutyl)amine was oxidized to N-nitrosobutyl(3-carboxypropyl)amine. A time-dependent increase was observed in the amount of N-nitrosobutyl(3-carboxypropyl)amine formed and simultaneous disappearance of N-nitrosobutyl(4-hydroxybutyl)amine added, indicating that the bladder can metabolize N-nitrosobutyl(4-hydroxybutyl)amine to the metabolite considered responsible for tumor induction in the urinary bladder of laboratory animals. At 15, 30, 60, and 120 min the percentages of N-nitrosobutyl(3-carboxypropyl)amine formed were 11, 22, 36, and 64%, respectively, and 62, 48, 37, and 26% of N-nitrosobutyl(4-hydroxybutyl)amine remained unchanged. When N-nitrosodibutylamine was introduced into the isolated urinary bladder and incubated for 120 min, its oxidized metabolites N-nitrosobutyl(4-hydroxybutyl)amine and N-nitrosobutyl(3-carboxypropyl)amine were formed, amounting to, respectively, 0.13 and 0.06% of the substrate added. The glucuronide of N-nitrosobutyl(4-hydroxybutyl)amine was incubated in the isolated rat urinary bladder both as a buffer and as a urine solution in order to detect cellular and urinary beta-glucuronidase activity. In both systems N-nitrosobutyl(4-hydroxybutyl)amine released was about 1% at 4 h and this percentage did not increase at 6 h. N-Nitrosobutyl(3-carboxypropyl)amine was detectable at 2 h and reached 0.2% of the substrate incubated at 6 h. The results indicate that the urinary bladder may play a role in activating bladder carcinogens.
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PMID:Development of an experimental model for studying bladder carcinogen metabolism using the isolated rat urinary bladder. 359 34

The cancer chemotherapeutic efficacy of dopamine (DA) was evaluated in female strain A mice bearing transplantable Ehrlich ascites carcinoma. The results demonstrated significant inhibition of tumor growth with appreciable increase in the host survival time following DA treatment. Diminished activity of the growth-related respiratory enzyme succinate dehydrogenase along with stimulated activity of the lysosomal enzyme, beta-glucuronidase in DA-treated tumor cells indicated inhibition of tumor growth as well as active lysis of the tumor cells. The direct effect of this compound on tumor proliferation was demonstrated by marked inhibition of DNA synthesis. RNA synthesis was only marginally inhibited.
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PMID:Antitumor effect of i.p. dopamine in mice bearing Ehrlich ascites carcinoma. 359 22

The activity of beta-glucuronidase in methyl-N-nitrosourea-induced rat mammary tumors regressing after ovariectomy was studied. beta-Glucuronidase, acid phosphatase, and beta-hexosaminidase were similarly increased in the lysosome-rich fraction of regressing compared to growing tumors, whereas in the soluble fraction, a 5-fold increase in the activity of beta-glucuronidase midway regression was not paralleled by an increase in the specific activity of the other two enzymes. Results of sedimentability studies indicated an equal stability of the lysosomes at the two tumor conditions. The elevated beta-glucuronidase activity in the soluble fraction was completely precipitable by rabbit monospecific antisera against beta-glucuronidase from other species. The activity in the soluble and in the lysosome-rich fraction showed a similar pH dependence and electrophoretic mobility of immunoreactive subunits, and only minor differences in affinity towards concanavalin A:Sepharose. Thus, the increased "soluble" beta-glucuronidase activity is neither tumor nor cytosol specific. Cell death during tumor regression is believed to occur according to a controlled sequence of event, called apoptosis. Dying cells become apoptotic bodies which are further degraded during phagocytosis by neighboring tumor cells. We discuss that breakage of these bodies during homogenization of the tumor is the cause for the observed increase in soluble beta-glucuronidase activity, while the lysosomes of the ingesting tumor cells remain intact. Physiologically, the enhanced intratumoral availability of beta-glucuronidase and other lysosomal enzymes might facilitate the hydrolysis of conjugates of a variety of xenobiotics and, possibly, also of steroid hormones.
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PMID:Origin of the increased activity of beta-glucuronidase in the soluble fraction of rat mammary tumors during ovariectomy-induced regression. 360 44

Mouse peritoneal macrophages were cultured for 3 days with or without zymosan and at the same time exposed to various inhibitors of cellular metabolism. The cells were assayed for selective release of a lysosomal enzyme, and for cytotoxic activity against a tumor cell line, L-929-cells. Selective release of beta-glucuronidase was demonstrated in the supernatants from zymosan-stimulated macrophages. The stimulated macrophages were cytotoxic for the tumors cells, evaluated by measuring release of radioactivity during subsequent 4 days' co-culture of macrophages and 14C-thymidine-labelled tumor cells, and by counting cells per culture. Colchicine caused a slight, variable reduction in enzyme release and no change in cytotoxic effect from stimulated macrophages. Monensin decreased extracellular enzyme secretion and reduced the cytotoxicity in stimulated macrophages to control levels. Chloroquine caused a similar reduction in lysosomal enzyme release and cytotoxic activity in zymosan-stimulated cells. This inhibitor increased the enzyme release from control cells and induced a small, variable cytotoxic effect from these cells. The data indicate co-variation between macrophage-mediated cytotoxicity and a secretory process which can be blocked by monensin. The need for intact lysosomal function was also demonstrated.
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PMID:Cytotoxic activity of stimulated mouse macrophages exposed to various inhibitors. 371 7

We found a tumor metastasis-associated heparan sulfate (HS)-degrading endoglycosidase in melanoma cells that is a unique endo-beta-glucuronidase (heparanase) capable of specifically cleaving HS at intrachain sites (M. Nakajima, T. Irimura, N. DiFerrante, and G. L. Nicolson, 1984, J. Biol. Chem. 259, 2283-2290). To perform rapid and microscale quantitative assays of heparanase we developed a solid-phase HS substrate by crosslinking radiolabeled HS onto agarose gel beads using one covalent linkage. The HS from bovine lung was partially N-desulfated and labeled with [14C]acetic anhydride. Free HS amino groups were completely acetylated, and reducing terminal saccharides were reductively aminated. The HS derivatives with amino groups at their reducing termini were coupled to amino-reactive agarose beads. Incubation of the solid-phase HS substrates with B16 melanoma cell extracts in the presence of D-saccharic acid 1,4-lactone (a potent exo-beta-glucuronidase inhibitor) resulted in the time- and dose-dependent release of [14C]HS fragments. Human melanoma cell lines were tested for HS-degrading endoglycosidase using the newly developed solid-phase HS substrates. The human malignant melanoma cells tested had high levels of HS-degrading activity that were comparable to those of highly metastatic murine B16-F10 melanoma cells.
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PMID:A solid-phase substrate of heparanase: its application to assay of human melanoma for heparan sulfate degradative activity. 376 58

A chemotactic factor was identified in the supernatants of human large granular lymphocytes (LGL) activated by a glutaraldehyde-fixed NK-sensitive tumor, K562. The factor stimulated migration of human LGL, rat alveolar macrophage (RAM), and human monocytes and neutrophils (PMN). The locomotor response was chemotactic and chemokinetic on the basis of unidirectional migration in concentration gradients. The cell producing the factor was detected exclusively in LGL-rich Percoll fraction coincident with the peak of NK lytic activity and HNK-1+ cells. The monoclonal phenotype of the cell was HNK-1+, partially OKT-11+, OKM-1-, OKT-3-, OKT-4-, and OKT-8-. The factor was released by LGL within 20 min of incubation with Sr++, a cation that is able to induce LGL degranulation. A powerful chemoattractant was also detected in the granules of the rat LGL leukemia, RNK. Chemotactic activity coincided with granule enzyme beta-glucuronidase and cytolysin after RNK nitrogen cavitation and Percoll fractionation of subcellular constituents. The RNK granule chemoattractant induced unidirectional migration of human LGL and was also active against rat alveolar macrophages and human PMN. Anti-RNK granule antibody conjugated to Sepharose 4B was able to deplete the chemotactic activity from both K562-induced LGL supernatants and solubilized RNK granules. These observations indicate that a leukocyte chemotactic factor (NK-LCF) is present in NK cell granules and is probably released after tumor-induced granule exocytosis.
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PMID:NK-leukocyte chemotactic factor (NK-LCF): a large granular lymphocyte (LGL) granule-associated chemotactic factor. 377 4

Circulating macrophages and metastatic tumor cells can penetrate the vascular endothelium and migrate from the circulatory system to extravascular compartments. Both activated murine macrophages and different metastatic tumor cells (B16-BL6 melanoma; ESb T-lymphoma) attach, invade, and penetrate confluent vascular endothelial cell monlayer in vitro, by degrading heparan sulfate proteoglycans in the subendothelial extracellular matrix. The sensitivity of the enzymes from the various sources degrading the heparan sulfate proteoglycan was challenged and compared by a series of inhibitors. Activated macrophages demonstrate a heparanase with an endoglycosidase activity that cleaves from the [35S]O4 = -labeled heparan sulfate proteoglycans of the extracellular matrix 10 kDa glycosaminoglycan fragments. The macrophages do not store the heparanase intracellularly but it is instead found pericellularly and requires a continuous cell-matrix contact at the optimal pH for maintaining cell growth. The degradation of [35S]O4 = -labeled extracellular matrix proteoglycans by the macrophages' heparanase is significantly inhibited in the presence of heparan sulfate (10 micrograms/ml), arteparon (10 micrograms/ml), and heparin at a concentration of 3 micrograms/ml. In contrast, other glycosaminoglycans such as hyaluronic acid, dermatan sulfate, and chondroitin sulfate as well as the specific inhibitor of exo-beta-glucuronidase D-saccharic acid 1,4-lactone failed to inhibit the degradation of sulfated proteoglycans in the subendothelial extracellular matrix. Degradation of this heparan sulfate proteoglycan is a two-step sequential process involving protease activity followed by heparanase activity. However, the following antiproteases--alpha 2-macroglobulin, antithrombin III, leupeptin, and phenylmethylsulfony fluoride (PMSF)--failed to inhibit this degradation process, and only alpha 1-antitrypsin inhibited the heparanase activity. B16-BL6 metastatic melanoma cell heparanase, which is also a cell-associated enzyme, was inhibited by heparin to the same extent as the macrophage heparanase. On the other hand, heparanase of the highly metastatic variant (ESb) of a methylcholanthrene-induced T lymphoma, which is an extracellular enzyme released by the cells to the incubation medium, was more sensitive to heparin and arteparon than the macrophages' heparanase, inhibited at concentrations of 1 and 3 micrograms/ml, respectively. These results may indicate the potential use of heparin or other glycosaminoglycans as specific and differential inhibitors for the formation in certain cases of blood-borne tumor metastasis.
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PMID:Murine macrophage heparanase: inhibition and comparison with metastatic tumor cells. 380 31

A new technique was applied to the study of human osteosarcoma. Ten slices of 10 micron were cut serially from 2 X 2 X 6 mm shock frozen blocks of human osteosarcoma for chemical analysis. Before and after each series of 10 slices, one slice of 10 micron was separated for morphological analysis. Four different types of osteosarcoma were investigated: Case 1 was an atypical osteoblastic osteosarcoma, case 2 a small cell sclerosing osteosarcoma, case 3 a well-differentiated parosteal osteosarcoma grade I, and case 4 a highly malignant anaplastic osteosarcoma. Alkaline phosphatase, acid phosphatase, beta-glucuronidase and proteolytic activities were analysed as well as matrix collagen and hexosamine, phosphorus (Pi and Po), protein, DNA, and water content. In accordance with the morphology, the obtained data illustrate the great heterogeneity of osteosarcomas. Although case 1, 2 and 3 all represent calcifying types of the tumor, characteristic differences exist with regard to the matrix and the degree of calcification. In contrast to these three, case 4 presents a noncalcified type of osteosarcoma whose matrix contains relatively high amounts of hexosamine and low amounts of collagen, whereas DNA and water contents are high. The data from the analysis of osteosarcoma were compared with previous results from the calf epiphyseal growth plate in order to define differences and similarities between the formation of tumor bone and the physiological formation of hard tissue.
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PMID:Biological characterization of human bone tumors. IV. Combined biochemical and histological analyses of different osteosarcomas. 386 64


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