Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0001418 (adenocarcinoma)
 68,496 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A case of primary adenocarcinoma of the urinary bladder occurring in a patient with type 1 multiple endocrine adenomatosis (MEA) is presented. The patient was a 36-year-old female who had a past history of type 1 multiple endocrine adenomatosis, namely, adenomatosis of the parathyroid gland, insulin and gastrin-producing adenomatosis of the pancreas, and prolactin-producing pituitary adenoma. She was admitted in January 1981 with the complaints of gross hematuria, pollakisuria and micturition pain lasting for about one year and a half. Cystoscopic examination revealed four solid tumors in the posterior and left lateral walls of the bladder with diffuse mucosal hyperemia. Biopsy of the tumors disclosed that they were adenocarcinoma. Clinical examinations revealed that there was no extravesical primary malignant neoplasm in this case. Radical cystectomy with urinary diversion by ileal conduit was performed on January 22, 1981. Histological examination revealed that the tumor was adenocarcinoma originating from the vesical mucosa. Follow-up for over three years since the time of surgery has not shown any sign of tumor recurrence or occurrence of extravesical malignant neoplasm. In addition, 28 cases of primary adenocarcinoma of urinary bladder in Japan reported during the last 25 years are reviewed and analyzed.
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PMID:[A case of primary adenocarcinoma of the urinary bladder occurring in a patient with type 1 multiple endocrine adenomatosis (MEA)]. 286 84

A single dose of dimethylbenz[a]anthracene (DMBA) at 20 mg/kg resulted in 100% incidence of intraductal mammary adenocarcinomas in Wistar rats, the large tumors averaging 1.87 +/- 0.45 g. gamma-Glutamyltranspeptidase activities were elevated in DMBA-induced mammary adenocarcinomas relative to lactating mammary tissue in all fractions examined: 18.8-fold in homogenates; 22.1-fold in particulate fractions; and 5.7-fold in supernatant fractions. In DMBA-induced mammary adenocarcinomas, gamma-glutamyltranspeptidase was 95% particulate, 5% supernatant, whereas in lactating mammary tissue, gamma-glutamyltranspeptidase was equally distributed between particulate and supernatant fractions. Particulate gamma-glutamyltranspeptidase from DMBA-induced mammary adenocarcinomas as well as lactating mammary tissue displayed classical Michaelis-Menten characteristics: for the adenocarcinoma enzyme Km was 2.5 nM and Vmax 200 nmol mg-1 min-1; for mammary tissue enzyme Km was 2.5 nM and Vmax 11.1 nmol X mg-1 X min-1. Both particulate enzymes were activated at 50 degrees C relative to 37 degrees C to the same extent: 1.37-fold. The activities of gamma-glutamyltranspeptidase were increased 1.8-fold in the livers of rats bearing DMBA-induced mammary adenocarcinomas relative to age-matched controls. Plasma levels of gamma-glutamyltranspeptidase were also increased 1.6-fold in tumor bearing rats. There was no observable sign of liver damage in tumor bearing rats; plasma glutamic pyruvic transaminase levels were normal in these animals. Blood glucose levels were elevated 17% in rats bearing DMBA-induced mammary adenocarcinomas compared to age-matched controls, although plasma insulin levels were the same in both groups: 35.4 +/- 3.5 microIU/ml for the former; 31.9 +/- 3.1 microIU/ml for the latter.
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PMID:gamma-Glutamyltranspeptidase in dimethylbenz[a]anthracene-induced mammary adenocarcinomas and in livers of tumor bearing rats. 288 76

A case of prostatic carcinoma with the cellular patterns of an adenocarcinoma and carcinoid tumor is reported. The tumor contained ultrastructural dense core neuroendocrine granules, and immunoperoxidase staining revealed prostatic acid phosphatase, prostatic-specific antigen, chromogranin, neuron-specific enolase, serotonin, adrenocorticotrophic hormone (ACTH), somatostatin, parathormone, calcitonin, bombesin, and glucagon but no insulin. The patient had exhibited hypercalcemia that may have been related to hormone production by the tumor. The literature on the endocrine aspect of the prostate and its tumor is reviewed.
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PMID:Prostatic carcinoma with endocrine features. A report of a neoplasm containing multiple immunoreactive hormonal substances. 289 Dec 93

[125I]Monoiodinated vasoactive intestinal peptide (125I-VIP) was cross-linked with human colonic adenocarcinoma cells (HT29 cells) grown as a monolayer using dithiobis(succinimidylpropionate) as cross-linking reagent. The cross-linked polypeptides were separated by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. A major polypeptide of Mr = 67 000 was characterized and it behaved like a high-affinity binding site for VIP according to the following data. The concentration of native VIP (0.5 nM) giving half-maximum inhibition of 125I-VIP covalent cross-linking with this polypeptide was very similar to that giving half-maximum displacement of 125I-VIP on HT 29 cells (0.6 nM). Glucagon or insulin was unable to inhibit the labelling of the Mr-67 000 component. In our experimental conditions neither specific 125I-VIP binding nor covalent labelling was observed with monolayers of Madin Darby canine kidney epithelial cells (MDCK cells) or African green monkey kidney fibroblasts (Vero cells) while the Mr-67 000 polypeptide was also characterized with human rectal adenocarcinoma cells (HRT 18 cells), known to possess the VIP receptor. Preincubation of HT 29 cells with native VIP at 37 degrees C, before 125I-VIP binding and subsequent cross-linking reaction, decreased the labelling of the Mr-67 000 polypeptide up to 80%. Assuming one molecule of 125I-VIP cross-linked per polypeptide, we have characterized, for the first time, a major polypeptide of Mr = 64 000, which belongs to the high-affinity VIP binding site of an intestinal human cell line.
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PMID:Covalent cross-linking of vasoactive intestinal peptide (VIP) to its receptor in intact colonic adenocarcinoma cells in culture (HT 29). 299 66

The transplantable hormone-responsive rat mammary adenocarcinoma 13762NF was dissociated with collagenase and hyaluronidase. Cells were cloned directly or lines were established from mass cultures and cells from these lines were cloned. Clones differed in cellular morphology, colony morphology on plastic or in collagen gel, growth rate, growth response to hormones, and hormone receptor levels. Growth response to prolactin, estradiol, progesterone, cortisol, and epidermal growth factor (EGF) was determined by culturing the cells within collagen gel and using a serum-free medium base of DME/F12 (1:1) with insulin, linoleic acid, and BSA. The clones varied in their hormone responses, with all 20 of the clones tested responding to cortisol in combination with EGF. Some clones would respond to EGF, cortisol, or progesterone when used alone. None of the clones tested could be stimulated by prolactin or estradiol. Receptor levels for estradiol, progesterone, glucocorticoids, and EGF were assessed in 3 selected clones differing in their hormone responsiveness. Receptor levels appeared to correlate with hormonal sensitivity. Selected clones transplanted into female F344 rats produced carcinomas with histopathologies similar to the original tumor.
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PMID:Heterogeneity in the hormonal responsiveness of clones derived from the 13762NF rat mammary tumor. 300 10

The effects of insulin on glucose transport and metabolism were examined in cultured HT29 human colonic adenocarcinoma cells. The presence of glucose transporters was verified by D-glucose displaceable [3H]cytochalasin B binding. The Kd and Bmax values from cytochalasin B binding studies were 190 +/- 30 nM and 8.4 +/- 1.4 pmol/mg protein, respectively. Glucose transport determined with 3-O-methylglucose showed saturable kinetics with a Km of 5.8 +/- 0.4 mM and a Vmax of 0.047 +/- 0.003 mumol/mg protein per min at 25 degrees C. Moreover, in HT29 cells, two classes of insulin binding sites were detected in radioligand binding experiments. Although insulin failed to stimulate glucose transport, it was found to activate glycolysis in HT29 cells. Glucose consumption increased from 0.33 +/- 0.03 mumol/mg protein per h to 0.49 +/- 0.05 mumol/mg protein per h and lactate production was augmented from 0.67 +/- 0.04 mumol/mg protein per h to 0.87 +/- 0.06 mumol/mg protein per h in response to 10(-7) to 10(-5) M insulin. Insulin also enhanced mannose metabolism. Apart from these two hexoses, HT29 cells exhibited a surprisingly narrow substrate specificity. With the possible exception of glyceraldehyde, little lactate was produced from alternative substrates, including adenosine, inosine, ribose, deoxyribose, dihydroxyacetone, galactose and fructose either with or without insulin. Despite its limited utilization by the glycolytic pathway, adenosine was readily salvaged for de novo synthesis of adenine nucleotides. These findings suggest that insulin directly influences substrate utilization through the glycolytic pathway in HT29 cells without activating the glucose transport pathway.
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PMID:Insulin regulation of glucose metabolism in HT29 colonic adenocarcinoma cells: activation of glycolysis without augmentation of glucose transport. 305 95

As described previously (I. Kijima-Suda et al., Cancer Res., 46: 858-862, 1986), a sialyltransferase inhibitor, 5-fluoro-2',3'-isopropylidene-5'-O-(4-N-acetyl-2,4-dideoxy-3,6,7,8-tetra -O- acetyl-1-methoxycarbonyl-D-glycero-alpha-D-galactooctapyranosyl)ur idine (KI-8110), inhibits pulmonary metastasis of murine colon adenocarcinoma 26 sublines of high (NL-17) and low (NL-44) metastatic potential. To investigate the mechanism of this inhibition, the effect of KI-8110 on the metastatic cascade, especially on the interaction between tumor cells and platelets which may play a crucial role in tumor cell metastasis, was examined. NL-17 cells induced irreversible platelet aggregation in heparinized human platelet-rich plasma in vitro. This activity was reduced by pretreatment of the tumor cells with KI-8110. Inhibition of aggregation was also induced by the treatment of tumor cells with neuraminidase or Limax flavus agglutinin, a lectin specific for sialic acid. Sialic acid, fucose, sialyllactose, and bovine submaxillary mucin inhibited this tumor cell-induced platelet aggregation, while galactose, mannose, lactose, alpha 1-acid glycoprotein, fetuin, and asialo-bovine submaxillary mucin did not. KI-8110 also inhibited platelet-derived growth factor-dependent growth of NL-17 cells, but showed no effect on insulin or epidermal growth factor-dependent growth of the tumor cells. Platelet-derived growth factor-induced phosphorylation of membrane protein was reduced by treatment of NL-17 cells with KI-8110. The same result was obtained in the neuraminidase-treated membrane fraction of NL-17 cells. These results suggest that KI-8110 inhibits experimental tumor cell metastasis by inhibiting the interaction between tumor cells and host platelets in at least two pathways, and this may be due to a reduction of sialic acid contents of the membrane surface of tumor cells.
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PMID:Possible mechanism of inhibition of experimental pulmonary metastasis of mouse colon adenocarcinoma 26 sublines by a sialic acid: nucleoside conjugate. 328 33

Insulin binding and receptor tyrosine kinase activity were investigated in the insulin-responsive R3230AC mammary adenocarcinoma. Insulin receptors, partially purified by wheat germ agglutinin-agarose chromatography, displayed electrophoretic properties similar to those of normal tissues and demonstrated autophosphorylation of the beta subunit. Tyrosine kinase activity of tumor preparations was measured by incorporation of 32P from ATP into the synthetic polypeptide substrate glutamic acid80:tyrosine20. The Km (app) for ATP, 15 to 30 microM in tumors from ovariectomized or intact rats, appeared to be increased by 10(-7) M insulin in vitro, with the calculated Vmax increased by 3- to 5-fold; the Km (app) for glutamic acid80:tyrosine20 was 2 to 3 microM and insulin increased the Vmax by 25 to 50%. The effects of diabetes and insulin treatment and of various doses of estradiol, progesterone, estradiol plus progesterone, or tamoxifen on insulin binding, basal tyrosine kinase activity, and insulin-inducible tyrosine kinase activity in vitro were studied in tumors from treated animals. Preparations from diabetic rats had elevated insulin binding and basal tyrosine kinase activity and displayed a striking dose-related increase in the ability for insulin induction of tyrosine kinase activity in vitro compared to intact animals; these effects of diabetes were prevented by administration of insulin. Over comparable doses, insulin growth factor 1 added in vitro induced tyrosine kinase activity minimally versus that seen for insulin. Treatment of rats with pharmacological doses of sex steroid hormones produced changes in insulin binding capacity and/or basal tyrosine kinase activity and, depending on dose, usually resulted in increased basal kinase activity relative to insulin binding. The insulin-inducible increase in tyrosine kinase activity in vitro was not altered by treatment with estradiol or estradiol plus progesterone in vivo, whereas high doses of progesterone attenuated the response. A consistent finding with increasing doses of sex steroids was an increase in the half-maximum dose or 50% maximum induction dose for insulin, implying reduced responsiveness. Tamoxifen administered to intact rats increased insulin binding and blunted the insulin-induced increase in tyrosine kinase in vitro; these effects were not seen in ovariectomized rats...
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PMID:Effects of diabetes and sex steroid hormones on insulin receptor tyrosine kinase activity in R3230AC mammary adenocarcinomas. 328 34

Animals given transplants of the MAC16 colon adenocarcinoma show a progressive decrease in carcass weight as the tumor size increases without a reduction in either fluid or caloric intake when compared with non-tumor-bearing controls. There is a decrease in both carcass fat and muscle mass which is directly proportional to the weight of the tumor. In male animals weight loss occurs when the tumor mass comprises more than 0.3% of the body weight and reaches 30% when the tumor represents 3% of the body weight. There is evidence for the production by the tumor of both lipolytic and proteolytic factors, which may be responsible for the cachexia, since two related mouse adenocarcinomas, which do not produce weight loss, have little lipolytic or proteolytic activity. The lipolytic factor is nondialyzable and is destroyed by both heat and acid. Both insulin and 3-hydroxybutyrate suppress the lipolytic activity of the tumor extract. The MAC16 tumor also contains a serine protease, the activity of which is also completely abolished by insulin and 3-hydroxybutyrate. Animals bearing the MAC16 tumor have an elevated plasma lipolytic and proteolytic activity when compared with non-tumor-bearing controls, suggesting a peripheral effect of the tumor products. The catabolic factors elaborated by the MAC16 adenocarcinoma may be responsible for the loss of both the fat and nonfat carcass mass, but they do respond to normal metabolic controls.
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PMID:Production of lipolytic and proteolytic factors by a murine tumor-producing cachexia in the host. 331 59

The euglycaemic glucose clamp technique has been used to assess insulin resistance in patients with colorectal adenocarcinoma. Ten cancer patients were studied and compared with control subjects matched for age, sex and nutritional status. Forty-one euglycaemic clamps were performed at one of five different insulin infusion rates (20, 30, 40, 100 or 200 milliunits min-1 m-2). Glucose disposal was significantly decreased in the cancer group at all insulin infusion rates, whilst attained insulin levels and metabolic clearance rates of insulin were comparable in the control and cancer groups. Analysis of dose-response data allowed assessment of sensitivity (insulin concentration of half maximal glucose disposal) and responsiveness (maximal glucose disposal). Responsiveness was significantly reduced in the cancer group (40.3 versus 71.5 mumol kg-1 min-1; P less than 0.001), whilst sensitivity was similar (93.7 milliunits l-1 in controls versus 90.8 milliunits l-1 in cancer patients), suggesting a postreceptor defect in insulin action in the cancer group.
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PMID:Insulin resistance in patients with colorectal cancer. 331 27


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