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)

Metabolism of antipyrine was studied in 12 patients with gastric carcinoma and 5 control subjects with peptic ulcer matched for sex, body weight, height, and smoking history. The mean antipyrine half-life was significantly longer (21.5 +/- 1.5 hr) in 3 patients with disseminated gastric carcinoma compared to control subjects (9.3 +/- 1.5 hr) (P less than 0.001). There was no significant difference in the mean antipyrine half-life between 9 patients with localized gastric carcinoma and control subjects. Similarily, the mean metabolic clearance rate of antipyrine was significantly lower (22.8 +/- 5.0 ml/hr/kg) in patients with disseminated gastric carcinoma compared to control subjects (52.6 +/- 13.4 ml/hr/kg) (P less than 0.02). Thus, the presence of gastric carcinoma in humans might alter antipyrine elimination. Significant negative correlation was observed between antipyrine half-life and albumin concentration (r = -0.786, P less than 0.01). These observations indicate that the decrease in antipyrine half-life is not primarily due to the presence of tumor but rather to the nutritional status of an individual.
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PMID:Microsomal enzymes in patients with gastric carcinoma as determined by plasma half-life of antipyrine. 75 Feb 70

Sprague-Dawley rats received in 10 mg/kg body weight (group I) or 30 mg/kg body weight (group II) ethylnitrosourea (ENU) orally on the 19th day of pregnancy. Their offspring were treated with Bacille Calmette-Guerin, human albumin, hydrocortisone, cyclophosphamide or nicotine starting on the 6th day of life. The ENU treatment significantly reduced the life expectancy of all offspring. Treatment of the offspring did not influence tumor frequency, induction time or localization of neurogenic malignant tumors. Cyclophosphamide treatment of group II offspring increased the number of females bearing mammary carcinomas.
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PMID:Influence of five different postnatal lifelong treatments on the transplacental carcinogenicity of ethylnitrosourea in Sprague-Dawley rats. 79 45

Research Institute of Endocrinology and Hormone Chemistry, Khar'kov It was shown that realization of a neoplastic process in the breast is determined, in particular, by the chemical structure of agents employed and their dosage. So 1-thyroxine, depending on the dosage used, may stimulate the development of tumor process in mammary glands, but exert no influence on it (an effect of "the effect extinction"), and finely suppress tumor development. Among the determining factors the activity of thyreotropic function of the hypophysis and a concentration of an albumin bound form of thyroxine in blood are of special importance.
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PMID:[The influence of thyroid and antithyroid preparations on the development of induced breast cancer]. 82 75

Indirect immunofluorescence studies on sections of human normal breast tissue, benign breast lesions, and breast adenocarcinomas were performed with the use of monospecific fluorescein-conjugated antisera to human alpha, gamma, and mu chains, albumin, and C3. In all tissues, benign and malignant, immunohistologic localization of IgA and IgM was noted in patterns previously described for other secretory epithelia. IgG was localized at the tumor cell, but was not associated with epithelial cells from either normal breast tissue or benign breast lesions. Except for a single case of benign cystosarcoma phylloides, all normal, benign, and malignant breast tissues failed to react with anti-C3. These findings were compared with previous studies employing dissociated tumor cells, and the potential application of these methods to pathologic diagnosis was examined.
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PMID:Immunofluorescence studies of benign and malignant human mammary tissue. 82 47

Two-dimensional immunoelectrophoresis was used to evaluate 8 cervical cancer speciments, 11 other gynecologic tumors, and 5 specimens of normal cervix. Antigens were water-soluble tissue extracts and antisera prepared in rabbits. When tested against antisera to cervical cancer, cancer antigens showed 14-17 precipitin lines whereas normal cervix showed 10-16. A single heavy heterogeneous precipitin line with an electrophoretic mobility of 0.58 relative to bovine albumin was observed in all cervical cancer specimens but not in normal cervical or other tumor specimens. Further evidence for the uniqueness of this antigen was sought by enhancement (addition of another antigen to the first phase of electrophoresis which increased the size of common peaks) and suppression (addition of another antiserum to the second phase, whereby the peak size of components to which both sera have antibody was decreased). The specific precipitin line was neither suppressed by the addition of antisera to normal tissue nor enhanced when normal tissue antigen was added to the tumor antigen preparation. More conclusively, adsorption of the tumor antiserum with normal tissue had no effect on the unique tumor-associated precipitin line, whereas all other precipitin lines were removed. This antigen was common to other cervical tumors because enhancement was demonstrated with three other cervical tumor specimens. The identification of a distinct and separate antigen associated with cervical carcinoma will permit further characterization and possible development of immunodiagnostic methods.
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PMID:Identification of a tumor-associated antigen in cervical carcinoma by two dimensional (crossed) immunoelectrophoresis. 83 63

Experimental evidence is presented that supports the use of the cold agar-gel electrophoretic method for the clinical quantitation of specific estrogen-binding protein present in some human mammary carcinomas. It is necessary to dilute tumor extracts to avoid interference by serum-borne, non-relevant hormone-binding proteins such as albumin, which migrates to the same anodal region as does the binding protein. Dilution to 2.5 mg or less of total protein per milliliter circumvents such interference while still permitting reliable quantitation of the binding protein. Seventy-two mammary carcinomas were compared for binding-protein content by both the cold agar-gel electrophoresis and a single-point dextran-coated charcoal assay. The correlation coefficient (0.96) indicated excellent agreement between results by the two methods. In addition results are presented which indicate that the preparation of tumor extracts for electrophoresis does not require the use of an ultracentrifuge.
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PMID:Electrophoretic assay of specific estrogen receptors: a contribution to methodology. 91 71

Decreased serum albumin levels are commonly observed in patients with carcinoid tumor, who also show several characteristic clinical and biochemical abnormalities. A large comparative study on a group of 96 carcinoid patients was performed with the purpose of identifying some of the mechanisms leading to hypoalbuminemia in patients with this form of cancer, and thereby to shed light on the cause of hypoalbuminemia of cancer in general. Serum albumin values were compared with a number of clinical parameters (including extent of liver metastases, severity of diarrhea, degree of right heart failure, and extent of gastrointestinal surgery) and of laboratory data (prothrombin time, BSP retention, serum transferrin concentration, hematocrit value, and daily urine excretion of 5-hydroxy-indoleacetic acid). In several patients the gastrointestinal protein loss was assessed by the 51Cr-albumin technique, whereas albumin renewal and distribution were evaluated by the use of 125I-albumin. The data obtained showed that the main factors in determining decreased serum albumin levels in patients with carcinoids are both reduced synthesis and increased loss of the protein. The hepatic synthetic defect appears to be related to a progressive decrease in the number of functioning liver cells; the origin of the gastrointestinal protein loss may be related to the obvious tumor involvement of the gut wall, as well as to the pharmacologically-induced diarrhea. Right heart failure occurring as a result of the carcinoid heart disease may be an additional cause for gastrointestinal protein loss in patients with carcinoid tumor.
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PMID:Pathophysiology of hypoalbuminemia associated with carcinoid tumor. 97 3

Tyrosyl-, histidyl-, lysyl-, and phenylalanyl-tRNA's from 3 tumors (DBAH, DBAH, and DBA), differing in growth rates and from host mammary glands and liver, were compared by means of methylated albumin kieselguhr (MAK) column and by reverse-phase-5 chromatography. The elution profiles of lysyl-tRNA's from DBAH and DBA, phenylalanyl Trna's from DBAH and DBAH, and histidyl-tRNA's from DBA3 tumors exhibited extra isoaccepting species, compared with host liver and mammary glands. The distribution of acylatable tyrosyl-tRNA's in DBA3 and DBAH, phenylalanyl-tRNA's in DBAH and DBAH2, and histid-l-tRNA's in DBA3 is higher than that in liver, whereas no appreciable differences were observed in the lysyl-tRNA contents of the tumors and liver. The chromatographic alternations appeared to be a property of the tumor tRNA's and not due to differences in aminoacyl-tRNA synthetases or due to the aggregation of tRNA's. The structural and functional significance of these findings are discussed.
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PMID:Transfer RNA species in tumors of different growth rates. 97 94

Localization of a radiopharmaceutical agent in a "tumor" is best conceptualized in terms of the altered regional physiology attendant to the presence of the "tumor". Such localization should be expected to occur in association with other disease states characterized by similar altered regional physiology. Neoplasms, areas of inflammation, and certain phases of infarct development are characterized by increased permeability of their capillary beds to macromolecules. This is largely due to neovascularization and the large intercapillary pores associated with new growth of capillary beds in these circumstances. Often, total perfusion to such lesions is increased in comparison to surrounding normal tissue. Thus, in all three clinical conditions, the entry of macro-molecules into the interstitial fluid space from the intravascular space is increased above that seen in normal tissue. Moreover, with neoplasms and inflammatory processes, there may be a delay in new lymphatic vessel growth adding to the residence time of the macromolecules in the interstitial fluid space. In all three conditions, the increased macrophage activity associated with tissue necrosis may result in ingestion of the labeled macromolecule by the macrophage. Pinocytosis may result in ingestion of the labeled macromolecule by other cells in the lesion, or there may be specific receptor sites on the cell membrane for the macromolecule, which may lead to fixation of the labeled macromolecule on the cell surface and possible intracellular translocation of the label itself. Radiolabeled macromolecules such as albumin, fibrinogen, or gamma globulins, and radionuclides that bind to macromolecules such as radiogallium, radioindium, and other radioelements, exhibit localizing behavior in tumors, inflammatory lesions, and during certain stages of infarcts. In the case of radiogallium and radioindium, the binding macromolecule is transferrin, and it is known that some cells have specific receptor sites for transferrin-bound iron on the cell membrane. It is possible that certain cells within these lesions have cell membrane receptor sites for radiogallium- and radioindium-labeled transferrin, and the cell erroneously accepts these radioelements from the transferrin in lieu of iron in attempting to engage in heme enzyme synthesis. Another mechanism that may be operative in the localization of agents in neoplasms, infarcts, and inflammatory lesions may be the altered cell permeability found in many cells of such lesions. It is known that many agents, such as supravital dyes, are excluded from entering normal cells by the selective permeability of normal cell membranes. When cell membrane permeability is altered, such as can be seen in traumatized, dying, or dead cells, the normally excluded agent may penetrate the abnormal cell membrane and bind, and consequently accumulate in intracellular constituents.
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PMID:Mechanisms for localization of radiopharmaceuticals in neoplasms. 98 76

Rates of incorporation of thymidine and uridine, but not leucine, decrease markedly in L1210 (V) cells within 1 hour of incubation in DULBECCO'S medium containing 10% serum. 2-Mercaptoethanol (2-ME) after a latent period of more than 5 hours causes an increase in nucleotide incorporation. Bovine serum albumin can substitute for serum in the medium, but a higher concentration of 2-ME is required for growth. After charcoal treatment of the albumin less 2-ME is required. These experiments suggest that inhibition of the tumor cells is caused by a serum factor whose effect is antagonized by the thiol.
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PMID:Studies of the mechanism of growth promotion of lymphoma cells by 2-mercaptoethanol in vitro. 105 63


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