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)

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

Rats with 9L brain tumors received intraperitoneal injections of iododeoxyuridine (IUdR) and bromodeoxyuridine (BUdR) to estimate the duration of the deoxyribonucleic acid (DNA) synthesis phase (Ts) and the potential doubling time (Tp) of individual tumors. Different sequences and intervals (2 or 3 hours) of IUdR and BUdR administration were evaluated. After denaturation, tumor sections were reacted with Br-3, a monoclonal antibody that identifies only BUdR, and then were stained immunohistochemically by the avidinbiotin complex method. An antibody that recognizes both IUdR and BUdR, IU-4, was applied to the sections and identified by the alkaline phosphatase-antialkaline phosphatase method. Nuclei labeled only with IUdR stained blue, while those labeled with BUdR or with BUdR and IUdR stained brown. The fraction of cells that either left or entered the S-phase during the time between administration of IUdR and BUdR was measured to calculate Ts and Tp, assuming that the labeled cohort completed the DNA synthesis at a constant rate. The Ts was 8.8 hours (coefficient of variation (cv) = 0.05) and the Tp was 64.2 hours (cv = 0.08). The sequence and interval of administration of IUdR and BUdR had a minimal effect on Ts and Tp. In studies of 9L cells in monolayer culture, the Ts was 9.6 hours (cv = 0.08) and the TP was 30.6 hours (cv = 0.06). Double labeling with BUdR and IUdR allows the duration of the S-phase and potential doubling time of individual brain tumors to be estimated in situ from a single biopsy specimen.
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PMID:Cell kinetics of rat 9L brain tumors determined by double labeling with iodo- and bromodeoxyuridine. 236 82

Using radioimmunoassay methods the authors assayed the concentration of biochemical neoplasm markers (BMN) in 106 patients with neurological diseases (M-56, F-50) in the serum, and in 20 cases in the cerebrospinal fluid. In certain cases these markers were present, and sometimes their concentration was raised: ferritin in multiple sclerosis from 200 to 1365 ng/ml, in ischaemic stroke up to 327.9 ng/ml, in Parkinson's disease up to 423 ng/ml in the serum. In some cases of other diseases the levels of carcinoembryonic antigen (CEA), acid prostatic phosphatase (PAP) and alpha-fetoprotein (AFP) were raised, similarly as that of human chorionic gonadotropin (HCG). Further studies are being conducted on BMN, including also other markers (CA 125, CA 199), with monoclonal antibodies, beta-endorphins and prostaglandins in neurological diseases, including multiple sclerosis. It is suggested (Nowak) that BMN may have an indirect role in the aetiology and pathogenesis of certain diseases of the nervous system and that they may have connections with prostaglandins.
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PMID:[Biochemical neoplasm markers in selected neurological diseases]. 243 40

Phosphorylation of pp60c-src at Tyr-527, six residues from the carboxy terminus, has been implicated in regulation of the protein-tyrosine kinase activity of pp60c-src. Here we show that dephosphorylation of pp60c-src by phosphatase treatment in vitro caused a 10- to 20-fold increase in pp60c-src protein-tyrosine kinase activity. Binding of specific antibody to the region of pp60c-src which contains phosphotyrosine-527 also increased kinase activity. Each treatment increased phosphorylation of added substrates and of Tyr-416 within pp60c-src by a similar mechanism that involved altered interactions with ATP and increased catalytic rate. We suggest that the phosphorylated carboxy terminus acts as an inhibitor of the protein kinase domain of pp60c-src, unless its conformation is altered by either dephosphorylation or antibody binding. The antibody additionally stimulated the phosphorylation of forms of pp60c-src that had reduced gel mobility, much like those phosphorylated in kinase reactions containing pp60c-src activated by polyomavirus medium tumor antigen. These in vitro experiments provide models for the activation of pp60c-src in cells transformed by polyomavirus. We also show that autophosphorylation of pp60c-src at Tyr-527 occurs only to a very limited extent in vitro, even when Tyr-527 is made available for phosphorylation by treatment with phosphatase. This suggests that other protein-tyrosine kinases may normally phosphorylate Tyr-527 and regulate pp60c-src in the cell.
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PMID:Dephosphorylation or antibody binding to the carboxy terminus stimulates pp60c-src. 243 3

To recognize progression of an inoperable prostatic cancer we use clinical parameters and the prostate specific phosphatase. The prostate specific antigen (PSA) is a new, sensitive and specific laboratory tumor marker. With 363 specimens of patients without prostatic cancer we defined for the normal range of this serum parameter. In 98 men with histologically proven prostatic cancers we investigated for the clinical relevancy of the serum level of PSA. We believe, that measurement of serum PSA give important information for clinical management of prostatic cancer.
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PMID:[Clinical relevance of radioimmunologic determination of prostate specific antigen in prostate cancer]. 244 Jan 70

We have compared the level of phosphotyrosyl phosphatase activity in lysates from normal human colon mucosal cells and human colon carcinoma cells and analyzed the effect of incubating these cells with sodium orthovanadate, an inhibitor of phosphotyrosyl phosphatase activity, on the relative abundance of acid-stable phosphotyrosine and on in vitro protein kinase activity of pp60c-src. Additionally, we compared the effect of lysing these cells in buffer containing only nonionic detergents with RIPA buffer, which contains both sodium dodecyl sulfate and deoxycholate, on the in vitro kinase activity of pp60c-src. Our results show that the level of detectable phosphotyrosyl phosphatase activity in lysates derived from normal colon cells and colon carcinoma cells is very similar. Additionally, the abundance of acid-stable phosphotyrosine in these cells cultured in the absence or presence of vanadate is not significantly different. However, incubation of these cells with vanadate significantly stimulates the activity of pp60c-src derived from the normal colon cells in immune-complex kinase assays, while having no detectable effect on the activity of pp60c-src from the colon tumor cells. The in vitro protein kinase activity of pp60c-src derived from RIPA buffer lysates of colon carcinoma cells was found to be elevated five- to sevenfold when compared with pp60c-src from these same cells lysed in buffer containing only Nonidet-P 40 as a detergent. The type of lysis buffer did not effect the activity of pp60c-src from normal colon mucosal cells. These results provide additional evidence that the activity of pp60c-src may be regulated differently in colon carcinoma and normal colon mucosal cells.
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PMID:Analysis of pp60c-src tyrosine kinase activity and phosphotyrosyl phosphatase activity in human colon carcinoma and normal human colon mucosal cells. 244 18

The authors have used a sensitive alkaline phosphatase-anti-alkaline-phosphatase immunohistochemical method to examine 28 human pulmonary carcinomas for the presence of renin. Immunoreactive renin was found in 23 (82%) cases. Specific staining was always associated with small vessels in the stroma of the tumor or in adjacent areas of inflamed fibrous tissue. Within vessels, renin was localized in the cytoplasm of medial cells. Adenocarcinoma exhibited the most consistent staining (11/12 cases), and this appeared to be independent of the degree of tumor differentiation. Immunoreactive renin was also detected in squamous cell (7/8 cases), undifferentiated large cell (4/4 cases), and small cell undifferentiated carcinoma (1/1 cases), but the number of vessels and intensity of staining were usually less than seen in adenocarcinoma. Staining was not found in the bronchioloalveolar variant of adenocarcinoma (0/3 cases). By means of immunoaffinity chromatography with monoclonal antibodies (MAbs) raised to kidney renin, both active and inactive renin were extracted from homogenates of surgical specimens. The molecular weight of both forms of renin was approximately 59,000 daltons.
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PMID:Renin in blood vessels in human pulmonary tumors. An immunohistochemical and biochemical study. 245 Apr 64

An immunochemical study of normal prostatic tissue, adenoma and cancer identified the following five antigens: alpha 2-ferroprotein, tissue gamma-esterase, lactoferrin, acidic phosphatase and prostatic beta-globulin. The two latter proteins proved organo-specific prostatic antigens. Levels of all the proteins were measured in normal, adenoma and cancer tissues. A sharp drop in the concentration of organospecific proteins was observed in tumor tissue. The study established a relationship between the level of organospecific proteins and cell differentiation of cancer, which was particularly pronounced for beta-globulin.
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PMID:[The nature of the antigenic restructuring of tumors of the human prostate]. 246 Sep 99

In this study fresh frozen tissue samples of benign osseous tumors (five non-osteogenic fibromas, one fibrous dysplasia, one chondromyxoidfibroma), tumors of uncertain biological behaviour (eight cases of histiocytosis X, two giant-cell tumors), and of malignant intraosseous tumors (two malignant fibrous histiocytomas, two malignant histiocytosis, four osteosarcomas, one chondrosarcoma and two Ewing sarcomas) were studied with a panel of monoclonal antibodies reactive with monocyte/macrophages and various types of dendritic cells. In addition, tumors were further defined with a broad spectrum of antibodies against filamentous proteins and lymphocyte differentiation antigens. The specimens were stained with a triple-layer immunoalkaline phosphatase protocol. Tumors stained with these antibodies could be roughly divided into two groups. The first group comprised tumors with one predominant cell population reactive with one particular monoclonal antibody. In this group, cases of histiocytosis X were found to be consistently labelled with CD-1 antibodies. The giant-cell tumors showed a very homogeneous staining with certain monocyte/macrophage antibodies (Ki-M8). Nevertheless, even in these tumors, heterogeneity was demonstrated by the occurrence of cells with monocytic differentiation in histiocytosis X and conversely by the occurrence of cells with differentiation antigens of the dendritic cell system in giant-cell tumors. An exception has to be made for the two cases of malignant histiocytosis examined. These tumors were selectively labelled with antibodies against monocyte/macrophages (Ki-M8, IOM-1). The second group comprised tumors showing a high degree of heterogeneity demonstrated by the varying amounts of tumor cells reacting with the applied markers of the monocyte/macrophage and dendritic cell systems. In most cases it was difficult to ascribe labelled cells to the tumor cell population as opposed to an "innocent bystander" inflammatory cell population. This distinction was especially difficult in malignant fibrous histiocytomas underlining the current concept that these tumors are of primitive mesenchymal rather than true histiocytic origin.
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PMID:Histiocytic differentiation in benign and malignant bone tumors. 246 63

The authors have used two immunoalkaline phosphatase methods to study nonhematopoietic tumor tissues of four patients, one each with alveolar cell carcinoma of the lung, renal cell carcinoma, gastric adenocarcinoma, and colon carcinoma. They found, regardless of specific antibodies used, definite enzyme activity in the tumor cells of these four patients. Although it was possible to determine that the tumor cells were epithelial in origin because of their intense staining with antibodies to epithelial cell antigens, control slides labeled with nonimmune mouse ascites also contained cells with definite enzyme activity. In two of these cases, unlabeled smears were stained for alkaline phosphatase and showed that the tumor cells contained endogenous levamisole-resistant enzyme activity. This endogenous enzyme activity is not demonstrable in either the benign cells of these cases or the benign or malignant cells of other control cases. The findings suggest that the immunoalkaline phosphatase methods also have their inherent endogenous enzymic problems. They also suggest that cytochemical demonstration of levamisole-resistant alkaline phosphatase may be a useful cell marker for the identification of tumor cells in serous effusions.
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PMID:Diagnostic significance of levamisole-resistant alkaline phosphatase in cytochemistry and immunocytochemistry. 246 83


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