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)

We investigated the diagnostic role of creatine kinase isoenzyme BB (CK-BB) in lung cancer. CK-BB was assayed using a radioimmunological system by saturation with Mallinchrodt double antibody 125I labelled (RIA Quant-CPK-BB). Sensitivity was 97% and specificity 90% in 44 cancers (T2-T3), in 36 non-cancers (chronic bronchitis) and in 48 healthy controls. Mean serum CK-BB values for patients with chronic bronchitis (2.64 +/- 1.1 ng/ml) were virtually the same as in normal subjects. Patients with lung cancer had markedly higher serum CK-BB values (9.17 +/- 2.6 ng/ml) than either the control group (healthy subjects) or the chronic bronchitis patients (p less than 0.01). These results lead us to suggest that CK-BB serum determination might prove useful in screening pulmonary disorders. However, further studies are essential to establish: 1) the relationship between serum levels of the isoenzyme and the histology and stage of the neoplastic disease; 2) the relation between CK-BB and the aggressive potential of the neoplastic clone.
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PMID:Creatine kinase isoenzyme BB: a lung cancer associated marker. 324 44

Elevated creatine phosphokinase (CPK) MB isoenzyme has become accepted as a highly specific criterion for the diagnosis of myocardial infarction (MI). A patient with metastatic neuroendocrine carcinoma of the colon who had marked and persistent elevation of CPK-MB isoenzyme, in the absence of clinical and cardiographic evidence for MI, is described. The CPK-MB level was 25 percent (normal, less than 3 percent) on admission, 39 percent postoperatively, and 57 percent on discharge. A prompt decline in serum CPK-MB activity (11 percent, less than 3 percent) paralleled chemotherapy-induced tumor regression. Resurgence of the isoenzyme heralded recurrent disease. These findings suggest that CPK-MB may be a valuable adjunct marker in the diagnosis and monitoring of neuroendocrine carcinomas.
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PMID:Elevated creatine phosphokinase MB in a patient with neuroendocrine carcinoma of the colon--evidence for a tumor marker. Report of a case. 335 1

The in vivo exchange kinetics of creatine kinase in the hind leg muscle of rats containing a transplanted mammary adenocarcinoma has been investigated using 31P magnetic resonance spectroscopy. Using a solenoid coil, the adenosine triphosphate (ATP) resonances arising from the tumor could be distinguished from ATP resonances arising from the muscle surrounding the tumor by use of inversion spin transfer techniques. This procedure affords a specific method of evaluating ATP metabolism of tumors in vivo.
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PMID:In vivo determination of ATP in tumors using 31P inversion spin transfer. 336 72

BA-HAN-1C is a clonal rat rhabdomyosarcoma cell line composed of proliferating mononuclear cells, which partly fuse to terminally differentiated postmitotic myotube-like giant cells. The exposure to retinoic acid in vitro resulted in time- and dose-dependent changes of both cell differentiation and cell growth. The mononuclear cells revealed bundles of newly formed thick and thin myofilaments, never observed in untreated cultures, and exhibited signs of contact inhibition. In addition, there was a statistically significant increase (P less than 0.001) in the number of terminally differentiated postmitotic myotube-like giant cells and in the creatine kinase activity (P less than 0.05) which was used as a biochemical differentiation marker. At the same time cell growth was significantly inhibited (P less than 0.001) in vitro and a decrease in plating efficiency, as well as in saturation density, was observed. These data demonstrate that retinoic acid can suppress cell growth and simultaneously initiate differentiation in a malignant mesenchymal tumor cell line. However, despite the clonal nature of BA-HAN-1C, the complete status of terminal differentiation was not achieved by all tumor cells. The reason why not all tumor cells responded to retinoic acid is unknown at the present time and will have to be the subject of further studies.
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PMID:Terminal differentiation and growth inhibition of a rat rhabdomyosarcoma cell line (BA-HAN-1C) in vitro after exposure to retinoic acid. 340 49

Mitochondrial creatine kinase (CK-mit) is increased in cancer tissues of the digestive tract. There is no difference in molecular weight, electrophoretic and kinetic properties between the isoenzymes extracted from the tumor and those from the adjacent normal tissues. High non-CK-M/total CK activity ratios in some sera from cancer patients probably reflect leakage of CK-mit from the tumor tissues.
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PMID:Source of elevated serum mitochondrial creatine kinase activity in patients with malignancy. 342 77

The CK-BB isoenzyme is ubiquitous in neoplastic tissue, but with low activity. Accordingly, it might be a nonspecific and insensitive tumor marker. Evaluation of BB isoenzyme in serum might indicate the extent of diseases or the response to therapy. The presence of CK-MB in patients with cancers may cause confusion with AMI. Serial determinations of both CK and lactate dehydrogenase isoenzymes are of great help in differential diagnosis. The presence of mit-CK is a poor prognostic sign in patients with malignancy. The greatest clinical significance of CK-BB and macro-CK isoenzyme lies in their effect on various assays for CK-MB. Macro-CK types 1 and 2 are much more heat stable than are CK-MB and CK-BB, and so by heating samples for 20 min at 45 degrees C the presence of thermostable macro types can be demonstrated. Macro-CK type 2 has a much higher activation energy than macro-CK type 1. If macro-CK is present, determination of the activation energy easily differentiates between types 1 and 2. CK-Bi seems to be glycosylated protein, and it is thought that glycosylation may be a general way of enzyme inactivation. If inactivation inside the cell is postulated, it has to be shown that enzymes indeed pass into the cell compartments where glycosylating enzymes are located. Another possible mechanism is within the circulation. Whether malignant cells themselves produce Ck-Bi or if inactivation occurs in the blood is still unknown. In this connection, one finding is that in plasma of cancer patients, CK-Bi can be reactivated to CK-BB by mercaptoethanol to 95%, whereas in plasma of normal persons there is no reactivation of the much lower CK-Bi concentrations.
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PMID:Creatine kinase and its isoenzymes in neoplastic disease. 351 70

We used an enzyme-linked immunoabsorbent assay to measure creatine kinase (CK; EC 2.7.3.2) BB in the sera of 58 cancer patients. A pre-incubation step with an anti-CK-M antibody-coated bead removed M chain components, and CK-BB was quantified with use of an anti-CK-B antibody-coated tube. No cross reactivity was observed with mitochondrial CK or CK-MM; CK-MB cross reacted slightly (1.6%). Macro CK type 1 was measured as CK-BB. Average analytical recovery of purified CK-BB added to serum was 97.7%. Although the enzyme activity of CK-BB is labile, our studies show that this protein is antigenically stable for 12 months when stored frozen. The upper limit of normal for CK-BB concentration was 0.3 micrograms/L (95th percentile, n = 25). Of the 20 cases of breast cancer of various stages, none showed any increases of serum CK-BB. Only two of 18 patients with prostatic carcinoma (stage D), and two of 10 patients with oat-cell carcinoma of the lung had increased concentrations of CK-BB in the serum. Ten patients with squamous cell cancer of the lung had normal concentration of the enzyme. Thus the CK-BB isoenzyme is not frequently increased in cancers of the prostate, lung, and breast, and it has little apparent value as a tumor marker for these diseases.
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PMID:Reassessment of creatine kinase BB as a marker for cancer of the prostate, breast, and lung. 359 21

Three human rhabdomyosarcoma cell lines (Rh10, Rh18, and Rh28) have been established from three independently derived xenografts. These lines have been characterized as mesenchymal in origin (reactivity to desmin and vimentin antibodies) and as expressing a human fetal muscle surface antigen recognized by monoclonal antibody 5.1 H11. Measurable levels of creatine phosphokinase have been detected in the cell lines. Rh10 and Rh28 exhibit the same chromosomal translocation and express an atypical lactate dehydrogenase isoenzyme which may be homologous to those previously reported in other tumor types. The karyotype analysis has confirmed that each cell line was derived from its respective tumor and thus provides a unique model for future investigations.
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PMID:Characterization of cell lines derived from xenografts of childhood rhabdomyosarcoma. 360 78

We have examined the control of actin isoform synthesis by pituitary-derived fibroblast growth factor and serum in BC3H1 cells, a tumor-derived nonfusing muscle cell line. Under differentiating conditions in BC3H1 cells, the synthesis of beta- and gamma-actin ceases, and the rate of alpha-actin synthesis is increased concomitant with cessation of cell growth. Addition of fetal calf serum to differentiated cells reverses the process, whereas the addition of pituitary-derived fibroblast growth factor inhibits synthesis of alpha-actin but fails to induce the synthesis of beta- and gamma-actin. Analysis of RNA from differentiated BC3H1 cells after the addition of fetal calf serum indicated that the serum-induced increase in beta- and gamma-actin synthesis reflected an increase in their mRNA levels. In contrast, the repression of alpha-actin synthesis by fetal calf serum or fibroblast growth factor appears to reflect the translation efficiency of alpha-actin mRNA. Fibroblast growth factor is a competence factor for BC3H1 cells which allows them to progress from G0 4 h into the G1 phase of the cell cycle. In order to understand the nature of the intracellular signals responsible for the effect of fibroblast growth factor, we treated cells with vanadate, a known inhibitor of tyrosine-specific protein phosphatases. Vanadate fully mimics the action of fibroblast growth on actin synthesis and creatine phosphokinase synthesis and causes BC3H1 cells to exit the G0 portion of the cell cycle, as demonstrated by the induction of the c-fos proto-oncogene following addition of serum, vanadate, or bovine pituitary-derived fibroblast growth factor to these cells. We conclude that repression of alpha-actin synthesis and induction of the synthesis of beta- and gamma-actin are under independent control and that the induction of beta- and gamma-nonmuscle actin synthesis following serum addition is independent from movement into the cell cycle, and dependent on as yet unidentified serum components. The rate of synthesis of alpha-actin can be controlled by a defined mitogenic polypeptide fibroblast growth factor, which in short term experiments primarily affects the rate of translation of alpha-actin mRNA. The repression by fibroblast growth factor is most likely due to activation of a tyrosine specific protein kinase(s).
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PMID:Control of muscle differentiation in BC3H1 cells by fibroblast growth factor and vanadate. 364 14

A 72-yr-old man, having a lung tumor with metastatic spread to liver and bone, was hospitalized with a lactate dehydrogenase (LD; EC 1.1.1.27) activity and a creatine kinase (CK; EC 2.7.3.2) activity in serum of 30 and 2 times the upper reference limit (URL), respectively. The LD isoenzyme-1/LD activity ratio was 62% (2 times URL). This ratio was maintained throughout hospitalization, during which LD activity increased up to 90 times URL. Macro CK type 2 activity represented almost all of the CK activity, which increased up to 4 times URL during hospitalization. The patient died the 29th day after admission. The enzyme abnormalities were thought to stem from tumor tissue.
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PMID:Increased serum lactate dehydrogenase isoenzyme 1 and macro creatine kinase type 2 in a patient with lung cancer. 366 6


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