Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Sections of hypernephroid carcinoma from 20 cases were investigated for aldolase isozymes A and B by a mixed aggregation immuno-cytochemical technique, and for the brush border membrane enzymes aminopeptidase and alkaline phosphatase by conventional histochemical techniques. It was found that the cases could be grouped into four types: type 1 (1 case) contained all 4 enzymes; type 2 (7 cases) contained all enzymes except aldolase-B; type 3 (7 cases) possessed aldolase-A and one brush border membrane enzyme; type 4 (5 cases) contained only aldolase-A. The aldolase-A concentration in all tumor cells was higher than that in proximal tubule cells, whereas the concentration of the two brush border enzymes was lower. In cases tydolase-B and/or higher amounts of the brush border enzymes than the surrounding cells. No correlation was observed between clear cell and granular cell hypernephroid carcinomas or the invasiveness or the nuclear polymorphism of the tumors on the one hand with their enzyme type on the other. These histological enzyme analyses suggest that most, if not all, hypernephroid carcinomas are derived from kidney proximal tubule cells and that the tumor cells then progressively lose aldolase-B, and subsequently the brush border enzymes, but at the same time producing more aldolase-A. The presence of the enzyme-rich patches suggest different patterns of proliferation and differentiation among the tumor cell population. Three tumors other than hypernephroid carcinoma were also examined in this way. The results suggest that histoenzymological analyses are of general applicability in studies of tumor progression. They should also be useful for biopsy and aspiration cytology.
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PMID:A classification of tumor development based on an analysis of enzymes in tissue sections of hypernephroid carcinoma in man. 101 98

To assess changes in aldolase isozyme patterns (A, B, and C) in renal cell carcinoma (RCC) tissues and to evaluate whether serum aldolase A might be a useful marker for RCC, quantitative analysis by enzyme immunoassay and immunohistochemical localization were performed. Concentrations of aldolase A in RCC (7300 +/- 6300 ng./mg. protein n = 26) were significantly higher than those of normal cortex (720 +/- 410 ng./mg. protein, n = 14, p less than 0.01); concentrations of aldolase C in RCC (48.0 +/- 8.0 ng./mg. protein) were also significantly higher than those of normal cortex (8.7 +/- 4.7 ng./mg. protein, p less than 0.01). On the other hand, concentrations of aldolase B in normal cortex were 18,100 +/- 10,100 ng./mg. protein (n = 14), whereas the values in RCC were only 130 +/- 270 ng./mg. protein, a significant lowering (p less than 0.01). Immunohistochemically, aldolases A and C were found localized in all RCC tissues (n = 10); aldolase B was faintly stained in only a few tumor cells of two cases (20%). Levels of serum aldolase A were elevated (greater than 300 ng./ml.) in 30 (75%) of 40 patients with RCC as compared to three (6.3%) of 48 individuals with urogenital benign diseases and in seven (21%) of 34 cases with non-RCC urogenital malignancies. Since it is generally accepted that RCC are derived from renal proximal tubules, these findings indicate that aldolase B, the predominant isozyme in the normal case, changes into aldolases A and C during carcinogenesis and that serum aldolase A could be a new useful biomarker for RCC.
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PMID:An immunochemical and immunohistochemical study of aldolase isozymes in renal cell carcinoma. 185 54

Didemnin B (NSC 325319), a cyclic depsipeptide isolated from a Carribean sea tunicate, exhibited potent antitumor activity in preclinical studies. After determining the maximum tolerated dose in our previous phase I/II trial, we conducted a phase II study of this drug in patients with previously treated small cell lung cancer; the starting dose was 6.3 mg/m2 intravenously over 30 min every 28 days. The major side effects were in the neuromuscular system and included severe muscle weakness, myopathy and/or myotonia by electromyography, and elevation of creatine phosphokinase and aldolase levels. We also observed modest increases in bilirubin and alkaline phosphatase levels. There were minimal hematologic toxic effects. No response was observed among 15 evaluable patients, leading us to conclude that didemnin B was toxic but inactive in patients with previously treated small cell lung cancer at the stated dose and schedule. A review of the literature revealed no significant antitumor activity in cancers of the colon, breast, ovaries, cervix, or lung (non-small cell) or in renal cell carcinoma. Further clinical trials for didemnin B may not be warranted at the stated dose and schedule.
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PMID:Phase II clinical trial of didemnin B in previously treated small cell lung cancer. 789 44

New markers/targets for renal cell carcinoma (RCC) are needed to enable earlier detection and monitoring of disease and therapeutic targeting. To identify such molecules, normal and RCC-derived primary cell lines have been used as a simplified model system for studying changes that accompany tumorigenesis. Short-term cultures allow enrichment of relevant cell types from tissue samples, which is balanced against the potential for in vitro changes. Examination of 3 proteins with altered expression in RCC tissue showed the maintenance of normal-tumour differences in culture, although some changes were apparent, including alteration in the isoform of aldolase. Comparative analysis of primary cell lines by 2-DE found 43 proteins up-regulated and 29 down-regulated in at least three out of five tumour cell lines. Many of the observed changes have been previously reported in RCC, including up-regulation of several glycolytic enzymes, vimentin and heat shock protein 27, validating the approach. Additionally, several novel changes in protein expression were found, including up-regulation of several proteins involved in actin cytoskeleton organisation such as radixin and moesin, two members of the septin family, and the actin bundling protein, fascin. Validation studies using Western blotting and immunohistochemistry indicate that several of these molecules may be useful as markers for RCC.
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PMID:Proteomic analysis of primary cell lines identifies protein changes present in renal cell carcinoma. 1659 13