Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

Three aldolase isoenzymes; aldolase A, B and C were found in various human tissues including gastric mucosa, by means of substrate specificities (the fuctose-1, 6-diphosphate aldolase/fructose-1-phosphate aldolase activity ratio) and electrophoresis. The basic pattern of aldolase isoenzyme in man consisted of nine active bands, which were designated as I, II, III, IV, V, VI, VII, VIII and IX band from anode side respectively. The I band corresponded to aldolase C, V to aldolase A and IX to aldolase B. The II, III and IV band are hybrid molecules composed of subunit of aldolase A and C, and the VI, VII and VIII of subunit of aldolase A and B. The V band was present in all tissues, while IX was detected in the liver, kidney and stomach. The I, II, III and IV band were found in all tissues except for muscle. These findings were extremely different from those in other species. In normal gastric mucosa, active bands were composed of I, II, III, IV, V, VIII and IX band, while in gastric cancerous tissue, I, II, III, VIII and IX band were absent or markedly decreased in activity. In contrast, the V band increased. In fetal gastric mucosa, they showed the same pattern as cancerous. In extract of cancerous tissues, the FDP/F1P activity ratio was 20.5+/-2.2, as compared with 7.2+/-0.1 in normal gastric mucosa. In serum of patients with gastric cancer, the FDP/F1P activity ratio was 9.7+/-1.2, while it was 2.9+/-0.4 in normal human serum. These results suggest that the elevation in serum of the FDP/F1P ratio in gastric cancer is due to increase in muscle type isoenzyme (aldolase A) which is derived from cancerous tissue. Furthermore, the analysis of serum aldolase isoenzyme will save for cancer diagnosis.
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PMID:[The distribution of the aldolase isoenzymes in various human tissues and the anomaly in cancerous tissues -especially in gastric cancer- (author's transl)]. 124 Aug 53

We investigated three aldolase isozymes (aldolase A, B, and C) in human lung cancer by using an indirect peroxidase labeled antibody method. We used 27 tissue samples obtained at surgical operations which were fixed in periodate-lysine-4% paraformaldehyde (PLP) solution, and embedded in optimum cutting temperature (OCT) compound. They were 11 adenocarcinomas, 9 squamous cell carcinomas, 3 large cell carcinomas, 3 small cell carcinomas, and 1 adenosquamous carcinoma. Aldolase A and C expressed intensely positive stainings in the cytoplasm of cancer cells compared with normal lung tissues, and its positivities were 81% respectively. However, Aldolase B showed almost negative staining, and its positivities were only 41%. These rates had no relation to the histological types or pathological stages of lung cancers, and suggested that human lung cancer contained increased levels of aldolase A, and C.
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PMID:[An immunohistochemical study on three aldolase isozymes in human lung cancer]. 131 19

Two mechanistically distinct forms of fructose-bisphosphate aldolase are known to exist. It has been assumed that the Class II (metallo) aldolases are evolutionary more primitive than their Class I (Schiff-base) analogs since the latter had only been found in eukaryotes. With the identification of prokaryotic Class I aldolases, we present here an alternative scheme of aldolase evolution. This scheme proposes that both aldolase classes are evolutionarily ancient and rationalizes the observed highly variable expression of both enzyme types in contemporary file forms.
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PMID:Fructose-bisphosphate aldolases: an evolutionary history. 141 94

In this report we demonstrate the novel finding that aldolase A interacts with DNA sequences in mouse SEWA sarcoma cells. This interaction was initially observed through the identification of a 40 kDa protein which was eluted from a DNA affinity chromatography column consisting of the long terminal repeat (LTR) of the endogenous intracisternal A-type particle (IAP). Microsequencing analysis identified this 40 kDa protein as the glycolytic enzyme, aldolase A. The use of specific anti-aldolase antibodies enabled the identification and subsequent purification of aldolase from the nuclear protein fraction of two SEWA sublines, one that is adherent and one that grows in suspension. In order to confirm our initial finding that aldolase is capable of interacting with DNA, proteins from each subline were immunopurified with anti-aldolase antibodies, eluted and then tested for their ability to interact with IAP-LTR DNA sequences. Interestingly, only aldolase derived from the anchorage dependent SEWA cells was capable of interacting with the IAP-LTR, however, several cell lines derived from human tumors also exhibited this activity. Subsequent studies revealed the ability of aldolase to interact with some but not every DNA sequence tested, implying that there may be a minimal DNA conformation and/or sequence requirement for this activity. The presence of aldolase A in the nuclei and its ability to interact with certain DNA sequences suggest a novel role for this metabolic enzyme.
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PMID:Aldolase-DNA interactions in a SEWA cell system. 154 45

The pattern of gene expression in fetal hepatocytes transformed in culture with a hepatocarcinogen (FRL cells) is studied with respect to a range of markers which are either developmentally regulated and/or shown to be expressed at high levels in hepatoma cells. The relative abundance of the respective mRNAs is determined and immunocytochemistry is used to detect the respective proteins in cultured cells. When compared with its normal counterpart, FRL cells retain the expression of transferrin, alpha 1-acid glycoprotein, gamma-glutamyltranspeptidase, and tyrosine aminotransferase at near normal levels, while expression of the liver-specific isoenzymes of pyruvate kinase (L form) and aldolase (B form) is reduced. The cell lines are different in that they fail to express albumin, alpha-fetoprotein, thiostatin and alpha 2-macroglobulin, and they express high levels of M2-pyruvate kinase and aldolase A, markers often found in abundance in hepatoma cells. Therefore transformation has resulted in different effects on different genes. Furthermore, it is of interest to find that the cells coexpress both forms of the pyruvate kinase isoenzymes which does not occur in the normal developing hepatocyte. These results indicate that it is possible to use this model to study changes which accompany transformation of fetal rat hepatocytes. The resulting cell lines have a stable phenotype and retain the changes which result from transformation even after extended passaging. This facilitates comparisons between the precursor cell and the tumor cell, both of which can be maintained under controlled conditions which exist in culture.
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PMID:Gene expression in clonally derived cell lines produced by in vitro transformation of rat fetal hepatocytes: isolation of cell lines which retain liver-specific markers. 170 49

Three monoclonal antibodies (MAbs1A2, 3C5, and 4C2) for human aldolase A [EC 4.1.2.13] were established. MAbs1A2, 3C5, and 4C2 were shown to belong to subclasses IgM, IgG1, and IgG2a, respectively. None of the MAbs inhibits aldolase A activity. Their epitopes were mapped in detail on the molecule by examining the reactivities of the MAbs to chimeric proteins between aldolases A and B [Kitajima et al. (1990) J. Biol. Chem. 265, 17493-17498] in ELISA and to the CNBr-cleaved fragments of aldolase A in immuno-blotting. MAbs1A2 and 3C5 reacted with sites located within amino acid residues 306-363 at the C-terminal region of the enzyme. MAb4C2 recognized an epitope of the enzyme present within amino acid residues 34-108 at the N-terminal region. In a competitive binding assay, MAbs1A2 and 3C5 competed with each other for binding to the antigen and also interfered with the binding of MAb4C2, whereas MAb4C2 failed to inhibit the binding of MAbs1A2 and 3C5 to the antigen. MAb3C5 showed a species-specificity in the reaction with the antigen; it reacted with human and rabbit aldolase A with similar reactivity but not at all with the rat and mouse enzymes, which differ from the human and rabbit enzymes in two amino acid residues at positions 328 and 348. Reactivities of MAbs to aldolase A were further examined with engineered enzymes containing an amino acid substitution.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Monoclonal antibodies recognizing amino-terminal and carboxy-terminal regions of human aldolase A: probes to detect conformational changes of the enzyme. 171 40

The aldolase isozyme family is composed of three members, A, B, and C, which are encoded by separate genes. The proteins are expressed in a tissue-restricted manner during development and in the adult. To elucidate the regulation of aldolase mRNA in the mouse liver, we analyzed its expression by a number of methods including Northern blot, RNA dot blot, and nuclear run-on assays. Our experiments demonstrate that the expression of aldolase A in the liver is primarily regulated by post-transcriptional control. In contrast, we found that changes in the level of aldolase B mRNA are due to changes in the rate of initiation of transcription. In addition, we examined the regulation of aldolase expression in the adult kidney. We found that although the kidney has eight times more aldolase B than the liver, the rate of initiation of transcription is similar in both tissues. Also, the rate of initiation of transcription of aldolase A is the same in the adult kidney and liver although there is 40 times more steady state aldolase A mRNA in the kidney than in the liver.
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PMID:Distinct developmental regulatory mechanisms for two members of the aldolase gene family. 182 33

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

We analysed the genetic diversity and environmental correlates of the aldolase A and B genes by means of restriction endonucleases (DNA RFLP analysis), in the four chromosomal species (2n = 52, 54, 58 and 60) of the actively speciating subterranean mole-rats of the Spalax ehrenbergi superspecies in Israel. The results indicated that: (i) both aldolase genes are highly polymorphic; (ii) fragment frequencies and fragment profiles display geographical patterns and significant ecological correlates; (iii) discriminant analysis largely succeeded in separating the four chromosomal species on the basis of variation of aldolase RFLPs.
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PMID:Aldolase DNA polymorphism in subterranean mole-rats: genetic differentiation and environmental correlates. 198 68

The aldolase isozymes A, B, and C in tumor tissues (63) and sera (104) of patients with lung cancer were determined with an enzyme immunoassay system, compared with normal lung tissues (13), and the sera of normal healthy subjects (100). Tissue aldolase A and C concentrations were enhanced in 83% (52/63) and 51% (32/63) of patients with lung cancer, respectively, regardless of histologic type or stage (P less than 0.01). But aldolase B was not elevated in tissue levels. In the sera of patients with lung cancer, there were no significant elevations of the isozymes. Immunohistochemically aldolase A and C stained more intensely in the cytoplasm of lung cancer cells than those in normal tissues. These results indicate lung cancer cells contain enhanced tissue levels of aldolase A and C.
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PMID:Immunochemical and immunohistochemical studies on three aldolase isozymes in human lung cancer. 200 36


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