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)

The activities of six different enzymes were compared in 29 normal, 34 dysplastic, and 80 cancerous (both primary and metastatic) human breast tissues; in MCF-7 cells; and in primary rat mammary tumors. Benign lesions generally showed enzyme activities similar to those of normal breast tissues. Malignant tumors had significantly increased activities of lactate dehydrogenase (LDH), malate dehydrogenase (MDH), fructose-bisphosphate aldolase, hexokinase (HK), pyruvate kinase (PK), and creatine kinase. Enzyme activity in the malignant tumor was always higher than that in apparently normal or fibrocystic tissue from the same patient. Enzyme activities did not correlate with the levels of estrogen and progesterone receptors. LDH, MDH, and HK were elevated to a similar extent in all the tissues examined. Conversely, PK was elevated to a much greater extent in cancerous tissues, particularly in MCF-7 cells. The elevated activities of these enzymes may have diagnostic potential, especially when tumor tissue and apparently normal tissue from the same patient are compared.
J Natl Cancer Inst 1984 Feb
PMID:Enzyme activities in normal, dysplastic, and cancerous human breast tissues. 658 10

Isozyme patterns of 23 different enzymes were compared in normal, benign, and malignant breast tissues; in MCF-7 cells; and in organoids of normal human breast tissue. Benign lesions generally showed isozyme patterns similar to those of normal tissues. Lactate dehydrogenase isozyme 5 was significantly increased in malignant tumors; MCF-7 cells had only lactate dehydrogenase (L-lactate:NAD oxidoreductase; EC 1.1.1.27). The mitochondrial form of malate dehydrogenase was also significantly increased in human malignant tumors; this was especially evident when comparing tumor and apparently uninvolved breast tissue from the same patient. The K4 isozyme of pyruvate kinase was the major form in most malignant breast tumors, but in only 41% of normal tissues, 30% of fibrocystic disease specimens, and 46% of fibroadenomas. A more anodal band of pyruvate kinase, probably a K3M or K3Kpm hybrid, predominated in most normal and benign tissues, but in only 63% of primary and 56% of secondary tumors. All specimens had predominantly creatine kinase BB, aldolase A4, and hexokinase I. Traces of aldolase A3C and of hexokinase II were observed in some tumors. None of the tumors had the Regan variant of alkaline phosphatase. The isozymes of lactate and malate dehydrogenases and of pyruvate kinase appear to be the most promising as putative tumor markers.
Cancer Res 1983 Dec
PMID:Isozyme patterns of normal, benign, and malignant human breast tissues. 664 May 38

A solid-phase, noncompetitive radioimmunoassay has been developed for aldolase B in human serum and tissues. Aldolase B was purified from human liver, and specific antisera to purified aldolase B were obtained from chickens. Specific antihuman aldolase B IgG was purified by affinity chromatography. Disposable polypropylene plates were coated with affinity purified specific IgG antibody and used for radioimmunoassay with 125I-specific IgG antibody to aldolase B. The nonspecific binding was minimized by saturating the binding sites of the plates with 2% ovalbumin in 0.1% Tween 20. This radioimmunoassay is specific for the aldolase B subunit, with no cross-reactivity with human aldolase A or aldolase C subunits. Aldolase B is predominantly found in normal liver. Relatively high aldolase B levels are also observed in kidney. Serum levels of aldolase B in 21 normal subjects ranged from 21 to 39 ng per ml, with a mean of 28.7 +/- 8.6 (2 S.D.) ng per ml. Forty of 42 (95%) patients with acute and chronic hepatitis without cirrhosis had serum aldolase B levels greater than 40 ng per ml. Serum aldolase B levels correlated well with total serum aldolase enzyme activities (r = 0.967) and SGPT (r = 0.951) in patients with liver diseases. In cancer patients, serum aldolase B was slightly elevated in 15 of 26 (58%) patients with cancer metastatic to the liver or primary liver cell carcinoma, whereas no elevation of serum aldolase B was observed in 16 cancer patients without liver metastasis. Measurements of aldolase B serum levels by radioimmunoassay appear to be a useful measure of liver cell necrosis from benign or malignant liver diseases.
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PMID:Human aldolase B serum levels: a marker of liver injury. 672 19

A comparison of several serum tumor markers (lactate dehydrogenase (LDH), LDH isozyme, hydroxybutylrate dehydrogenase (HBD), alkaline phosphatase (ALP), cholinesterase (Choline-E), aldolase (ALD), leucine aminopeptidase (LAP), gamma-glutamyl transpeptidase (gamma-GTP), human chorionic gonadotropin (HCG), carcinoembryonic antigen (CEA) and alpha 1-fetoprotein (AFP)) was made in patients with carcinoma or benign tumor of the ovary and healthy control subjects. The greatest positive rates were obtained with the markers HBD (76.5%) and Choline-E (73.3%) for patients with carcinoma of the ovary, respectively. However, based on false positive results, Choline-E was also greatest (50.0%) for patients with benign tumor of the ovary. The lowest false positive rates were obtained with ALD, but the positive rates for patients with stage I and II diseases were 0.0%. The most suitable single marker for patients with stage I and II diseases was HBD (62.5%), followed by LDH (41.7%). Three of 4 patients with early cancer, who had normal serum LDH levels, showed abnormal LDH isozyme patterns (elevated LDH-4 and -5). A combination of LDH activity and LDH isozyme resulted in an increase in the positive results (41.7% to 70.0%), that is, the cancer patients were positive for one of the two markers. For CEA, AFP and HCG, the positive results were 26.9%, 19.0% and 7.1%, respectively. Positive and false positive rates for ALP were 36.7% and 7.1%, but the positive rates in the early stage were lower (14.3%), compared to those for LDH and HBD. HBD and LDH activities in the ovarian malignant tissues and ascitic fluids were significantly higher than those in the benign tumor tissues and ascitic fluids, resulting in a significant elevation of serum LDH and HBD levels in the patients. Moreover, it was suggested that inhibition test of ALP by the inhibitors might be able to identify the tissue origin of ALP in the cancer patients.
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PMID:[Diagnostic value of biochemical tumor markers in serum of patients with cancer of the ovary]. 683 10

GLycolytic enzymes were studied from normal human retinas (both fetal and adult) and from retinoblastomas of eight patients and an established retinoblastoma cell line. No significant differences were found between the enzyme activities in the tissues investigated except for hexokinase and pyruvate kinase, which were significantly decreased in the tumor cells. In fetal retina, five different forms of pyruvate kinase could be detected by electrophoresis (K4, K3M, K2M2, KM3, and M4). In adult retina the K4 isozyme is almost absent, while in retinoblastoma the M4 isozyme is hardly present. In the retinoblastoma cell line, the M4 isozyme is completely absent. Alanine inhibition of pyruvate kinase from the retinoblastoma cell line is more inhibited compared to the pyruvate kinase of fetal retina and retinoblastoma and is even more inhibited compared to adult retina. Electrophoresis of aldolase from adult retina revealed the presence of all potential A-C hybrids (A4, A3C, A2C2, AC3, and C4). Fetal retina, however, is characterized by the predominance of the A type. The same patterns were observed in the retinoblastoma cell line and retinoblastoma. However, in other brain tumors, e.g., gliomas of adults, a five-membered A-C hybrid set is found. Electrophoresis of hexokinase from normal fetal and adult retina revealed the predominance of hexokinase type I; retinoblastoma and retinoblastoma cell line are both characterized by the presence of considerable amounts of hexokinase type II. The isozyme shifts in retinoblastoma result in an enzyme pattern identical to that of fetal retina except for the presence of hexokinase type II.
Cancer Res 1982 Oct
PMID:Characterization of some glycolytic enzymes from human retina and retinoblastoma. 710 15

A specific radioimmunoassay was developed for the quantification of human muscle type aldolase (M-ALD) in human serum. The method utilized the double antibody radioimmunoassay technique using radioiodinated M-ALD, chicken antibody to M-ALD and rabbit antibody to chicken IgG. The serum M-ALD values of 41 normal healthy subjects ranged from 130 to 210 ng/ml, average 171 +/- 39 ng/ml. In 76 noncancer hospital patients, excluding patients with muscle diseases, the serum M-ALD values ranged from 125 to 220 ng/ml, average 164 +/- 52 ng/ml. In contrast, 129 cancer patients had high serum M-ALD values of 586 +/- 926 ng/ml, ranging from 85 to 5,800 ng/ml. Eighty-six percent of the cancer patients showed serum M-ALD concentrations over the normal range. The measurement of M-ALD values in the serum of patients by radioimmunoassay may be a valuable laboratory test in the diagnosis and follow-up of cancer patients.
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PMID:Diagnosis of cancer by radioimmunoassay of muscle type aldolase. 742 85

We studied the alteration of aldolase isozymes in the serum and tissues of patients with cancer and other diseases using radioimmunoassays specific for aldolase A, B, and C subunits. Aldolase B was predominantly found in adult liver, where aldolase A and C were distinctly low. Aldolase A and B showed almost the same concentration in fetal liver, while in neonatal liver aldolase B protein concentrations were much higher than aldolase A. In contrast, aldolase A was the predominant isozyme found in hepatoma and gastric cancer tissues, whereas aldolase B was distinctly low in hepatoma tissues, and extremely low in gastric cancer tissues. These results suggest that the aldolase A is a more fetal type of liver isozyme than the aldolase B and C, and aldolase B is a more differentiated type of liver isozyme than aldolase A and C. Serum FDP aldolase activities were elevated in half of patients with liver diseases, all patients with muscle diseases and a few patients with cancer. Serum aldolase A levels were elevated in patients with muscle diseases and cancer, but not elevated in patients with liver diseases. In contrast, serum aldolase B levels were elevated in patients with liver disease, but not elevated in patients with muscle diseases and other diseases without liver injury. Serum aldolase B levels showed a trend to decrease in cancer patients with normal GPT levels. Serum aldolase A/B ratios were significantly increased in cancer patients with normal GPT levels, whereas they showed the decreased levels in patients with liver diseases.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Alteration of aldolase isozymes in serum and tissues of patients with cancer and other diseases. 804 42

Enzymology has acquired a prominent place in human pathology, and serum enzyme investigations have become a prerequisite for various diseases, including cancer. Serum phosphohexose isomerase (PHI), aldolase (ALD) and alkaline phosphatase (ALP) levels were evaluated in 90 untreated patients with cervical carcinoma and 84 healthy age-matched females (controls). The concentrations of the three enzymes were significantly raised (p < 0.001) in patients compared to the controls. Receiver operating characteristic curve analysis revealed higher sensitivities of PHI and ALP, as compared to ALD at different specificity levels between 60 and 95%. Combined use of PHI and ALP revealed increased sensitivity and specificity. Combined use of PHI, ALD and ALP revealed a greater number of responders with enzyme values within the normal range than nonresponders. The results suggest that combined evaluation of the enzymes might be helpful to establish a useful aid to strengthen the armamentarium currently employed in the diagnosis and treatment monitoring of patients with cervical carcinoma.
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PMID:Combined use of serum enzyme levels as tumor markers in cervical carcinoma patients. 814 29

Glycolysis, which is the primary energy source in cancer cells, is known to be controlled by allosteric regulators, as well as by reversible binding of glycolytic enzymes to cytoskeleton. We have previously found that different calmodulin antagonists decrease the levels of allosteric activators of glycolysis, and reduce ATP content and cell viability in B16 melanoma cells. Here we report of a novel, additional, mechanism of action of calmodulin antagonists in melanoma cells. We show that these drugs cause a detachment of the glycolytic enzymes, phosphofructokinase (ATP: D-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) and aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13), from cytoskeleton of B16 melanoma cells. This effect was dose- and time-dependent, and preceded the decrease in cell viability. The detachment of glycolytic enzymes from cytoskeleton would reduce the provision of local ATP, in the vicinity of the cytoskeleton-membrane and would affect cytoskeleton structure. Since the cytoskeleton is being recognized as an important modulator of cell function, proliferation, differentiation and neoplasia, detachment of the glycolytic enzymes from cytoskeleton induced by calmodulin antagonists, as well as their reported inhibitory action on cell proliferation, make these drugs most promising agents in treatment of cancer.
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PMID:Detachment of glycolytic enzymes from cytoskeleton of melanoma cells induced by calmodulin antagonists. 921 7

It is known that the serum in cancer patients has the characteristics of the heat-stability. The factor produce the heat-stability is known to be due to tumor marker(TM) such as CEA, CA125(glycoprotein), CA19-9, CA15-3, SLX, CA50, CA72-4, DU-PAN-2, ST-439, SPAN-1(mucin) and alpha 1-acid glycoprotein, IAP(acute reactants). CEA belongs to IgG supergene family protein and is not oncofetal protein. CA19-9 is synthesis in subjects with Le(a) or Le(b) type, but negative in Le(a- b-) type. Thus, CA19-9 is not available as TM in Le(a- b-) type. Many TMs can be classified in 3 types because cancer cell has the character of immature cells which composed of immature proteins or glycoproteins. (1) Oncofetal protein: AFP(fetal albumin), PTHrP(fetal PTH) (2) The immature isozyme type: increase of amylase(salivary type), CPK(brain type) and aldolase (muscle and brain type) (3) The immature protein in biosynthesis process: increase of precursor protein(prepro type or pro type) such as PIVKA-II(preprothrombin), ProGRP, TPA or CYFRA 21-1(pro-keratin?) and hormone precursor in hormone producing tumor.
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PMID:[Tumor marker--present and future]. 931 Dec 62


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