scholarly journals Comparison of glycolytic enzyme and isoenzyme activity in breast cancers and dysplasia

2012 ◽  
Vol 65 (5-6) ◽  
pp. 200-205 ◽  
Author(s):  
Katica Bajin-Katic
Keyword(s):  
Breast Cancer ◽  
Enzyme Activity ◽  
Lactate Dehydrogenase ◽  
Pyruvate Kinase ◽  
Enzyme Concentration ◽  
Glycolytic Enzyme ◽  
Disc Electrophoresis ◽  
Breast Cancers ◽  
Lactate Dehydrogenase Activity ◽  
Total Enzyme Activity

The study was aimed at assessing the total enzyme activity and the profile of breast cancer and dysplasia on the human material. In addition, the validity of data was evaluated from the aspect of improving diagnostics. Lactate dehydrogenase activity, as well as the profile of its isoenzymes, pyruvate kinase and hexokinase, were measured. The study included 60 samples of breast cancer, out of which 20 were benign breast tumours and 40 were 1st and 2nd degree dysplasia of the breast. The samples were collected from the patients operated at the Institute for Oncology of Faculty of Medicine in Sremska Kamenica. Lactate dehydrogenase isoenzymes were separated by the vertical polyacrylamide gel disc electrophoresis according to the slightly modified Brewer and Ashworth?s method. The activity of all the tested enzymes was measured under the conditions of linear kinetics in the function of time and enzyme concentration. Lactate dehydrogenase-5 was found in 88% of the analyzed breast cancer samples, whereas it was not detected in breast dysplasia. Pyruvate kinase (4.-isoenzyme) was about 50 times higher and the activity of hexokinase was 3 times higher in breast cancer than in breast dysplasia. Lactate dehydrogenase-5 and pyruvate kinase (4.-isoenzyme) are particularly important and reliable markers of malignity. The results obtained for quantitative and qualitative changes in the enzyme activity can be used to improve diagnostics and early diagnostics of malignant breast neoplasm.

Heterogeneity of Glycolytic Enzyme Activity and Isozyme Composition of Pyruvate Kinase in Breast Cancer

Tumor Biology ◽  
1988 ◽  
Vol 9 (4) ◽  
pp. 178-189 ◽  
Author(s):  
A. Hennipman ◽  
B.A van Oirschot ◽  
J. Smits ◽  
G. Rijksen ◽  
G.E.J. Staal
Keyword(s):  
Breast Cancer ◽  
Enzyme Activity ◽  
Pyruvate Kinase ◽  
Glycolytic Enzyme

scholarly journals Targeting Pyruvate Kinase M2 and Lactate Dehydrogenase A Is an Effective Combination Strategy for the Treatment of Pancreatic Cancer

Cancers ◽  
2019 ◽  
Vol 11 (9) ◽  
pp. 1372 ◽  
Author(s):  
Goran Hamid Mohammad ◽  
Vessela Vassileva ◽  
Pilar Acedo ◽  
Steven W. M. Olde Damink ◽  
Massimo Malago ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Cell Proliferation ◽  
Enzyme Activity ◽  
Lactate Dehydrogenase ◽  
Tumor Growth ◽  
Pyruvate Kinase ◽  
Glycolytic Enzymes ◽  
Pyruvate Kinase M2 ◽  
Tumor Tissues

Reprogrammed glucose metabolism is one of the hallmarks of cancer, and increased expression of key glycolytic enzymes, such as pyruvate kinase M2 (PKM2) and lactate dehydrogenase A (LDHA), has been associated with poor prognosis in various malignancies. Targeting these enzymes could attenuate aerobic glycolysis and inhibit tumor proliferation. We investigated whether the PKM2 activator, TEPP-46, and the LDHA inhibitor, FX-11, can be combined to inhibit in vitro and in vivo tumor growth in preclinical models of pancreatic cancer. We assessed PKM2 and LDHA expression, enzyme activity, and cell proliferation rate after treatment with TEPP-46, FX-11, or a combination of both. Efficacy was validated in vivo by evaluating tumor growth, PK and LDHA activity in plasma and tumors, and PKM2, LDHA, and Ki-67 expression in tumor tissues following treatment. Dual therapy synergistically inhibited pancreatic cancer cell proliferation and significantly delayed tumor growth in vivo without apparent toxicity. Treatment with TEPP-46 and FX-11 resulted in increased PK and reduced LDHA enzyme activity in plasma and tumor tissues and decreased PKM2 and LDHA expression in tumors, which was reflected by a decrease in tumor volume and proliferation. The targeting of glycolytic enzymes such as PKM2 and LDHA represents a promising therapeutic approach for the treatment of pancreatic cancer.

scholarly journals Regional enzyme development in rat brain. Enzymes associated with glucose utilization

1984 ◽  
Vol 218 (1) ◽  
pp. 131-138 ◽  
Author(s):  
S F Leong ◽  
J B Clark
Keyword(s):  
Enzyme Activity ◽  
Lactate Dehydrogenase ◽  
Rat Brain ◽  
Brain Regions ◽  
Glycolytic Enzyme ◽  
Glycolytic Potential ◽  
Key Enzyme ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Potential Enzyme Activity ◽  
The Brain

The development of key enzyme activities concerned with glucose metabolism was studied in six regions of the rat brain in animals from just before birth (-2 days) through the neonatal and suckling period until adulthood (60 days old). The brain regions studied were the cerebellum, medulla oblongata and pons, hypothalamus, striatum, mid-brain and cortex. The enzymes whose developmental patterns were investigated were hexokinase (EC 2.7.1.1), aldolase (EC 4.1.2.13), lactate dehydrogenase (EC 1.1.1.27) and glucose-6-phosphate dehydrogenase (EC 1.1.1.49). Hexokinase, aldolase and lactate dehydrogenase activities develop as a single cluster in all the regions studied, although the timing of this development varies from region to region. Glucose-6-phosphate dehydrogenase activity, however, declines relative to glycolytic enzyme activity as the brain matures. When the different brain regions are compared, it is clear that the medulla develops its glycolytic potential, as indicated by its potential enzyme activity, considerably earlier than the other regions (hypothalamus, striatum and mid-brain), with the cortex and cerebellar activities developing even later. This enzyme developmental sequence correlates well with the neurophylogenetic development of the brain and adds support to the hypothesis that the development of the potential for glycolysis in the brain is a necessary prerequisite for the development of neurological competence.

scholarly journals Extraction, Purification and Kinetic Study of Lactate Dehydrogenase of Male Chicken from Ebocha-oil Exploration Area, Nigeria

2019 ◽  
pp. 1-12
Author(s):  
Chimdi E. Esonu ◽  
G. O. C. Onyeze ◽  
Kizito M. E. Iheanacho ◽  
Linus N. Nwaogu ◽  
Simon-Peter Odirichukwu
Keyword(s):  
Enzyme Activity ◽  
Lactate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Gel Filtration ◽  
Oil Exploration ◽  
Sodium Pyruvate ◽  
Lactate Dehydrogenase Activity ◽  
Ammonium Sulphate Precipitation ◽  
Muscle Tissues ◽  
Exploration Area

Aim: This study focused on the extraction, purification and kinetic studies of lactate dehydrogenase of male chickens from Ebocha oil exploration area, Imo state, Nigeria. Methods: Twenty-one apparently healthy mature (6-9 months) male chickens (Gallus domesticus) from Ebocha oil exploration area, Imo State, Nigeria were screened for lactate dehydrogenase activity, thus accessing the level of chronic cell exposure to gas flaring. Their thigh muscle tissues were severed and investigated for lactate dehydrogenase activity using the standard method and sodium pyruvate as the substrate. Lactate dehydrogenase was isolated and purified by ammonium sulphate precipitation, desalted by dialysis and then gel filtration. Results: The enzyme activity increased with advancement in the purification steps and was maximum using dialysis. The values for the lactate dehydrogenase activities were 103.43±3.27 U/L, 279.50±5.38 U/L, 318.16±13.08 U/L, 100.47±2.59 U/L, with a purification fold of 1, 3.7, 6.24 and 2.55 for the purification steps respectively. Also, the values of the protein concentrations were 0.071 mg/ml, 0.050 mg/ml, 0.035 mg/ml and 0.027 mg/ml (values for the crude enzyme, ammonium sulphate precipitation, dialysis and gel filtration respectively). The enzyme showed optimal activity at pH range of 5.5-6.5 and temperature of 30ºC-40ºC. Using sodium pyruvate as the substrate, with a fixed enzyme volume, an increase in the concentration of substrate resulted in increase in enzyme activity until a saturation point 0.3mM was reached. The apparent Km and Vmax values obtained were 0.01 mM and 0.12 U/mg/min. The Lineweaver-burk plot of the partially purified enzyme gave real Km and Vmax values of 0.20 mM and 0.16 U/mg/min respectively. Conclusion: Partial purification procedures and biochemical properties of lactate dehydrogenase, from the muscle tissues of male chickens of Ebocha origin, gives room for more investigation on the metabolic shift caused by chronic exposure of the environment, humans and livestock to gas flaring and petroleum exploration.

scholarly journals In-Cell Determination of Lactate Dehydrogenase Activity in a Luminal Breast Cancer Model – ex vivo Investigation of Excised Xenograft Tumor Slices Using dDNP Hyperpolarized [1-13C]pyruvate

Sensors ◽  
2019 ◽  
Vol 19 (9) ◽  
pp. 2089 ◽  
Author(s):  
Yael Adler-Levy ◽  
Atara Nardi-Schreiber ◽  
Talia Harris ◽  
David Shaul ◽  
Sivaranjan Uppala ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Lactate Dehydrogenase ◽  
Cultured Cells ◽  
Ex Vivo ◽  
Lactate Production ◽  
Response Assessment ◽  
Luminal Breast Cancer ◽  
Cancer Type ◽  
Lactate Dehydrogenase Activity ◽  
Ldh Activity

[1-13C]pyruvate, the most widely used compound in dissolution-dynamic nuclear polarization (dDNP) magnetic resonance (MR), enables the visualization of lactate dehydrogenase (LDH) activity. This activity had been demonstrated in a wide variety of cancer models, ranging from cultured cells, to xenograft models, to human tumors in situ. Here we quantified the LDH activity in precision cut tumor slices (PCTS) of breast cancer xenografts. The Michigan Cancer Foundation-7 (MCF7) cell-line was chosen as a model for the luminal breast cancer type which is hormone responsive and is highly prevalent. The LDH activity, which was manifested as [1-13C]lactate production in the tumor slices, ranged between 3.8 and 6.1 nmole/nmole adenosine tri-phosphate (ATP) in 1 min (average 4.6 ± 1.0) on three different experimental set-ups consisting of arrested vs. continuous perfusion and non-selective and selective RF pulsation schemes and combinations thereof. This rate was converted to an expected LDH activity in a mass ranging between 3.3 and 5.2 µmole/g in 1 min, using the ATP level of these tumors. This indicated the likely utility of this approach in clinical dDNP of the human breast and may be useful as guidance for treatment response assessment in a large number of tumor types and therapies ex vivo.

scholarly journals The liver/erythrocyte pyruvate kinase gene complex [Pk-1] in the mouse: regulatory gene mutations

1991 ◽  
Vol 58 (3) ◽  
pp. 233-241 ◽  
Author(s):  
Lesley A. Fitton ◽  
Morag Davidson ◽  
Karen J. Moore ◽  
Daniel J. Charles ◽  
Walter Pretsch ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Pyruvate Kinase ◽  
Structural Gene ◽  
Regulatory Gene ◽  
Gene Mutations ◽  
Enzyme Concentration ◽  
Gene Complex ◽  
Kinase Gene ◽  
Wild Mice ◽  
Allelic Differences

SummaryNine enzyme activity variants and one charge variant of liver/erythrocyte pyruvate kinase have been found amongst laboratory and wild mice. Four of the enzyme activity variants were previously reported to be caused by allelic differences in the structural gene,Pk-ls. Analysis of two putative regulatory gene mutations is now reported, both of which map at, or close to, the structural gene on chromosome 3. One of these mutations, in the inbred strain SWR, is tissue specific, affecting enzyme concentration in the liver but not the erythrocyte the other, which arose in a mutation experiment, doubles the enzyme concentration in both tissues. The organization and the nomenclature in the [Pk-1] gene complex are discussed and are compared with the organization of other comprehensively analysed gene complexes in the mouse.

Sign in / Sign up

Export Citation Format

Share Document