Total tissue lactate dehydrogenase activity in endometrial carcinoma

2008 ◽  
Vol 18 (6) ◽  
pp. 1272-1278 ◽  
Author(s):  
Š. ŠIMAGA ◽  
M. Abramić ◽  
M. Osmak ◽  
D. Babić ◽  
J. Ilić-Forko
Keyword(s):  
Lactate Dehydrogenase ◽  
Endometrial Carcinoma ◽  
Significant Rise ◽  
Diagnostic Sensitivity ◽  
Ovarian Carcinomas ◽  
Tissue Samples ◽  
Lactate Dehydrogenase Activity ◽  
Ldh Activity ◽  
Clinicopathologic Findings ◽  
Total Tissue

Lactate dehydrogenase (LDH) is essential for continuous glycolysis necessary for accelerated tumor growth. The aim of this study was to reconsider if assay of total tissue activity of this enzyme could be useful as marker for endometrial carcinoma (EC). Activity of LDH was measured spectrophotometrically in homogenate supernatants of uterine tissue samples of 40 patients (10 normal endometria, 27 normal myometria, and 33 EC), including 30 matched pairs. Data obtained were analyzed in relation to clinical and histopathologic findings and compared with our previously published results on the tissue levels of the same enzyme in ovarian cancer and on the proteolytic activity of dipeptidyl peptidase III (DPP III) in EC (suggested biochemical indicator of this malignancy). Significantly increased (1.8–3.0 times; P< 1 × 10−4) LDH activity was observed in EC samples if compared with normal uterine tissues. This rise was not related to the clinicopathologic findings, however. In contrast to previous results on LDH in ovarian carcinomas, a significant rise in LDH activity was found already in grade 1 EC. Using the cutoff value of 1.06 U/mg, diagnostic sensitivity of 82%, specificity of 100%, and accuracy of 91% for total tissue LDH assay have been calculated. A correlation of tissue's LDH and DPP III activities was found, and their combined assay for EC showed increased diagnostic sensitivity (94%) and accuracy (96%).

Quantitative biochemical analysis of lactate dehydrogenase in human ovarian tissues: correlation with tumor grade

2005 ◽  
Vol 15 (3) ◽  
pp. 438-444 ◽  
Author(s):  
Š. ŠIMAGA ◽  
M. Osmak ◽  
D. Babič ◽  
M. ŠPREM ◽  
B. Vukelič ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Specific Activity ◽  
Malignant Tumors ◽  
Ovarian Tissue ◽  
Tumor Grade ◽  
Benign Tumors ◽  
Ovarian Carcinomas ◽  
Lactate Dehydrogenase Activity ◽  
Ldh Activity ◽  
Benign Ovarian Tumor

In an attempt to identify glycolytic capacity of normal and neoplastic human ovary, total lactate dehydrogenase (LDH) activity was measured in tissue cytosol originating from 69 patients (18 with benign ovarian tumor, 34 with ovarian carcinoma, six with nonepithelial ovarian malignant tumors, and 11 with tumor metastatic to ovary) and compared to the LDH activity of normal ovarian tissues (n = 19). Median value of total LDH-specific activity expressed as U/mg protein was 0.546 in normal tissues, 0.584 in benign tumors, 1.071 in malignancies metastatic to ovaries, 0.872 in nonepithelial primary ovarian tumors, and 0.818 in primary carcinomas. A significant rise in LDH-specific activity was found in malignant primary and secondary tumors of epithelial and nonepithelial origin, but not in benign neoplasms, compared to the activity in normal tissue. Ovarian carcinomas of serous histologic type did not differ in LDH activity from mucinous tumors. However, poorly differentiated carcinomas (grade 3) showed significantly enhanced activity of this glycolytic enzyme when compared to its grade 1 counterpart. The subgroup of grade 1 tumors did not differ in LDH activity from normal and benign ovarian tissue. Obtained results suggest that direct correlation might exist between ovarian epithelial tumor grade and lactate dehydrogenase activity.

scholarly journals MODELING THE EFFECTS OF LEAD POLLUTION ON LACTATE DEHYDROGENASE ACTIVITY

10.23856/3305 ◽  
2019 ◽  
Vol 33 (2) ◽  
pp. 50-55
Author(s):  
Olena Konovalova
Keyword(s):  
Heavy Metals ◽  
Lactate Dehydrogenase ◽  
Energy Metabolism ◽  
Lead Acetate ◽  
Lead Pollution ◽  
Lactate Dehydrogenase Activity ◽  
Influence Mechanism ◽  
Ldh Activity ◽  
Small Doses ◽  
Experimental Substantiation

The changes of activity of LDH and its isoenzymatic fractions under load with lead acetate are described. The introduction of a subacute dose of Pb2 + led to a decrease in the LDH activity of the rat liver and an increase in the heart. Preliminary introduction of small doses of Pb2 + partially prevents increased LDH activity in the heart and completely inhibits its increase in the liver. The proportion of urea-stable fraction in the heart and blood serum is significantly increased, indicating an increase in the aerobic direction of energy metabolism. The obtained results are the experimental substantiation of further investigations of influence mechanism of heavy metals on the organism, as well as the motivation to prevent environmental pollution by man-made xenobiotics.

scholarly journals Urinary Lactate Dehydrogenase Activity and Its Isozyme Patterns in Kawasaki Disease

2017 ◽  
Vol 2017 ◽  
pp. 1-6
Author(s):  
Yoichi Kawamura ◽  
Seiichiro Takeshita ◽  
Takashi Kanai ◽  
Mari Takizawa ◽  
Yusuke Yoshida ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Kawasaki Disease ◽  
Pattern Analysis ◽  
Upper Urinary Tract ◽  
Potential Significance ◽  
Lactate Dehydrogenase Activity ◽  
Isozyme Patterns ◽  
Ldh Activity ◽  
Sterile Pyuria ◽  
Ldh Isozymes

Abnormal urinary findings, such as sterile pyuria, proteinuria, and microscopic hematuria, are often seen in the acute phase of Kawasaki disease (KD). We investigated the potential significance of urinary lactate dehydrogenase (U-LDH) activity and its isozyme patterns in KD. Total U-LDH activity and its isozymes (U-LDH1-5) levels were compared among 120 patients with KD, 18 patients with viral infection (VI), and 43 patients with upper urinary tract infection (UTI) and additionally compared between intravenous immunoglobulin (IVIG) responders (n=89) and nonresponders (n=31) with KD. Total U-LDH activity was higher in KD (35.4±4.8 IU/L, P<0.05) and UTI patients (66.0±8.0 IU/L, P<0.01) than in VI patients (17.0±6.2 IU/L). In the isozyme pattern analysis, KD patients had high levels of U-LDH1 and U-LDH2, while UTI patients had high levels of U-LDH3, U-LDH4, and U-LDH5. Furthermore, IVIG nonresponders of KD had significantly higher levels of total U-LDH activity (45.1±4.7 IU/L, P<0.05), especially U-LDH1 and U-LDH2 (P<0.05), than IVIG responders (32.0±2.8 IU/L). KD patients have increased levels of total U-LDH activity, especially U-LDH-1 and U-LDH2, indicating a unique pattern of U-LDH isozymes different from that in UTI patients.

Lactate Dehydrogenase Activity and Isoenzyme Patterns in Serous Middle Ear Effusions

1973 ◽  
Vol 82 (2) ◽  
pp. 192-195 ◽  
Author(s):  
S. K. Juhn ◽  
John S. Huff ◽  
Michael M. Paparella
Keyword(s):  
Lactate Dehydrogenase ◽  
Otitis Media ◽  
Middle Ear ◽  
Biochemical Characterization ◽  
Middle Ear Mucosa ◽  
Lactate Dehydrogenase Activity ◽  
Intracellular Enzyme ◽  
Ldh Activity ◽  
Serous Otitis Media ◽  
Isoenzyme Patterns

Biochemical characteristics of middle ear effusions (MEE) should provide a better understanding of the etiopathogenesis of serous otitis media. In order to develop another parameter for the biochemical characterization of the MEE, lactate dehydrogenase (LDH) and LDH isoenzyme patterns in the serous middle ear effusion and serum from 20 patients with serous otitis media were compared. The LDH activity was measured by the usual spectrophotometric method. The isoenzyme patterns were compared on electropherograms using cellulose polyacetate strips. The LDH activity in MEE was significantly higher (P < 0.001) than it was in serum. Fractions of isoenzymes 1 and 2 were each smaller in MEE than in serum. Isoenzymes 4 and 5 have a significantly higher (P < 0.001) fraction in MEE than in serum. Since LDH is an intracellular enzyme and middle ear mucosa is reported to have high content of isoenzymes 4 and 5, the inflammatory changes in the middle ear mucosa which may release intracellular LDH, are suggested as the cause of both higher activity of LDH and the higher fractions of isoenzymes 4 and 5 in MEE than those in the serum.

scholarly journals Relationship between ontogenetic changes in foraging ecology and muscle lactate dehydrogenase activity in wild smallmouth bass (Micropterus dolomieu)

2016 ◽  
Vol 73 (9) ◽  
pp. 1389-1394 ◽  
Author(s):  
Frédéric Laberge ◽  
Nicholas Edmunds ◽  
Irene Yin-Liao ◽  
Kevin S. McCann
Keyword(s):  
Body Size ◽  
Lactate Dehydrogenase ◽  
Foraging Ecology ◽  
Trophic Position ◽  
Smallmouth Bass ◽  
Diet Shift ◽  
Micropterus Dolomieu ◽  
Muscle Lactate ◽  
Lactate Dehydrogenase Activity ◽  
Ldh Activity

The activity of muscle glycolytic enzymes scales positively with body size in active fish, a phenomenon thought to counter the increased costs of burst swimming faced by larger individuals. Recent work argued that changes in these enzymes during ontogeny additionally reflect changes in foraging ecology. Here, we evaluated the relationship between muscle anaerobic metabolism and foraging ecology in a population of wild smallmouth bass (Micropterus dolomieu) by relating activity of muscle lactate dehydrogenase (LDH) to estimates of trophic position and habitat use obtained from stable isotope signatures. As expected, LDH activity increased with body size. However, further analysis showed associations between foraging ecology and LDH activity. Specifically, a shift to higher trophic position, indicating a change in diet, was paralleled by a shift to increased LDH activity. However, a steady mass-specific decrease in LDH activity was observed as the fish grew above the size associated with this diet shift. Further, lower LDH activity was associated with increasing use of littoral carbon sources. These findings contribute to our understanding of how plasticity in muscle anaerobic potential is associated with fish foraging ecology.

scholarly journals Lactate-dehydrogenase activity in the rat testis: a comparison between fluorometric assay of freeze-dried sections and histochemical localization with phenazine methosulphate.

1978 ◽  
Vol 26 (11) ◽  
pp. 967-972 ◽  
Author(s):  
L Heywood ◽  
A Blackshaw
Keyword(s):  
Lactate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Fluorometric Assay ◽  
Histochemical Localization ◽  
Assay Method ◽  
Interstitial Tissue ◽  
Lactate Dehydrogenase Activity ◽  
Ldh Activity ◽  
Freeze Dried ◽  
Phenazine Methosulphate

The activity of lactate dehydrogenase (LDH) in freeze-dried sections of rat testes was determined by using a fluorometric assay method and found to be 4.47 +/- 0.23 moles/Kg dry weight/hr (MKDH +/- S.E.M.) in whole sections, 3.31 +/- 0.16 in tubules and 12.0 +/- 1.9 in interstitial tissue. The activities and regional variation are similar to those measured in nervous tissue and are well correlated with the histochemical localization of LDH activity when phenazine methosulphate (PMS) is not used as an electron carrier. LDH and lipoamide dehydrogenase activity have the same histochemical distribution and there is no nonspecific staining with either method. The use of PMS results in reduced dependence on substrate and coenzyme and does not indicate higher interstitial activity but may provide an indication of developing lactate metabolism in maturing sperm. It is recomended that methods with and without PMS be used in studies of LDH activity in the testis.

Lactate dehydrogenase activity as measured by the SMAC is related to flow-cell energy.

1982 ◽  
Vol 28 (10) ◽  
pp. 2106-2109 ◽  
Author(s):  
E A Robertson ◽  
E Wright ◽  
R A Chesler ◽  
R J Elin
Keyword(s):  
Lactate Dehydrogenase ◽  
Light Intensity ◽  
Fiber Optic ◽  
Lactate Dehydrogenase Activity ◽  
Flow Cells ◽  
Ldh Activity ◽  
Cell Energy ◽  
The Difference ◽  
Calibration Material

Abstract Determination of lactate dehydrogenase (LDH) activity in the SMAC (Technicon) is based on the change in NADH absorbance between two flow cells. We noted that results for patients' specimens and controls changed when the fiber optic terminations for the two LDH channel flow cells were adjusted or "peaked" at the colorimeter chopper assembly. The energy (intensity) of light reaching the flow cells was varied by adjusting the fiber optic terminations, and the absorbance readings for a series of solutions containing NADH and patients' specimens were recorded. For both flow cells, when the fiber optic terminations were adjusted to increase the zero absorbance light intensity from 20 lines to 60 lines, a significant (p less than 0.0001) proportional change was seen in the absorbance readings. Evidently the difference in absorbance between the two flow cells is related not only to the NADH concentrations but also to the difference in the light intensity at the two flow cells. Consequently, changes in the adjustment of the fiber optic terminations produce systematic changes in results for LDH in patients' sera. These systematic changes in LDH results may be minimized by maintaining equivalent settings of the fiber optic terminations for the two flow cells and by using the calibration material with an absorbance most similar to that of patients' specimens.

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.

Synthesis of Novel tricyclic pyrazolo(1,4)oxathiinopyrazines and Evaluation of Their Competency Towards the Inhibition of Lactate Dehydrogenase Activity-Inhibition of LDH Activity

Drug Research ◽  
2018 ◽  
Vol 68 (11) ◽  
pp. 653-660
Author(s):  
Prasun Mukherjee ◽  
Asish Das ◽  
Raghwendra Mishra ◽  
Shovonlal Bhowmick ◽  
Achintya Saha
Keyword(s):  
Lactate Dehydrogenase ◽  
Glucose Metabolism ◽  
Drug Development ◽  
Dehydrogenase Activity ◽  
Elemental Sulfur ◽  
Sulfur Source ◽  
One Pot ◽  
Lactate Dehydrogenase Activity ◽  
Activity Inhibition ◽  
Ldh Activity

AbstractWe have evaluated the LDH inhibitory property of novel pyrazolo[4′,3′:5,6][1,4]oxathiino[2,3-b]pyrazine derivatives which have been synthesized from easily available starting materials through a one-pot protocol that offers the use of elemental sulfur as the sulfur source. These newly synthesized compounds may aid to drug development for neoplastic and non-neoplastic diseases characterized by increased glucose metabolism. Additionally, they may act as suitable starting materials which can be further structurally modified for the development of new LDH inhibitors with higher efficacy and specificity.

scholarly journals Lactate dehydrogenase activity staining demonstrates time-dependent immune cell infiltration in human ex-vivo burn-injured skin

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Joshua Cuddihy ◽  
Gongjie Wu ◽  
Laptin Ho ◽  
Hiromi Kudo ◽  
Andreas Dannhorn ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Immune Cell ◽  
Burn Injury ◽  
Ex Vivo ◽  
Cell Types ◽  
Steady Increase ◽  
Cellular Infiltration ◽  
Lactate Dehydrogenase Activity ◽  
Burn Wounds ◽  
Ldh Activity

AbstractBurn injuries constitute one of the most serious accidental injuries. Increased metabolic rate is a hallmark feature of burn injury. Visualising lactate dehydrogenase (LDH) activity has been previously used to identify metabolic activity differences, hence cell viability and burn depth in burn skin. LDH activity was visualised in injured and uninjured skin from 38 sub-acute burn patients. LDH activity aided the identification of spatially correlating immunocompetent cells in a sub-group of six patients. Desorption Electrospray Ionisation Mass Spectrometry Imaging (DESI MSI) was used to describe relative lactate and pyruvate abundance in burned and uninjured tissue. LDH activity was significantly increased in the middle and deep regions of burnt skin compared with superficial areas in burnt skin and uninjured tissue and positively correlated with post-burn time. Regions of increased LDH activity showed high pyruvate and low lactate abundance when examined with DESI-MSI. Areas of increased LDH activity exhibited cellular infiltration, including CD3 + and CD4 + T-lymphocytes and CD68 + macrophages. Our data demonstrate a steady increase in functional LDH activity in sub-acute burn wounds linked to cellular infiltration. The cell types associated are related to tissue restructuring and inflammation. This region in burn wounds is likely the focus of dysregulated inflammation and hypermetabolism.

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