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.

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%).

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.

Use of purified lyophilized human lactate dehydrogenase isoenzyme 5 in a study of measuring lactate dehydrogenase activity.

1989 ◽  
Vol 35 (8) ◽  
pp. 1774-1776 ◽  
Author(s):  
D A Smith ◽  
G C Moses ◽  
A R Henderson
Keyword(s):  
Lactate Dehydrogenase ◽  
Half Life ◽  
Specific Activity ◽  
Lactate Dehydrogenase Activity ◽  
Bovine Albumin ◽  
First Order ◽  
First Order Kinetics ◽  
The Stability ◽  
Lactate Dehydrogenase Isoenzymes ◽  
Excellent Stability

Abstract We examined the stability of human lactate dehydrogenase (EC 1.1.1.27) isoenzyme 5--purified to a specific activity of about 400 kU/g--when lyophilized in a buffered, stabilized matrix of bovine albumin. This isoenzyme was prepared with a final activity of about 500 U/L and stored at -20, 4, 20, 37, and 56 degrees C for as long as six months. This isoenzyme decayed with approximate first-order kinetics, with an estimated half-life at -20 degrees C of about 475 years. Stability of reconstituted samples stored at 20 or 4 degrees C was poor, suggesting that the reconstituted material should be used without delay; material stored at -20 degrees C showed excellent stability for 15 days. We propose that such preparations might be further investigated as standards for use in electrophoresis of lactate dehydrogenase isoenzymes.

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 Hereditary lactate dehydrogenase A-subunit deficiency as cause of early postimplantation death of homozygotes in Mus musculus.

Genetics ◽  
1992 ◽  
Vol 131 (2) ◽  
pp. 413-421 ◽  
Author(s):  
S Merkle ◽  
J Favor ◽  
J Graw ◽  
S Hornhardt ◽  
W Pretsch
Keyword(s):  
Lactate Dehydrogenase ◽  
Gamma Ray ◽  
Specific Activity ◽  
Physicochemical Characteristics ◽  
Metabolic Energy ◽  
Null Alleles ◽  
Wild Type ◽  
Ldh Activity ◽  
A Subunit

Abstract Two ethylnitrosourea-induced heterozygous mouse mutants with approximately 58 and 50% of wild-type lactate dehydrogenase (LDH) activity and a gamma-ray-induced heterozygous mutant with 50% of wild-type LDH activity in blood, liver and spleen (expressing predominantly the Ldh-1 gene) were recovered in mutagenicity experiments following spermatogonial treatment. Physiological and genetic studies revealed no indications for differences in fertility as well as hematological or other physiological traits between heterozygotes of each mutant line and wild types. This suggests that neither the mutations in the heterozygous state per se nor the resulting approximate 42 to 50% LDH deficiency affect metabolism and fitness. Physicochemical and immunological studies clearly demonstrated that the two mutations with 50% deficiency in heterozygotes result from null alleles of the Ldh-1 structural locus, generating neither enzyme activity nor immunological cross-reacting material. In contrast, the heterozygous mutant with approximately 58% of normal blood LDH activity was shown to be due to a Ldh-1 allele creating protein subunits, which in random assortment with wild-type subunits in vivo exhibit a reduced specific activity and further alterations of kinetic and physicochemical characteristics. All the mutations in the homozygous state were found to be lethal at an early postimplantation stage of embryonic development, probably due to a block of glycolysis with the corresponding loss of the main source of metabolic energy during this ontogenetic stage. The distinct physiological consequences of the total absence of a functioning LDH-A subunit in mice and humans are discussed.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Ovarian Masses-Applicable IOTA ADNEX Model versus Morphological Findings for Accurate Diagnosis and Treatment

2021 ◽  
Vol 11 (22) ◽  
pp. 10789
Author(s):  
Tudor Butureanu ◽  
Demetra Socolov ◽  
Daniela Roxana Matasariu ◽  
Alexandra Ursache ◽  
Ana-Maria Apetrei ◽  
...  
Keyword(s):  
At Risk ◽  
Surgical Treatment ◽  
Ovarian Tumor ◽  
Malignant Tumors ◽  
Benign Tumors ◽  
Adnexal Masses ◽  
Borderline Tumors ◽  
Benign Ovarian Tumor ◽  
Significant Difference ◽  
Ovarian Masses

A common problem in gynecological practice is the differential diagnosis of the ovarian masses. The clinician must apply the IOTA (International Ovarian Tumor Analysis) ADNEX (Assessment of Different Neoplasia in the Adnexa) model criteria to evaluate the risk of benign, borderline or malignant tumors. The aim of this study was to verify if the IOTA ADNEX model is a practical tool to be used before surgery and if there is a significant difference between IOTA ADNEX criteria and histological findings. A prospective single center study was performed between January 2017 and December 2019 in Obstetrics and Gynecology Hospital “Cuza-Voda”, Iasi, Romania. The study included 230 patients between 17 and 74 years old diagnosed with persistent adnexal masses. We applied the IOTA ADNEX model protocol predicting the risk of benign, borderline or malignant masses. The golden standard remains the histological diagnosis of the surgically removed mass. The patients that had been diagnosed using ultrasonography with persistent adnexal masses between 30 and 291 mm were operated on in our clinic. In our study. the majority of patients had benign ovarian tumor mass, these being 223 (96.96%) patients, from whom, according to IOTA ADNEX protocol, the correspondence was: 91.8–99.7% at risk of benign tumors, 0.3–4.5% at risk of borderline tumors and 0.3–8.2% at risk of malignant masses. Unexpected findings were obtained from the malignant group that included five patients (2.17%) with the following correspondence: 96.1–99% at risk of benign tumors, 0.6–2.4% at risk of borderline tumors and 1–3.9% at risk of malignant masses. After applying the IOTA ADNEX model criteria, the patients with a suspicion of malignant disease were correctly guided towards surgical treatment in an oncological center. In our hospital, surgical treatment was only proposed to those patients with high suspicion of benign masses.

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