The lactate dehydrogenases of the chicken: estimation and repression during the development of lymphoid and other tissues

1968 ◽  
Vol 46 (6) ◽  
pp. 555-562 ◽  
Author(s):  
G. A. Schultz ◽  
R. F. Ruth
Keyword(s):  
Lactate Dehydrogenase ◽  
Total Activity ◽  
Bursa Of Fabricius ◽  
Ldh Activity ◽  
Great Excess ◽  
Lactate Dehydrogenases

Eight organs of 148 embryos, chicks, and chickens were used for estimations of total lactate dehydrogenase (LDH) activity and its distribution among the five principal isoenzymes, LDH-1 to LDH-5. Heart and liver have the greatest total activities, and brain, bursa of Fabricius, and thymus have the least. During development, total activities may follow similar trends. The heart parallels the liver, kidney and spleen parallel gastrocnemius, and brain and bursa parallel thymus. The distribution of activity among the isoenzymes is independent of the parallels in total activity: the heart acquires a great excess of LDH-1 relative to LDH-5, the gastrocnemius acquires an excess of LDH-5 relative to LDH-1, and the six other organs maintain an excess of LDH-1. The separate activities of LDH-4 and LDH-5 may remain very low, as in brain, bursa, and thymus. The total LDH activity of lymphoid and other organs may be reduced by 19-nortestosterone, an androgen which suppresses lymphopoiesis. The effect of this androgen on the LDH activity of the bursa may be detected before gross effects are obvious.

A search for the best buffer to use in assaying human lactate dehydrogenase with the lactate-to-pyruvate reaction.

1976 ◽  
Vol 22 (11) ◽  
pp. 1872-1875 ◽  
Author(s):  
S N Buhl ◽  
K Y Jackson ◽  
R Lubinski ◽  
R E Vanderlinde
Keyword(s):  
Lactate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Total Activity ◽  
Buffering Capacity ◽  
Buffer Concentration ◽  
Commercial Preparation ◽  
Lactate Dehydrogenases

Abstract Highly purified human lactate dehydrogenases I and V were assayed in 17 different buffers, at a variety of reaction pH's. Diethanolamine and 2-amino-2-methyl-1,3-propanediol provided the best measurements of the enzyme, assayed lactate-to-pyruvate. However, the commercial preparation of 2-amino-2-methyl-1,3-propanediol contained insoluble matter and was relatively expensive. All of the four buffers nowmost commonly used were found to present difficulties. Glycine and pyrophosphate were inhibotory tolactate dehydrogenase activity with increasing buffer concentration. 2-Amino-2-methyl-1-propanol had three major disadvantages: it is chemically unstable during reagent preparation; activity is dependent on buffer concentration; and the pH optima for isoenzymes I and V are vastly different. The pKa of tris(hydroxymethyl)aminomethane is 8.0 at 30 degrees C, whereas to measure total activity the reaction pH should be greater than 8.5; thus tris(hydroxymethyl)aminomethane has limited buffering capacity at the reaction pH.

scholarly journals Lactate Dehydrogenases as Metabolic Links between Tumor and Stroma in the Tumor Microenvironment

Cancers ◽  
2019 ◽  
Vol 11 (6) ◽  
pp. 750 ◽  
Author(s):  
Deepshikha Mishra ◽  
Debabrata Banerjee
Keyword(s):  
Lactate Dehydrogenase ◽  
Tumor Microenvironment ◽  
Cancer Cells ◽  
Drug Targets ◽  
Cancer Metabolism ◽  
Tumor Stroma ◽  
Metabolic Enzyme ◽  
Ldh Activity ◽  
Lactate Dehydrogenases

Cancer is a metabolic disease in which abnormally proliferating cancer cells rewire metabolic pathways in the tumor microenvironment (TME). Molecular reprogramming in the TME helps cancer cells to fulfill elevated metabolic demands for bioenergetics and cellular biosynthesis. One of the ways through which cancer cell achieve this is by regulating the expression of metabolic enzymes. Lactate dehydrogenase (LDH) is the primary metabolic enzyme that converts pyruvate to lactate and vice versa. LDH also plays a significant role in regulating nutrient exchange between tumor and stroma. Thus, targeting human lactate dehydrogenase for treating advanced carcinomas may be of benefit. LDHA and LDHB, two isoenzymes of LDH, participate in tumor stroma metabolic interaction and exchange of metabolic fuel and thus could serve as potential anticancer drug targets. This article reviews recent research discussing the roles of lactate dehydrogenase in cancer metabolism. As molecular regulation of LDHA and LDHB in different cancer remains obscure, we also review signaling pathways regulating LDHA and LDHB expression. We highlight on the role of small molecule inhibitors in targeting LDH activity and we emphasize the development of safer and more effective LDH inhibitors. We trust that this review will also generate interest in designing combination therapies based on LDH inhibition, with LDHA being targeted in tumors and LDHB in stromal cells for better treatment outcome.

Leukocyte Lactate Dehydrogenase in Bacterial Meningitis

PEDIATRICS ◽  
1974 ◽  
Vol 54 (1) ◽  
pp. 27-33
Author(s):  
David W. Powers ◽  
Elia M. Ayoub
Keyword(s):  
Lactate Dehydrogenase ◽  
Bacterial Meningitis ◽  
Newborn Infants ◽  
Neonatal Meningitis ◽  
Subdural Effusion ◽  
Upper Limit ◽  
Ldh Activity ◽  
Initiation Of Therapy ◽  
Peripheral Leukocytes ◽  
Normal Controls

Lactate dehydrogenase (LDH) was assayed in peripheral leukocytes of 32 children with bacterial meningitis, nine children with nonbacterial meningitis, and 24 age-matched, healthy controls. Leukocyte LDH activity in patients with bacterial meningitis was significantly higher than in patients with nonbacterial meningitis (p < 0.01) and normal controls (p < 0.001). Eighty-eight percent of the patients with bacterial meningitis had leukocyte LDH values exceeding, 150 units/106 WBC, the upper limit of normal value for controls. Nitroblue tetrazolium (NBT) dye tests performed on 23 patients with bacterial meningitis were elevated in ten patients (43%). The elevation of leukocyte LDH activity in patients with bacterial meningitis appears to be independent of the number of circulating granulocytes or the presence of bacteremia. A major factor which appeared to influence the leukocyte LDH activity was the duration of adequate antibiotic therapy. Sequential determinations showed a return of the LDH values to normal approximately ten days after the initiation of therapy. A rise in leukocyte LDH was encountered in two patients with subdural effusion. The finding of significantly elevated leukocyte LDH values in three newborn infants with neonatal meningitis and sepsis suggests that this test may be of value in the diagnosis of neonatal sepsis.

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 In Vivo Enzymes Activities of Some Ru(II) Compounds with N-Alkylphenothiazines

2016 ◽  
Vol 66 (4) ◽  
pp. 497-508
Author(s):  
P. Milena Krstić ◽  
Z. Sunčica Borozan ◽  
P. Sofija Sovilj ◽  
R. Sanja Grgurić-Šipka ◽  
M. Jelena Oljarević
Keyword(s):  
Antioxidant Activity ◽  
Enzyme Activity ◽  
Lactate Dehydrogenase ◽  
Normal Activity ◽  
Protective Effects ◽  
Toxic Compounds ◽  
Physiological Conditions ◽  
Positive Effects ◽  
Ldh Activity

Abstract The purpose of the present study was to investigate and compare the effects of two ruthenium complexes with trifluoperazine on acethylcholinesterase enzyme activity and lactate dehydrogenase levels in vivo under physiological conditions in rats blood. Complexes 1 and 2 showed positive effects on acethylcholinesterase at all doses and did not disturb its normal activity. Total LDH activity was inhibited in the presence of both complexes, but Ru(II) complexes showed different effects on the activity of LDH isoenzymes. The activities of LDH1 and LDH2 isoenzymes were decreased in all applied doses of the complex 2, while the activity of LDH2 reduced using complex 1 in the same doses. Results of the present study suggest the neuro- and cardio protective potential of oral administration of complexes 1 and 2, as non-toxic compounds under physiological conditions. These protective effects are the result of their potent antioxidant activity.

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.

Colorectal Cancer: Lactate Dehydrogenase (LDH) Activity as a Prognostic Marker

2009 ◽  
pp. 241-253 ◽  
Author(s):  
Michael I. Koukourakis ◽  
Alexandra Giatromanolaki ◽  
Efthimios Sivridis
Keyword(s):  
Colorectal Cancer ◽  
Lactate Dehydrogenase ◽  
Prognostic Marker ◽  
Ldh Activity
Sign in / Sign up

Export Citation Format

Share Document