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PubMed1991

Myocardial lactate dehydrogenase and its isoenzyme activities in transplanted human hearts.

Lactate dehydrogenase and its heart (H) and muscle (M) subunit activities were studied in right ventricular endomyocardial biopsies from eight transplanted human hearts and compared with five chronically failing hearts and six normal human hearts from brain-dead liver/kidney donors. Of the 17 transplant biopsies (taken 5-95 weeks postoperatively), only two showed histologic signs of chronic rejection: They were excluded from the group analysis. A higher proportion of the M subunit of lactate dehydrogenase (M%) was found in the transplanted and the chronically failing hearts than in the normal hearts, presumably reflecting increased myocardial anaerobic glycolytic stress. In the early post-transplantation period, M% was higher in the transplanted than in the chronically failing hearts. Thereafter M% gradually fell, but had not reached normal levels 1-2 years after transplantation. During that time it was similar to the values in the chronic-failure hearts. In the two biopsies with chronic rejection, M% was nearly twice as high as in contemporaneous biopsies showing mild or no rejection. Monitoring of enzymatic adaptation from endomyocardial biopsies may be of clinical interest.

Adolescent↗
PubMed1978

Changes in the liver lactate dehydrogenase isozyme profile after induced glycogenolysis.

Treatment with cystamine, phlorrhizin or nicotinic acid, which induced liver glycogenolysis, resulted in the increase of liver lactate dehydrogenase activity. This increase was counteracted by the administration of cycloheximide or actinomycin D and coincided with the increase os isozymes 4 and 3 and the decrease of isozyme 5. The enhancement of liver lactate dehydrogenase activity and the changes observed in the isozyme profile were similar to those observed after starvation. These results suggest that the changes in the lactate dehydrogenase isozyme profile found after cystamine, phlorrhizin or nicotinic acid administration may be related to the glycogenolytic effect of these compounds. These result in an adaptation of the liver lactate dehydrogenase to gluconeogenesis.

Animals↗
PubMed1987

Progestin stimulation of lactate dehydrogenase in the human breast cancer cell line T-47D.

We have previously reported that physiological levels of progestins alone stimulate lactate dehydrogenase in a dose-responsive manner in the progesterone-receptor-rich human breast cancer cell line T-47D. Using isozyme electrophoresis, we have not found that lactate dehydrogenase isozyme 5 is the only isozyme detectable in these cells, as has been reported for other human breast cancer cells in long-term tissue culture. Upon treatment with progestins, isozyme 5 remains the only isozyme detectable. T-47D cells were plated in charcoal-stripped serum-containing medium and grown for 2 days before treatment with progestin. Lactate dehydrogenase stimulation then plateaued after around 2-3 days of treatment with progestin and was maintained until around day 5, following which a decline in enzyme activity occurred. The effect is specific for progestins, and inhibited by the anti-progestin RU-38486 (17 beta-hydroxy-11 beta-(4-dimethyl-aminophenyl-1)-17 alpha-(prop-1-ynil)-estra-4,9-dien-3-one). Experiments using actinomycin D and cycloheximide suggests that the effect is dependent on RNA and protein synthesis, respectively. Lactate dehydrogenase stimulation occurs regardless of the presence of the estrogenic pH indicator Phenol red, and of whether it was analyzed per mg DNA or per mg protein.

Breast Neoplasms↗
PubMed1979

Substrate specificity of the lactate dehydrogenase isoenzyme C4 from human spermatozoa and a possible selective assay.

The activity of lactate dehydrogenase (EC 1.1.1.27) in normal human sperm lysates and in human heart and liver homogenates was determined by using a variety of 2-oxoacids as substrates. Sperm preparations were active with pyruvate, 2-oxobutanoate, 2-oxopentanoate and 2-oxohexanoate, while heart and liver extracts utilized only pyruvate and 2-oxobutanoate. Selective staining after gel electrophoresis indicated that the fraction corresponding to lactate dehydrogenase C4, the sperm-specific isoenzyme, was responsible for the utilization of substrates with a linear chain of 3 to 6 carbon atoms. The use of 5 mM 2-oxohexanoate allowed the selective determination of isoenzyme C4 in preparations containing different lactate dehydrogenase molecular forms.

Caproates↗
PubMed2000

Macro lactate dehydrogenase in a patient with myocarditis.

Elevated level of plasma lactate dehydrogenase activity in a patient with myocarditis was found to be due to the presence of lactate dehydrogenase-immunoglobulin complexes in circulation. The complexes were demonstrated by counter-immunoelectrophoresis. In this case, three immunoglobulins (IgG, IgA and IgM) and two types of light chains (lambda and kappa) combined with lactate dehydrogenase.

Adult↗
PubMed1991

Analysis of protein loop closure. Two types of hinges produce one motion in lactate dehydrogenase.

As shown in previous crystallographic investigations, upon binding lactate and NAD, lactate dehydrogenase undergoes a large conformational change that results in a surface loop moving roughly 10 A to cover the active site. In addition, there are appreciable movements (approximately 2 A) of five helices and three other loops. We demonstrate by a new fitting procedure that the loop moves on two hinges separated by a relatively rigid type II turn. The first hinge has few steric constraints on it, and its motion can be well accounted for by large changes in two torsion angles, i.e. as in a classic hinge motion. In contrast, the second hinge, which is part of a helix connected to the end of the loop, has many more constraints on it and distributes its deformation over more torsion angles. This novel motion involves the helix stretching and splitting into alpha-helical and 3(10)-helical components and substantial side-chain repacking in the sense of "cogs hopping between grooves" at its interface with the end of a neighboring helix. The loop is stabilized by five transverse (across loop) hydrogen bonds. These are preserved, through the conformational change and through 17 lactate dehydrogenase sequences, more than the longitudinal hydrogen bonds down the sides of the loop. Through a network of contacts, many of them conserved hydrophobic residues, the motion of the loop is propagated outward to structures that have no direct contact with the ligands. These moving structures are on the surface of the protein, and the whole protein can be subdivided into concentric shells of increasing mobility.

Amino Acid Sequence↗
PubMedDate not supplied

[Effect of ammonium chloride and urea on the activity of lactate dehydrogenase. A general model of catalysis].

The dependence of structural and functional properties of lactate dehydrogenase from the pig muscle (isoenzyme M4) on pH (6.9-8.5) on the effect of different forms of non-protein nitrogen (e.g. urea and ammonium chloride) has been investigated. It was shown that Vmax changes negligibly at pH 6.9-8.5 but K(m) increase markedly with pH elevation. At the alkali value of pH pyruvate inhibition disappeared. We have found that urea and ammonium chloride at the non-saturation concentrations inhibited the activity of lactate dehydrogenase. The inhibition constants (Ki and Ka) for urea and ammonium chloride were obtained from inhibition data. When analysing works of different authors and own results we propose the general model of catalysis of lactate dehydrogenase, which includes the formation of normal enzyme-substrate complex, abortive enzyme-NAD-pyruvate complex and the effect of different effectors, including nitrogen containing substances.

Ammonium Chloride↗
PubMed1990

Gossypol modulation of mouse heart and liver lactate dehydrogenase isoenzymes as a function of gender.

Acute treatment with gossypol produced both tissue specific and sex-dependent alterations of M and H subunits of mouse lactate dehydrogenase. Gossypol induced female mouse heart cytoplasma H subunit and inhibited both enzyme subunits in the male mouse. Gossypol induced mouse liver mitochondrial lactate dehydrogenase subunit M in both sexes 50 hrs after acute drug administration while was ineffective on the testicular enzyme. Induction of hepatic lactate dehydrogenase may enhance NADH:NAD ratio, resulting in alteration of cellular redox status and reduction of NAD utilization by other dehydrogenases. The gossypol-mediated sex-dependent changes of heart lactate dehydrogenase isoenzymes may be of value in the prediction of certain aspects of gossypol toxicity.

Animals↗
PubMed1988

A re-evaluation of the molecular size of duck epsilon-crystallin and its comparison with avian lactate dehydrogenases.

A biochemical comparison of epsilon-crystallin isolated from the duck lens and lactate dehydrogenases of chicken heart has been made in order to establish the structural and functional identities of these two proteins. The native molecular weight of epsilon-crystallin was re-examined by combining sedimentation and gel-filtration data. It was found that epsilon-crystallin is 150 kDa in contrast to the 120 kDa reported previously for this crystallin. Subunit cross-linking experiments corroborated that lactate dehydrogenase and epsilon-crystallin both exist as tetramers of four identical subunits in their native quaternary structures. Amino acid compositions plus N-terminal analyses revealed no differences between the two proteins. Duck epsilon-crystallin exhibited high enzymatic activity of lactate dehydrogenases even after a long period of storage, and showed characteristic thermostability at 50 degrees C for several hours. Comparison of the enzyme activity of duck lens homogenate with those of heart, liver and muscle tissues revealed that duck lens is a much richer source than other tissues for the isolation and characterization of this important enzyme which appears also as a structural protein in the lens.

Animals↗
PubMed1963

LACTATE DEHYDROGENASE IN TESTIS: DISSOCIATION AND RECOMBINATION OF SUBUNITS.

Electrophoretic resolution of lactate dehydrogenase in mature testes from a variety of animals revealed one or more unusual isozymes in addition to the usual five forms. Dissociation of the enzyme and recombination of the polypeptide subunits led to the formation of new isozymes and to a redistribution of activity among those normally present, indicating that lactate dehydrogenase synthesis in postpubertal testis is controlled by more than two genes.

Animals↗
PubMed1978

On the localization of lactate dehydrogenase in the ovaries and reproductive tracts of rats and mice.

The localization of lactate dehydrogenase in the ovaries and reproductive tracts of rats and mice has been studied by a methodology which minimizes loss of this soluble enzyme by diffusion, and allows comment on the subunit composition of the cellular enzyme. The results differ significantly from previous data with conventional methodologies. In particular, the major localization of activity in the present study was identified in interstitial cells, and not the corpora lutea or granulosa cells; and it was noticeable that neither species exhibited massively greater expression of lactate dehydrogenase activity in the oocytes than in adjacent cell types of the reproductive tract. The goblet cells of the Fallopian tube stained intensively for activity of this enzyme. These results have been discussed in relation to the discordant data in the literature, the important role of lactate dehydrogenase in mammalian development, and the evidence for a masking of the activity of this enzyme in oocytes and pre-implantation ova.

Animals↗
PubMed1989

Identification of epsilon-crystallin from swan lens as lactate dehydrogenase.

Characterization of lens crystallins from black swan, a rare aquatic bird belonging to the family Anatidae, was carried out to search for epsilon-crystallin with lactate dehydrogenase activity. Biochemical comparison of epsilon-crystallins isolated from the swan and duck lenses plus lactate dehydrogenase of chicken heart has also been made in order to establish the structural/functional relatedness of these proteins. Amino acid analyses showed essentially similar overall compositions for these three proteins. Kinetic analysis revealed differences between avian epsilon-crystallins and the authentic heart-type lactate dehydrogenase. The swan lenses similar to duck lenses appeared to contain a thermostable epsilon-crystallin which possesses very high enzymatic activity of lactate dehydrogenase. The characterization of epsilon-crystallins from the available species of aquatic birds may provide some insights into the evolution of this unique crystallin in the Aves and their enzymatic roles inside the lens.

Amino Acids↗
PubMed2005

Activity and latent activity of lactate dehydrogenase isoenzymes from patients with disadaptation.

Spontaneous proliferation and structural and functional properties of the cell membranes were studied by measuring activity and latent activity of lactate dehydrogenase isoenzymes in peripheral blood leukocytes from patients with disadaptation at admission to the hospital and during therapy. The spectrum of lactate dehydrogenase isoenzymes in patients with disadaptation at admission did not differ from the corresponding values in the control group. Therapy was accompanied by a shift in isoenzyme spectrum of lactate dehydrogenase toward the prevalence of one isoform, which probably reflected metabolic changes in immunocytes under conditions of adaptive immune response to psychoemotional stress. Latent activity of lactate dehydrogenase isoenzymes in patients at admission was below the control. Latent enzyme activity returned to normal during therapy. The observed changes in latent enzyme activity were probably associated with recovery of structural and functional properties of leukocyte membranes.

Adaptation, Physiological↗
PubMed1980

Determination of the interaction of lactate dehydrogenase with high-molecular-weight derivatives of AMP by affinity electrophoresis.

The interaction of lactate dehydrogenase with high-molecular-weight derivatives of AMP was studied by affinity electrophoresis in an alkaline buffer system and by means of kinetic measurements. AMP was coupled to synthetic hydroxypropylmethacrylamide copolymers through glycine, 6-aminohexanoic and 12-aminododecanoic spacer arms. The values of the dissociation constants (K) of the lactate dehydrogenase isoenzymes--immobilized AMP complexes determined by affinity electrophoresis decreased with increasing length of the spacer arm. Lactate dehydrogenase was competitively inhibited by high-molecular-weight derivatives of AMP; values of the inhibition constants (Ki) also depended on the spacer arm: the longer the spacer arm the stronger was the interaction between the enzyme and the inhibitor. Ki values for high-molecular weight derivatives of AMP were lower than those obtained for free AMP.

Adenosine Monophosphate↗
PubMed1995

D175 discriminates between NADH and NADPH in the coenzyme binding site of Lactobacillus delbrueckii subsp. bulgaricus D-lactate dehydrogenase.

The NAD-dependent D-(-)-lactate dehydrogenase (D-LDH) from Lactobacillus delbrueckii subsp. bulgaricus (in short, L. bulgaricus) has been modified at position 175 by site-directed mutagenesis, changing a conserved aspartate residue into an alanine. The D175A mutant enzyme displays a 40-fold shift in coenzyme preference from NADH to NADPH. This demonstrates that D175 truly belongs to the amino acid consensus GXGXXGX(17)D (where X represents any residue) which is the signature of the coenzyme binding site of most NAD-dependent dehydrogenases.

Alanine↗
PubMed1977

Lactate dehydrogenase isoenzymes linked to beta-lipoproteins and immunoglobulin A.

A clinically asymptomatic individual had an abnormal electrophoretic pattern for lactate dehydrogenase, seven isoenzyme bands being present. This atypical pattern was a result of an interaction of lactate dehydrogenase with immunoglobulin A and beta-lipoprotein. Lactate dehydrogenase enzymes LD2 and LD3 were the isoenzymes responsible for the formation of the complexes.

Adult↗
PubMed1981

The chemical reactivity of the histidine-195 residue in lactate dehydrogenase thiomethylated at the cysteine-165 residue.

The specific thiomethylation of cysteine-165 (insertion of a methylthio group, CH3-S-) in pig heart lactate dehydrogenase results in a decreased affinity for carbonyl ligands that is accompanied by a decreased nucleophilic reaction of histidine-195 with diethyl pyrocarbonate. The rate constants at 10 degrees C for the modification of native and thiomethylated lactate dehydrogenase by diethyl pyrocarbonate were 173 M-1 . s-1 and 8.7 M-1 . s-1 respectively. It was found that 0.86 +/- 0.07 histidine residue per subunit reacted with diethyl pyrocarbonate in thiomethylated lactate dehydrogenase. This reaction was not affected in the enzyme-NADH binary complex, but was diminished in the enzyme-NADH-oxamate ternary complex. In the enzyme-NADH complex the reaction of diethyl pyrocarbonate was controlled by two groups with pKa 6.8 and 7.9. The decreased reactivity of histidine-195 was selective in thiomethylated lactate dehydrogenase, since the reactivity of arginine and/or lysine residues was enhanced.

Binding Sites↗
PubMed1985

Mechanism and specificity of reconstitution of dimeric lactate dehydrogenase from Limulus polyphemus.

D-Lactate dehydrogenase (EC 1.1.1.28) from Limulus polyphemus is a homodimer which is composed of identical subunits of Mr = 35 000. The enzyme may be reversibly denatured and dissociated at acid pH or in 6M guanidine X HCl. The sigmoidal time course of reactivation obeys a consecutive uni-bimolecular mechanism with k1 = 6 X 10(-4) S-1 and k2 = 1.3 X 10(-4) M-1 S-1 (20 degrees C) as first- and second-order rate constants. Cross-linking experiments with glutaraldehyde prove that reactivation and dimer formation run parallel. Joint "synchronous" reconstitution of the enzyme with dimeric porcine mitochondrial malate dehydrogenase (after denaturation in 6M guanidine X HCl) does not yield active hybrids. The unchanged kinetics of reactivation in the absence and presence of the prospective partner of hybridization prove that inactive hybrid intermediates may also be excluded. The absence of hybrids upon synchronous reconstitution of the two closely related dimeric NAD-dependent dehydrogenases clearly suggests that the assembly of nascent oligomeric proteins must be highly specific.

Animals↗