Lactate dehydrogenase and its isoenzymes in human umbilical cord tissue]

Study on umbilical cord tissue, completely bloodless, for determination of lactate deshydrogenase activity and its distribution among the five iso-enzymes. Comparison with placenta, amniotic fluid, serums of blood of cord and of mother. Cord tissue is very active (about 360 muKatals, in average) and it is a similar result in placenta (as it is possibly bloodless). Blood serum of cord is more active than amniotic fluid, which is more active than maternal serum, but they are 80 to 200 times less active than cord tissue. After electrophoresis, a very large predominance of the slow iso-enzymes L.D.H. 4--5 is found in cord tissue (72%), amniotic fluid (67%) and placenta (56%), whereas the fast iso-enzymes L.D.H. 1--2 are predominant in the serums of cord blood and of mother. These data indicate an intense metabolic activity in the cord tissue, which has also an high level of lactate, and this seems related to the foetal metabolism for anaerobic glycolysis in oxygen weakly provided tissues.     

Lactate dehydrogenase isoenzymes in diabetic patients

Lactate dehydrogenase (LDH) isoenzyme profiles in human platelets and the sera of patients with type I and II diabetes mellitus and vascular complications, as well as normal subjects were measured utilizing a recently established, modified micromethod. LDH-3 was the predominating species in platelets (37.5 +/- 3.0%), with LDH-2, 1, 4 and 5 following in decreasing order of concentration. The LDH-3/LDH-4 ratio in platelets varied from 6.2 to 1.38. Type I and type II diabetic patients with vascular complications showed a significantly higher ratio for LDH-3/LDH-4 (3.99 +/- 1.20 for DM I, 2.16 +/- 0.25 for DM II patients) than the mean ratio for normal subjects (1.14 +/- 0.08). This platelet-specific LDH isoenzyme pattern may be the result of frequent in vivo platelet-vessel wall interactions in the diabetic patients whose platelets are known to be hyperaggregable in in vitro test systems. Since non-diabetic patients patients with vascular complications also displayed a similarly elevated LDH-3/LDH-4 ratio, a wider classification is preferable, although the measurement of the LDH isoenzyme pattern will be helpful in assessing diabetic vascular complications.     

Lactate dehydrogenase changes following several cardiac hypertrophic stresses.

The effects of four different cardiac hypertrophic stresses on cardiac lactate dehydrogenase (LDH) isozyme composition and activity were examined. Altitude-induced right ventricular hypertrophy was accompanied by an increase of 10% in the M subunit of LDH in right ventricle, left ventricle, and atria. Left ventricular hypertrophy induced by aortic stenosis also produced isozyme changes in the ventricles, but of only half the magnitude. Biventricular hypertrophy, induced by running or swimming, was accompanied by 4-5% increases in M LDH in the ventricles only. We conclude that changes in LDH activity are directly related to changes in the M subunit in all three portions of the heart. No changes in H subunit were noted under any of the stresses. It appears that the magnitude of changes in cardiac LDH isozyme composition are only marginally related to extent of hypertrophy.     

Lactate dehydrogenase isoenzymes of human semen

1. A lactate dehydrogenase isoenzyme present in human spermatozoa and semen was isolated and characterized biochemically in term of its pH for optimum activity and by means of K(m) values for lactate, NAD(+) and NAD analogues. The results were compared with those obtained with the human heart-type and the liver-type lactate dehydrogenase isoenzymes. 2. The enzyme was characterized by its resistance to digestion with different proteolytic enzymes. The time for 50% digestion in terms of residual dehydrogenase activity was compared with times obtained for the H(4)- and M(4)-types.     

Lactate dehydrogenase isozymes in type I,IIA and IIB fibres of rabbit skeletal muscles

Summary Lactate dehydrogenase (LDH) isozyme patterns were analysed by polyacrylamide (PAA) slab gel electrophoresis in extracts prepared from various rabbit skeletal muscles of defined fibre composition and by PAA microelectrophoresis of microdissected, histochemically typed single muscle fibres. The results obtained by electrophoresis of whole muscle extracts generally agreed with the data obtained from single fibre electrophoresis, i.e. the LDH isozyme pattern corresponded to that of the predominant fibre type. Type I Fibres from soleus and semitendinosus muscles were characterized by a unique pattern of all 5 LDH isozymes with a predominance of LDH-1, 2 and 3. The major fraction (80%) of the type II fibres from extensor digitorum longus and tibialis anterior muscles contained only LDH-5 (M₄). About 20% of the type II fibres contained in addition to LDH-5 small amounts of LDH-4 and LDH-3. The fraction of fibres containing LDH-5, LDH-4, and LDH-3 was similar (ca. 20%) in the histochemically defined IIA and IIB subpopulations In view of the fact that the major fractions of rabbit IIB fibres display low and of IIA fibres high aerobic oxidative capacities (Reichmann and Pette 1982), these data indicate that the expression of the H-subunit of LDH is not correlated with the aerobic-oxidative capacity of the fibre. It also appears not to be correlated with the presence of different myosin isoforms in IIA and IIB fibres.     

Lactate dehydrogenase isoenzymes of sperm cells and testes

1. The kinetic and metabolic properties of lactate dehydrogenase isoenzyme LDH_x from human sperm cells and rat testes were studied. 2. LDH_x shows a sensitivity to inhibition by stilboestrol diphosphate, urea and guanidinium chloride different from that of the LDH-H₄ and LDH-M₄ isoenzymes. 3. About 10 and 20% of the total lactate dehydrogenase activity of testes and sperm cells respectively were associated with particulate fractions. In sperm cells 11% was localized in the middle piece and 18·8% in the head fraction. LDH_x was found in all particulate fractions of sperm cells. The middle piece contained 41·0% of total LDH_x activity and showed high succinate dehydrogenase activity. 5. The pH-dependence of lactate/pyruvate and NAD⁺/NADH concentration ratios were estimated. Lactate dehydrogenase in sperm cells has maximal activity with NADH as coenzyme at pH7·5 and with NADPH as coenzyme at pH6·0. At pH6·0 a 10% greater oxidation of NADPH than of NADH was found. At acid pH lactate hydrogenase may function as an enzyme bringing about transhydrogenation from NADPH to NAD⁺. 6. In agreement with the stoicheiometry of the lactate de- hydrogenase reaction, the lactate/pyruvate concentration ratio decreased with increasing pH. 7. The lactate/pyruvate and NAD⁺/NADH concentration ratios were estimated with glucose, fructose and sorbitol as substrates and as a function of time after addition of these substrates. During a 20min. period after the addition of the substrates, changes in lactate/pyruvate and NAD⁺/NADH concentration ratios were noticed. Increasing concentration of the substrates mentioned gave rise to asymptotic increases in lactate and pyruvate. 8. Sorbitol did not act as a substrate for LDH_x. 9. The findings described are consistent with the idea that LDH_x is different from other known lactate dehydrogenase isoenzymes, but that it has a metabolic function similar to that of the isoenzymes of other tissues.     

Lactate dehydrogenase isoenzymes in cerebral cortex of young rats undernourished since birth]

The developmental profile of the isoenzymes of lacticodehydrogenase of cerebral cortex, investigated by starch gel electrophoresis, is not retarded during neo and post-natal undernutrition, although hypothyroidism is known to do so.     

Lactate dehydrogenase isoenzymes in benign and malignant prostatic tissues

84 prostatic tissue specimens consisted of 62 benign hyperplasias and 22 carcinomas have been studied regarding Lactate dehydrogenase isoenzymes pattern. A consistent and definite shift of the LDH5 : LDH1 ratio has been found in carcinomas respect to benign hyperplasias.     

Lactate dehydrogenase isoenzymes are present in matrix vesicles

Matrix vesicles were isolated from epiphyseal growth plates of young rabbits. Lactate dehydrogenase activity was detected in the isolated matrix vesicles only in the presence of detergents, suggesting that NADH, the cofactor for the assay, does not penetrate the membrane of matrix vesicles. In contrast, the activity of alkaline phosphatase, a marker enzyme of the outer surface of matrix vesicles, was detected in the matrix vesicles using p-nitrophenyl phosphate as the substrate both in the presence and absence of detergents. Lactate dehydrogenase activity was detected only in the cytosol of chondrocytes of the epiphyseal growth plates but not in other subcellular fractions, showing that lactate dehydrogenase is not from the plasma membrane and membranes of intracellular organelles of chondrocytes. The isolated matrix vesicles contained all five lactate dehydrogenase isoenzymes but did not possess other cytosolic enzymes. These results show that lactate dehydrogenase is located in the matrix vesicles and suggest the presence of a mechanism for the specific uptake of cytosolic lactate dehydrogenase and the possibility of enzymatic quantification of the matrix vesicles at various calcification sites.     

Lactate dehydrogenase isoenzymes in loach (Misgurnus fossilis) development

Isoenzyme patterns of lactatedehydrogenase (LDH, EC 1.1.1.27) were determined in the loach (Misgurnus fossilis) oocytes, unfertilized eggs, developing embryos and larvae, and the sensitivity of the isoenzymes to the effect of AgNO3, p-chlormercurybenzoate and high temperature were investigated. The presence of 4 phenotypes of LDH patterns which differed in the isozymes number, in their relative activity, in electrophoretic mobility in the polyacrylamide gel columnes and in the frequency of occurence in different populations of the investigated species is demonstrated. Before the hatching stage there appeared a new isozyme which was completely inhibited by AgNO3 and had the same electrophoretic mobility in all LDH phenotypes. During the larvae development the content of this LDH isozyme increased. Some isozymes, especially those which had low anodic mobility and decreased in their relative quantity, disappeared during the development of embryos and larvae, p-Chlormercurybenzoate in the concentration 1 mM and heating at 70 degrees C during 20 minutes did not significantly affect LDH activities in the loach eggs, embryos and larvae.