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PubMed1997

Amperometric lactate oxidase catheter for real-time lactate monitoring based on thin film technology.

An amperometric lactate oxidase catheter has been developed for in vivo application to real-time lactate monitoring. The electrochemical behaviour of the 1 x 3 mm Pt-Ag/AgCl thin film electrode is not significantly influenced by lactate oxidase-polyurethane covering. Gamma-irradiation (25 kGy) is suitable for the sterilization procedure. The final lactate catheter is characterized by a linear concentration range between 0.5 and 20 mmol/l lactate with a sensitivity around 2 nA mmol-1 l-1 lactate. The accuracy is demonstrated by the measurement of control sera. Both physiological and pathological materials correlate well with the declared values. The dry stored lactate catheter needs about 10 min for hydration and is characterized by response times t98% of less than 2 min. Ex vivo whole blood measurements using the lactate catheter (y) give a correlation with the BIOSEN Med L (x) of y = (1.010x + 0.513) mmol/l (r = 0.9748). Lactate values obtained by continuous catheter operation ex vivo correlate well with those obtained by BIOSEN Med L. First subcutaneous implantation (dog) underlines the characteristics obtained ex vivo: after 30 min hydration the lactate catheter follows the lactate concentration measured ex vivo with samples from the leg vein by BIOSEN Med L.

Animals↗
PubMed2000

In a medium containing glucose, lactate carbon is incorporated by gonococci predominantly into fatty acids and glucose carbon incorporation is increased: implications regarding lactate stimulation of metabolism.

The reason for stimulation by lactate of metabolism of gonococci growing in a medium containing glucose, which enhances pathogenicity by increasing growth rate, lipopolysaccharide (LPS) synthesis and protein formation, has been investigated. Tricine dodecylpolyacrylamide gel electrophoresis (SDS-PAGE) and thin layer chromatography (TLC) on homogenates of gonococci grown in this medium with [14C]lactate showed that lactate carbon was preferentially incorporated into lipid and LPS. Nuclear magnetic resonance (NMR) spectroscopy on lipid extracted from gonococci grown in the glucose containing medium with [13C]lactate showed that lactate carbon was incorporated into fatty acid moieties and not into ethanolamine or glycerol moieties. In contrast, NMR on lipid from gonococci grown with [13C]glucose indicated glucose carbon in both moieties. When unlabelled lactate was added, lipid synthesis from [l3C]glucose was stimulated and small amounts of different fatty acids were formed. The NMR data shows that gluconeogenesis from lactate carbon does not occur in the presence of glucose, suggesting that lactate is used solely for rapid production, via pyruvate, of acetyl CoA, the precursor not only for fatty acid synthesis but also for the constituents and products of the citric acid cycle, including ATP. The rapid formation of a high level of acetyl CoA is the probable reason for the stimulation of metabolism and oxygen uptake by lactate. 14C label on LPS was detected in its fatty acids. Most proteins that stained with silver in tricine SDS-PAGE were not significantly labelled by [14C]lactate in the glucose-containing medium. Two of three appreciably labelled proteins were identified by N-terminal sequencing as GroEL and porin 1B, and one of the two less labelled proteins was similar to peroxiredoxin type proteins. There were no signs of specific induction of these proteins by lactate and their labelling was consistent with fatty acids in attached lipid.

Bacterial Proteins↗
PubMed1989

Effects of lactate on pancreatic islets. Lactate efflux as a possible determinant of islet-cell depolarization by glucose.

The secretion of insulin from perifused rat pancreatic islets was stimulated by raising the glucose concentration from 5.6 to 20 mM or by exposure to tolbutamide. The addition of sodium lactate (40 mM) to islets perifused in the presence of glucose (5.6 mM) resulted in a small, transient, rise in the rate of secretion. The subsequent removal of lactate, but not glucose or tolbutamide, from the perifusate produced a dramatic potentiation of insulin release. The rate of efflux of 45Ca2+ was also increased when islets were exposed to a high concentration of glucose or lactate or to tolbutamide, and again subsequently upon withdrawal of lactate. Efflux of 86Rb+ was modestly inhibited upon addition of lactate and markedly enhanced by the subsequent withdrawal of lactate from islets. The output of [14C]lactate from islets incubated in the presence of [U-14C]glucose increased linearly with increasing concentrations of glucose (1-25 mM). It is proposed that the activation of islets by the addition or withdrawal of lactate is not due to increased oxidative flux, but occurs as a result of the electrogenic passage of lactate ions across the plasma membrane, resulting in islet-cell depolarization, Ca2+ entry and insulin secretion. The production of lactate via the glycolytic pathway, and the subsequent efflux of lactate from the islet cells with concomitant exchange of H+ for Na+, could be a major determinant of depolarization and hence insulin secretion, in response to glucose.

Animals↗
PubMed1992

Metabolism of pregnant-lactating rats is adapted to pregnancy rather than to lactation.

In pregnant-lactating rats implantation was induced on day 4 of lactation so that, as an exception, lactation coincided with the period of high fetal growth. The already present suckling litters of these animals lagged behind in growth, but the "second" litters were at birth normal in size and weight. Such pregnant-lactating rats were tested in vivo with intravenous glucose loads and compared with cyclic and lactating rats. Glucose tolerance was unaffected by the reproductive state. Pregnant-lactating rats showed, just as during their first pregnancy, low basal glucose levels. Their basal insulin levels and insulin responses, however, were decreased in comparison with the first pregnancy and resembled those of lactating rats. This may be due to an increased insulin turnover, because in vitro insulin responsiveness and insulin content of both "pregnant-lactating" and "pregnant" islets were increased in comparison with "cyclic" and "lactating" islets. It was concluded that the metabolism of pregnant-lactating rats is adapted to the pregnant rather than to the lactational state.

Adaptation, Physiological↗
PubMed1985

Lactate, pyruvate, and lactate-to-pyruvate ratio during exercise and recovery.

The pattern of lactate increase and its relation to pyruvate and lactate-to-pyruvate (L/P) ratio were studied during exercise and early recovery in 10 normal subjects for incremental exercise on a cycle ergometer. Gas exchange was measured breath by breath. Lactate and pyruvate were measured by enzymatic techniques. Lactate and log lactate changed only slightly at low levels of O2 uptake (VO2) but both began to abruptly increase at approximately 40-55% of the maximal VO2. However, the point of abrupt increase in pyruvate occurred at higher work rates and the rate of increase was not as great as that for lactate. Thus L/P ratio increased at the same VO2 as the log lactate increase. Following the exercise, pyruvate continued to increase steeply for at least the first 5 recovery min, whereas at 2 min lactate increased only slightly or decreased. Thus arterial L/P ratio reversed its direction of change and decreased toward the resting value by 2 min of recovery. Lactate, as well as L/P ratios, decreased in all subjects by 5 min. This study demonstrates that lactate and pyruvate concentrations increase slightly at low levels of exercise without a change in L/P ratio until a threshold work rate at which lactate abruptly increases without pyruvate. The resulting increase in L/P ratio is progressive as work rate is incremented and abruptly reverses when exercise stops.

Adult↗
PubMed2004

Diurnal rhythm of cerebrospinal fluid and plasma leptin levels related to feeding in non-lactating and lactating rats.

Leptin suppresses food intake and increases energy expenditure in the hypothalamus. Rats consume most of their daily food intake during the dark phase of the diurnal cycle. Lactating rats have increased food intake, but the involvement of leptin in the regulation of food intake in this physiological condition is not well understood. The present experiment was carried out to determine the circadian pattern of leptin concentrations in plasma and cerebrospinal fluid (CSF) in relation to the feeding behavior of non-lactating and lactating rats. Female rats were maintained on a controlled lighting schedule (lights on between 0600 and 1800 h) and the food intake of lactating rats was two- or threefold higher than that of non-lactating rats. In both groups, food intake was three times greater in the dark phase (P<0.01) compared with the light phase. The plasma concentrations of leptin were lower (P<0.01) in lactating rats than non-lactating rats in both light and dark phases, but there were no differences in plasma leptin levels between light and dark phases. In contrast, and in both groups, the leptin concentrations in CSF were lower (P<0.01) in the dark phase than in the light phase. Leptin levels in CSF were lower (P<0.01) in lactating rats than in non-lactating rats. We conclude that a diurnal pattern of leptin levels within the brain (but not in plasma) reflects characteristics of feeding behavior in lactating and non-lactating rats.

Animals↗
PubMed2000

Impaired expression of the uncoupling protein-3 gene in skeletal muscle during lactation: fibrates and troglitazone reverse lactation-induced downregulation of the uncoupling protein-3 gene.

The expression of uncoupling protein (UCP)-3 mRNA in skeletal muscle is dramatically reduced during lactation in mice. The reduction in UCP-3 mRNA levels lowers the amount of the UCP-3 protein in skeletal muscle mitochondria during lactation. Spontaneous or abrupt weaning reverses the downregulation of the UCP-3 mRNA but not the reduction in UCP-3 protein levels. In lactating and virgin mice, however, fasting increases UCP-3 mRNA levels. Changes in UCP-3 mRNA occur in parallel with modifications in the levels of free fatty acids, which are reduced in lactation and are upregulated due to weaning or fasting. Modifications in the energy nutritional stress of lactating dams achieved by manipulating litter sizes do not influence UCP-3 mRNA levels in skeletal muscle. Conversely, when mice are fed a high-fat diet after parturition, the downregulation of UCP-3 mRNA and UCP-3 protein levels due to lactation is partially reversed, as is the reduction in serum free fatty acid levels. Treatment of lactating mice with a single injection of bezafibrate, an activator of the peroxisome proliferator-activated receptor (PPAR), raises UCP-3 mRNA in skeletal muscle to levels similar to those in virgin mice. 4-chloro-6-[(2,3-xylidine)-pirimidinylthio] acetic acid (WY-14,643), a specific ligand of the PPAR-alpha subtype, causes the most dramatic increase in UCP-3 mRNA, whereas troglitazone, a specific activator of PPAR-gamma, also significantly increases UCP-3 mRNA abundance in skeletal muscle of lactating mice. However, in virgin mice, bezafibrate and WY-14,643 do not significantly affect UCP-3 mRNA expression, whereas troglitazone is at least as effective as it is in lactating dams. It is proposed that the UCP-3 gene is regulated in skeletal muscle during lactation in response to changes in circulating free fatty acids by mechanisms involving activation of PPARs. The impaired expression of the UCP-3 gene is consistent with the involvement of UCP-3 gene regulation in the reduction of the use of fatty acids as fuel by the skeletal muscle and in impaired adaptative thermogenesis, both of which are major metabolic adaptations that occur during lactation.

Animals↗
PubMed1985

Effect of bull selection for somatic cell count in first lactation on cell counts and pathogens in later lactations.

Somatic cell counts were measured one time on Meuse-Rhine-Ijssel cattle in The Netherlands. Experiment 1 involved 1,741 first lactation daughters of 31 bulls. Eleven bulls with daughters with either high or low average cell count were selected for further study of their daughters in third and fourth lactation. Cell counts and bacteriological tests were performed on 684 of the older daughters. A second experiment was conducted to measure daughters in second lactation and to obtain additional daughters in first lactation. This experiment recorded cell counts of 1,071 daughters of 10 of the bulls selected in Experiment 1. Heritability of the natural logarithm of cell count in first lactation was .081 based on daughters of 31 bulls in Experiment 1. Geometric daughter averages ranged from 206 to 700 X 10(3) cells/ml. Transmitting ability of bulls was estimated by the regressed least squares method. Ranking of bulls on first lactation cell count was different between the two experiments. Management factors and stage of lactation effects could be responsible for these differences. Within Experiment 2, the ranking of bulls on cell counts was nearly identical between first and second lactation. Daughter groups with low average cell count in first lactation in Experiment 2 had low averages in third and fourth lactation although some changes in ranking did occur. These results are consistent with a low to moderate genetic correlation between lactations for cell count. In general, daughter groups with higher average cell count had higher percentage of quarters with mastitis pathogens.

Animals↗
PubMed1980

Cyclic AMP regulation of lactate dehydrogenase. Isoproterenol and N6,O2'-dibutyryl cyclic AMP increase the levels of lactate dehydrogenase-5 isozyme and its messenger RNA in rat C6 glioma cells.

The mechanism of isoproterenol and N6,O2'-dibutyryl adenosine 3':5'-monophosphate (dibutyryl cAMP) induction of lactate dehydrogenase (EC 1.1.1.27) was investigated in the C6 rat glioma cell line. [3H]Leucine-labeled lactate dehydrogenase in noninduced and induced cells was quantitatively immunoprecipitated with rabbit anti-rat lactate dehydrogenase-5 antiserum. The immunoprecipitates were analyzed for 3H-labeled lactate dehydrogenase by electrophoresis on sodium dodecyl sulfate-polyacrylamide gels and isoelectrofocusing. Using this technique, it was shown that isoproterenol + 3-isobutyl-1-methylxanthine and dibutyryl cAMP cause an increase of the [3H]leucine incorporation into glioma cell lactate dehydrogenase. Analysis of the kinetics of induction and deinduction revealed no change in the rate of degradation of lactate dehydrogenase in the presence and absence of inducing agent, indicating that the induction was due to an increase in the rate of synthesis of the enzyme. The increased rate of synthesis was prevented by actinomycin D. Isoproterenol + 3-isobutyl-1-methylxanthine increased only the specific rate of synthesis of lactate dehydrogenase-5 isozyme and of the M subunit. The mechanism was further studied by assaying the level of functional mRNA coding for lactate dehydrogenase in a reticulocyte cell-free protein-synthesizing system using glioma cell poly(A)-containing RNA isolated from either isoproterenol or dibutyryl cAMP-induced cells. Analysis of the immunoprecipitated translation product by isoelectrofocusing revealed that isoproterenol or dibutyryl cAMP produced an approximately 8-fold stimulation of the poly(A) + RNA-directed synthesis of the lactate dehydrogenase M subunit. These data demonstrate that isoproterenol and dibutyryl cAMP control the level of functionally active lactate dehydrogenase mRNA in glioma cells which, in turn, determines the extent of synthesis of the lactate dehydrogenase M subunit.

1-Methyl-3-isobutylxanthine↗
PubMed2000

Effects of high and low blood lactate concentrations on sweat lactate response.

Sweat lactate results from eccrine gland metabolism, however, the possible clearance of blood lactate through sweat has not been resolved. On separate days in an environmental chamber (32 +/- 1 C) 12 subjects completed a constant load (CON) (30 min at 40% VO2 max) and an interval cycling trial (INT) (15 one-min intervals at 80% VO2 max, each separated by one min rest) each designed to elicit different blood lactate responses. Each 30 min cycling trial was preceded by 15 min warm-up (30 watts) and followed by 15 min passive rest. Sweat and blood were analyzed for lactate concentration at 15, 25, 35, 45, and 60 min during CON and INT. Total body water loss was used to calculate sweat rate (ml/hr). Blood lactate was significantly greater (p < or = 0.05) at 25, 35, 45, and 60 min during INT compared to CON (approximately 5 mmol/L vs 1.5 mmol/L). Sweat lactate was not significantly different (p>0.05) between trials at any time (approximately 10 mmol/L). Sweat rates (approximately 600ml/hr) and estimated total lactate secretion were not significantly different (CON vs. INT) (p > 0.05). Elevated blood lactate was not associated with changes in sweat lactate concentration. Sweat lactate seems to originate in eccrine glands independent of blood lactate.

Adult↗
PubMed1994

Metabolic Control of Anaerobic Glycolysis (Overexpression of Lactate Dehydrogenase in Transgenic Tomato Roots Supports the Davies-Roberts Hypothesis and Points to a Critical Role for Lactate Secretion.

Roots of all plants examined so far have the potential for both ethanol and lactate fermentation. A short burst of lactate fermentation usually occurs when plant tissues are transferred from normoxic to anoxic conditions. According to the Davies-Roberts hypothesis, the consequent pH drop both initiates ethanol fermentation and blocks further production of lactate by inhibiting lactate dehydrogenase (LDH). However, the role of LDH in this pH control mechanism is still a matter of debate. To perturb the control system in a defined way, a barley LDH cDNA under the control of the cauliflower mosaic virus 35S promoter was introduced into tomato (Lycopersicon esculentum Mill. cv VFMT) using Agrobacterium rhizogenes. The transgenic root clones expressed up to 50 times the LDH activity of controls. The fermentative metabolism of these clones was compared using roots grown previously in normoxic conditions or roots given a 3-d hypoxic pretreatment. During the transition from normoxia to anoxia, lactate accumulation was no faster and no more extensive in transgenic roots than in controls. Similarly, during prolonged anoxia the flux of 14C from [U-14C] glucose to lactate and ethanol was not modified by the expression of the transgene. However, in both transgenic and control roots, hypoxic pretreatment increased the flux to lactate and promoted lactate export to the medium. These results show that LDH has a very low flux control coefficient for lactate fermentation, consistent with the Davies-Roberts hypothesis. Moreover, they suggest that lactate secretion exerts major control over long-term lactate glycolysis in vivo.

Journal Article↗
PubMed1988

Lactate in fetal tissue during hypoxia; correlation to lactate, pH and base deficit in the fetal blood.

It was the aim of this study to investigate the relationship between the tissue concentrations of lactate in different organs, the blood lactate concentrations, and pH and base deficit in the extracellular fluid (BDecf) during fetal hypoxia. With regard to fetal blood analysis during labour the question is of major importance to what extent blood measurements can provide information concerning intracellular lactate concentrations, especially in the cerebral tissue. In 15 guinea-pig fetuses acute hypoxia was induced by anaesthesia, operative stress and abruption of the placenta. After puncture of the umbilical artery for blood analysis, tissue specimens were taken from the cerebral tissue, heart, liver, lung, muscle and fascia of the abdominal wall, bowel and kidney within 1 to 2 minutes and analyzed for lactate. The lactate concentrations were corrected according to the time interval from blood sampling to collection of tissue specimen. In acute hypoxia the lactate concentrations of the heart and the cerebral tissue were closely correlated to lactate, pH and base deficit measured in arterial blood. The tissue concentration of lactate in the heart and in the cerebrum exceeded the blood level approximately by 70 and 30-50%, respectively. At a pH greater than 7.10 and BDecf less than 8 mumol/ml, the lactate concentration in the cerebrum was about half the lactate concentrations leading to cerebral edema and cell necrosis in the hypoxic monkey fetus (Myers RE. In: Gluck L, ed. Intra-uterine asphyxia and the developing fetal brain. 1977, 37-97).

Acid-Base Equilibrium↗
PubMed1983

Comparison of the D-lactate stereospecific dehydrogenase of Limulus polyphemus with active-site regions of L-lactate dehydrogenases.

Lactate dehydrogenase (D-lactate:NAD+ oxidoreductase, EC 1.1.1.28) from the horseshoe crab, Limulus polyphemus, a dimeric enzyme stereospecific for D-lactate, has been purified by affinity chromatography. Maleyl tryptic peptides containing arginine residues isolated from the Limulus enzyme have been characterized and sequenced. The small peptides obtained from similarly treated L-lactate-specific enzyme homologs define major portions of the substrate and coenzyme binding regions and are virtually identical among L-lactate-specific enzymes. Although the six small peptides and free arginine isolated from the Limulus enzyme indicate that the small number of arginine tryptic peptides are located in a few discrete consecutive clusters similarly to the L-lactate dehydrogenases, the peptides nevertheless show no obvious sequence homology to the corresponding peptides from L-lactate dehydrogenases. These results indicate that this lactate dehydrogenase of altered substrate specificity either evolved with major rearrangements of the active site if it evolved from an L-lactate dehydrogenase, or that D-lactate dehydrogenases have evolved from a different protein. The results contradict proposed models which suggest that minor changes in the spatial orientation of pyruvate resulting from minimal rearrangement of the active site could accommodate the change in substrate specificity.

Amino Acid Sequence↗
PubMed2000

Relationship between milk somatic-cell counts in the first lactation and clinical mastitis occurrence in the second lactation of French Holstein cows.

The relationship between 10 cell-level descriptors in the first lactation and the risk of clinical mastitis in the second lactation was studied in 10205 Holstein cows from 1254 commercial herds using logistic regression. These 10 cell descriptors were based on the mean cell level over the whole first lactation, on the cell level at the beginning or at the end of the first lactation or on the proportion of cell counts below or above given thresholds. Separate analyses were also performed for subsets of herds defined according to their clinical mastitis incidence risk and their lactation mean somatic-cell count (SCC). Odds of clinical mastitis in second lactation was highest (lowest) for high- (low-) yielding cows. All cell descriptors provided consistent results. Lower (higher) mean cell level, higher (lower) proportion of low SCC values, and lower (higher) proportion of high SCC values in the first lactation were associated with a lower (higher) risk of clinical mastitis in the second lactation. The same trends were observed in all subgroups of herds. Cows with the lowest mean SCC in the first lactation had the lowest risk for clinical mastitis in the second lactation. This suggests that selection for decreased SCC may effectively reduce clinical mastitis incidence and that the breeding goal should favor cows with the lowest observed SCC.

Animals↗
PubMed1999

Postpartum body composition changes in lactating and non-lactating primiparas.

The objective of this study is to evaluate the postpartum body composition changes in lactating versus non-lactating or formula-feeding primiparas during the first 12 wk. Twenty primiparous females (age range 17-35 y) who decided to nurse or formula feed their infant were studied. The non-lactating mothers (n = 6) were younger (21 versus 29 y) and had a lower prepregnancy weight (55 kg versus 63 kg) than the lactating mothers (n = 14). Body weight, height, waist and hip measurements, 3-d dietary and activity records, skin-fold thickness from triceps, suprailiac, midthigh, and midupper arm circumference, and total body composition were evaluated at three time periods (at delivery, at 6 wk, and at 12 wk postpartum). Total body composition for bone mineral, lean, and fat mass was measured by dual energy x-ray absorptiometry. At delivery and 6 wk postpartum, the weights and heights were similar between the two groups. By 12 wk postpartum, the formula-feeding group had a weight loss that was different from delivery, 66 +/- 10 kg to 59 +/- 8 kg, P < 0.03. There was no significant weight change in the lactating group during the study. The weight loss consisted of more lean mass than fat mass. The total body bone mineral content did not differ between the two groups during the study. Both groups had reduction in their waist size from delivery to 12 wk postpartum. But only the non-lactating mothers had reductions in their hip and midthigh measurements. There were no changes between the two groups in the skin-fold measurements. Lactating mothers had a higher total daily calories (1974 +/- 318 versus 1464 +/- 178 calories, P < 0.002) and fat intake (63 +/- 14 versus 47 +/- 9 g, P < 0.02) than the non-lactating mothers. The energy expenditure was similar between both groups. In conclusion, during the first 12 wk postpartum, non-lactating mothers who were younger and weighed less prepregnancy lost body weight and had more waist, hip, and midthigh size reductions compared to lactating mothers.

Adolescent↗
PubMed1997

Oxytocin and prolactin suppress cortisol responses to acute stress in both lactating and non-lactating sheep.

Cortisol response to stress appears to differ between lactating and non-lactating animals. Lactating (14 d post partum) and non-lactating sheep were fitted with probes so that drugs and hormones could be infused directly into the posterior pituitary and paraventricular nucleus of the hypothalamus. The animals were also fitted with instruments to allow monitoring of heart rate, body temperature and blood cortisol levels. Their reactions to a source of acute stress (a barking dog) were then followed, with or without drug and hormone manipulation. Results in both lactating and non-lactating animals indicated shortcomings in the use of cortisol as a stress indicator. Infusing prolactin and oxytocin into either the posterior pituitary or the paraventricular nucleus of the hypothalamus suppressed cortisol responsiveness to stress in both lactating and non-lactating animals (the latter to a greater extent). In the absence of drugs, lactating animals had a slightly higher basal level of cortisol and a lower cortisol response to stress than their non-lactating counterparts. Despite suppression of cortisol responses, with or without drugs, other indicators of stress still changed with the presence of a barking dog, suggesting the complexity of control involved in stress responses.

Animals↗
PubMed2001

Lactate dehydrogenase has no control on lactate production but has a strong negative control on formate production in Lactococcus lactis.

A series of mutant strains of Lactococcus lactis were constructed with lactate dehydrogenase (LDH) activities ranging from below 1% to 133% of the wild-type activity level. The mutants with 59% to 133% of lactate dehydrogenase activity had growth rates similar to the wild-type and showed a homolactic pattern of fermentation. Only after lactate dehydrogenase activity was reduced ninefold compared to the wild-type was the growth rate significantly affected, and the ldh mutants started to produce mixed-acid products (formate, acetate, and ethanol in addition to lactate). Flux control coefficients were determined and it was found that lactate dehydrogenase exerted virtually no control on the glycolytic flux at the wild-type enzyme level and also not on the flux catalyzed by the enzyme itself, i.e. on the lactate production. As expected, the flux towards the mixed-acid products was strongly enhanced in the strain deleted for lactate dehydrogenase. What is more surprising is that the enzyme had a strong negative control ( CLDHJF1 =-1.3) on the flux to formate at the wild-type level of lactate dehydrogenase. Furthermore, we showed that L. lactis has limited excess of capacity of lactate dehydrogenase, only 70% more than needed to catalyze the lactate flux in the wild-type cells.

Fermentation↗
PubMed1988

Intracellular pH recovery and lactate efflux in mouse soleus muscles stimulated in vitro: the involvement of sodium/proton exchange and a lactate carrier.

The intracellular pH recovery after stimulation of mouse soleus muscles in vitro was studied by means of intracellular pH-sensitive microelectrodes. The lactate efflux and the total lactate content were measured by means of an enzymic method. During electrical stimulation for 2 min in a CO2/HCO3- -buffered Ringer's solution, pHi decreased by 0.5 units. The rate of pHi-recovery was independent of external bicarbonate, but dependent on the buffer concentration. The rate of intracellular pH recovery was reduced by the lactate transport inhibitors PCMBS and cinnamate, whereas the inhibitors of inorganic anion-exchange SITS and DIDS had no effect. The Na+/H+ exchange inhibitor amiloride reduced the rate of pHi recovery. The pHi recovery was faster than the lactate efflux, which could be accounted for by an Na+/H+ exchange. A number of inhibitor compounds were used in order to discriminate between the three possible lactate efflux pathways: the monocarboxylate carrier mechanism, the inorganic anion exchange, and the molecular (non-ionic) diffusion of lactic acid. The lactate efflux was partly inhibited by cinnamate, PCMBS and phloretin, but was unaffected by DIDS and tetrathionate. These experiments demonstrate the existence of a lactate carrier in mammalian skeletal muscles. The lactate carrier is responsible for more than half of the lactate efflux after muscle activity. Both the pHi recovery studies and the lactate efflux measurements showed that, under the given conditions, the inorganic anion-exchange mechanism is not essentially involved in the recovery processes after muscle activity.

Amiloride↗