Isoenzyme profile of lactate dehydrogenase in the cranial cervical sympathetic ganglion under normal conditions and during synaptic blockade

Gorelikov, P. L.; Savel’ev, S. V.

doi:10.1007/s10517-006-0055-x

Cited by 2 publications

(1 citation statement)

References 9 publications

(13 reference statements)

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“…LDH activity was determined by measuring the linear decrease of NADH absorbance at 340 nm within the first 6 minutes of the reaction. In order to identify the presence of the different LDH isoforms and also to measure total LDH activity in the opposite direction -towards pyruvate production, LDH isoenzymes were separated from whole-body homogenates with native disc PAGE (30 μg of total proteins per well), while in-gel LDH activity was detected using Na-lactate as substrate and nitroblue tetrazolium (NBT) as the chromogenic compound 69,70 . Gels were documented using BioDocAnalyze (BDA) digital system (Biometra, Germany) and the relative abundance of the bands was quantified in the program ImageJ (Rasband, W.S., ImageJ, U. S. National Institutes of Health, Bethesda, Maryland, USA, https://imagej.nih.gov/ij/, 1997-2018).…”

Section: Methodsmentioning

confidence: 99%

Effect of Cold Acclimation on Selected Metabolic Enzymes During Diapause in The European Corn Borer Ostrinia nubilalis (Hbn.)

Uzelac

Avramov

Čelić

et al. 2020

Sci Rep

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The European corn borer, Ostrinia nubilalis Hbn., is a pest Lepidopteran species whose larvae overwinter by entering diapause, gradually becoming cold-hardy. To investigate metabolic changes during cold hardening, activities of four metabolic enzymes-citrate synthase (CS), lactate dehydrogenase (LDH), alanine aminotransferase (ALT) and aspartate aminotransferase (AST) were measured in whole-body homogenates of pupae, non-diapausing and diapausing larvae acclimated to 5 °C, −3 °C and −16 °C. The highest CS activity was detected in non-diapausing larvae, reflecting active development, while the highest in vitro LDH activity was recorded in diapausing larvae at temperatures close to 0 °C, evidencing a metabolic switch towards anaerobic metabolism. However, in-gel LDH activity showed that production of pyruvate from lactate is triggered by sub-zero temperatures. The activities of both aminotransferases were highest in non-diapausing larvae. Our findings suggest that during diapause and cold hardening the aminotransferases catalyse production of L-alanine, an important cryoprotectant, and L-aspartate, which is closely tied to both transamination reactions and Krebs cycle. The results of this study indicate that, during diapause, the activity of metabolic enzymes is synchronized with exogenous factors, such as temperatures close to 0 °C. These findings support the notion that diapause is metabolically plastic and vibrant, rather than simply a passive, resting state.

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Section: Methodsmentioning

confidence: 99%

Effect of Cold Acclimation on Selected Metabolic Enzymes During Diapause in The European Corn Borer Ostrinia nubilalis (Hbn.)

Uzelac

Avramov

Čelić

et al. 2020

Sci Rep

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Lactate dehydrogenase isoenzymes in sympathetic neurons and satellite gliocytes in normal conditions and in blockade of nicotinic cholinoreceptors

Gorelikov

Savel’ev

2008

Neurosci Behav Physi

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Integral cytophotometry was used to measure lactate dehydrogenase (LDH) and its H-and M-isoforms in neurons and satellite gliocytes in tissue sections from the cranial cervical sympathetic ganglion of the rabbit in normal conditions and after experimental partial and complete pharmacological blockade of nicotinic cholinoreceptors (n-CR). In normal conditions, both cell types showed both the H-and M-type isoforms, though the isoenzyme profiles differed--neurons showed a dominance of H-isoform activity while the M-isoform was more active in satellite gliocytes. In partial and complete blockade, the activity of LDH and its H-and M-isoforms decreased significantly in proportion to the number of blocked n-CR. In satellite gliocytes, increases in the extent of blockade were associated with decreases in the activity only of the M-isoform, while the activity of the H-isoform did not change. In partial blockade, the LDH isoenzyme profile of satellite gliocytes shifted towards the neuronal isoform, while in complete blockade there was no difference from the LDH isoenzyme profile of intact neurons. These data led to the suggestion that the formation of lactate in satellite gliocytes is induced by nicotinic cholinergic synapses directly involved in neuron-glial interactions and in controlling the activity of the LDH enzyme system in sympathetic neurons.

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Isoenzyme profile of lactate dehydrogenase in the cranial cervical sympathetic ganglion under normal conditions and during synaptic blockade

Cited by 2 publications

References 9 publications

Effect of Cold Acclimation on Selected Metabolic Enzymes During Diapause in The European Corn Borer Ostrinia nubilalis (Hbn.)

Effect of Cold Acclimation on Selected Metabolic Enzymes During Diapause in The European Corn Borer Ostrinia nubilalis (Hbn.)

Lactate dehydrogenase isoenzymes in sympathetic neurons and satellite gliocytes in normal conditions and in blockade of nicotinic cholinoreceptors

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