scholarly journals LDH (Lactate Dehydrogenase): A Biochemical Marker for the Prediction of Adverse Outcomes in Pre-eclampsia and Eclampsia

2014 ◽  
Vol 66 (1) ◽  
pp. 23-29 ◽  
Author(s):  
Anupama Dave ◽  
Laxmi Maru ◽  
Astha Jain
2018 ◽  
Vol 2018 ◽  
pp. 1-7 ◽  
Author(s):  
Aneta Ostróżka-Cieślik ◽  
Barbara Dolińska ◽  
Florian Ryszka

Biolasol is a newly developed solution for storing the liver, pancreas, kidneys, and heart by simple hypothermia. It exhibits high efficacy in maintaining structural and functional integrity of the graft prior to its transplantation. The solution was modified by the addition of ascorbic acid (0.088g/l) and ascorbic acid with prolactin (1 μg/l PRL + 0.088g/l vitamin C). The effectiveness of the obtained solutions in the protection of nephrons of isolated porcine kidneys was assessed based on the analysis of the activity of ALT (alanine aminotransferase), AST (aspartate aminotransferase), and LDH (lactate dehydrogenase) as well as lactate concentration determined in perfundates collected after 2 h (0′ and 30′ preservation) and 48 h (0′ and 30′ preservation) of graft storage. It has been found that the synergistic action of Biolasol components determines the integrity and stability of cell membranes, which in turn affects the proper functioning of the organ after transplantation. The addition of ascorbic acid and prolactin to Biolasol affects the maintenance of the normal cytoskeleton of the stored graft.


Author(s):  
Vinitha Padmini Mary ◽  
M. Chellatamizh ◽  
S. Padmanaban

Background: LDH is an intracellular cytoplasmic enzyme. It is ubiquitous to all the major organ systems. Cellular enzymes in extracellular space have no metabolic function, although they serve as indicators of disturbances in cellular integrity. Serum LDH is abnormal in many disorders, therefore total serum LDH is highly sensitive but nonspecific test. In preeclampsia also LDH may be elevated and can indicate the prognosis for both mother and fetus. We conducted this study to examine the relationship between lactate dehydrogenase concentration and the severity of the disease and the occurrence of its complications.Methods: 200 pre-eclamptic women (121 with mild and 79 with severe pre-eclampsia) and 200 healthy normotensive controls were studied prospectively at Government Kilpauk medical college and hospital between January and December 2015. Demographic, hemodynamic, and laboratory data were compared among the three groups. The symptoms and complications of severe pre-eclampsia along with fetal outcome were analyzed according to the levels of LDH.Results: Severely pre-eclamptic patients were significantly younger, with low gravidity and parity. On the other hand, they had significantly increased systolic and diastolic pressure and liver enzymes, uric acid, urine albumin, and LDH levels. The symptoms and complications of pre-eclampsia along with perinatal mortality were increased significantly in patients with LDH >800 IU/l compared with those who had lower levels.Conclusions:  Lactate dehydrogenase is a useful biochemical marker that reflects the severity of pre-eclampsia. In our study, LDH has been evaluated as a biochemical marker for preeclampsia and as a prognosticator of the disease severity. Detection of high-risk patients with increased levels of LDH mandate close monitoring and management to prevent maternal and fetal morbidity and mortality.


2012 ◽  
Vol 443 (3) ◽  
pp. 747-755 ◽  
Author(s):  
Frank Norbert Gellerich ◽  
Zemfira Gizatullina ◽  
Sonata Trumbekaite ◽  
Bernard Korzeniewski ◽  
Timur Gaynutdinov ◽  
...  

The glutamate-dependent respiration of isolated BM (brain mitochondria) is regulated by Ca2+cyt (cytosolic Ca2+) (S0.5=225±22 nM) through its effects on aralar. We now also demonstrate that the α-glycerophosphate-dependent respiration is controlled by Ca2+cyt (S0.5=60±10 nM). At higher Ca2+cyt (>600 nM), BM accumulate Ca2+ which enhances the rate of intramitochondrial dehydrogenases. The Ca2+-induced increments of state 3 respiration decrease with substrate in the order glutamate>α-oxoglutarate>isocitrate>α-glycerophosphate>pyruvate. Whereas the oxidation of pyruvate is only slightly influenced by Ca2+cyt, we show that the formation of pyruvate is tightly controlled by Ca2+cyt. Through its common substrate couple NADH/NAD+, the formation of pyruvate by LDH (lactate dehydrogenase) is linked to the MAS (malate–aspartate shuttle) with aralar as a central component. A rise in Ca2+cyt in a reconstituted system consisting of BM, cytosolic enzymes of MAS and LDH causes an up to 5-fold enhancement of OXPHOS (oxidative phosphorylation) rates that is due to an increased substrate supply, acting in a manner similar to a ‘gas pedal’. In contrast, Ca2+mit (intramitochondrial Ca2+) regulates the oxidation rates of substrates which are present within the mitochondrial matrix. We postulate that Ca2+cyt is a key factor in adjusting the mitochondrial energization to the requirements of intact neurons.


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