Inhibition of human muscle-specific enolase by methylglyoxal and irreversible formation of advanced glycation end products

Gamian, Andrzej; Staniszewska, Magdalena; Danielewicz, Regina

doi:10.1080/14756360802187679

Cited by 21 publications

(13 citation statements)

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“…Glycation inhibition of MDH activity is rescued by aspirin and alpha crystalline [34]. In yeast, enolase is prime target protein for the glycation [35,36].…”

Section: Quantification Of Glycationmentioning

confidence: 99%

Proteomic Analysis of Glycated Proteins from Streptozotocin-Induced Diabetic Rat Kidney

et al. 2011

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Glycation of proteins leading to formation of advanced glycation end products (AGEs) has been considered as one of the important causes of diabetic nephropathy. Therefore, in this study, glycated proteins were detected by anti-AGE antibodies from kidney of streptozotocin-induced diabetic rat showing nephropathic symptoms, by using two dimensional electrophoresis and western blot analysis. These glycated proteins were identified and characterized by using combination of peptide mass finger printing and tandem mass spectrometric approaches. Glycated proteins identified included proteins from metabolic pathways, oxidative stress, cell signaling, and transport. Several of the proteins modified by glycation were involved in glucose metabolism. The extent of glycation was higher in diabetes compared to control, in the glycated proteins that were common to both control and diabetic kidney. Two dimensional electrophoresis proteins profiling of glycated proteins suggest that four of the glycated proteins were significantly up regulated in diabetes.

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“…Glycation inhibition of MDH activity is rescued by aspirin and alpha crystalline [34]. In yeast, enolase is prime target protein for the glycation [35,36].…”

Section: Quantification Of Glycationmentioning

confidence: 99%

Proteomic Analysis of Glycated Proteins from Streptozotocin-Induced Diabetic Rat Kidney

et al. 2011

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“…At all stages of the enzyme purification, the magnesium sulfate and temperature set at 4 °C were used to prevent the loss of the enolase activity. Magnesium ions are essential for both catalysis and stability of the enolase dimer [2] , [39] . Purification of β-enolase from human muscle tissue was performed according to the procedure described earlier [40] .…”

Section: Methodsmentioning

confidence: 99%

Experimental and bioinformatic approach to identifying antigenic epitopes in human α- and β-enolases

Danielewicz

Bednarz−Misa

Ceremuga

et al. 2018

Biochemistry and Biophysics Reports

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Human α- and β-enolases are highly homologous enzymes, difficult to differentiate immunologically. In this work, we describe production, purification and properties of anti-α- and anti-β-enolase polyclonal antibodies. To raise antibodies, rabbits were injected with enolase isoenzymes that were purified from human kidney (α-enolase) and skeletal muscle (β-enolase). Selective anti-α- and anti-β-enolase antibodies were obtained by affinity chromatography on either α- or β-enolase-Sepharose columns. On Western blots, antibodies directed against human β-enolase, did not react with human α-isoenzyme, but recognized pig and rat β-enolase. To determine what makes these antibodies selective bioinformatic tools were used to predict conformational epitopes for both enolase isoenzymes. Three predicted epitopes were mapped to the same regions in both α- and β-enolase. Peptides corresponding to predicted epitopes were synthesized and tested against purified antibodies. One of the pin-attached peptides representing α-enolase epitope (the C-terminal portion of the epitope 3 - S262PDDPSRYISPDQ273) reacted with anti-α-enolase, while the other also derived from the α-enolase sequence (epitope 2 - N193VIKEKYGKDATN205) was recognized by anti-β-enolase antibodies. Interestingly, neither anti-α- nor anti-β-antibody reacted with a peptide corresponding to the epitope 2 in β-enolase (G194VIKAKYGKDATN206). Further analysis showed that substitution of E197 with A in α-enolase epitope 2 peptide lead to 70% loss of immunological activity, while replacement of A198 with E in peptide representing β-enolase epitope 2, caused 67% increase in immunological activity. Our results suggest that E197 is essential for preserving immunologically active conformation in epitope 2 peptidic homolog, while it is not crucial for this epitope's antigenic activity in native β-enolase.

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“…Finally, it is known that the inhibition of enolase results in the formation of advanced glycation end products (AGEs) [442] and AGEs inhibit NKA enzyme activity [443]. Again, the mechanistic pathway has been elucidated to involve activation of AA metabolism via PLA2 activation [443].…”

Section: Molecular Mechanisms By Which Fluoride Inhibits Na+ K+-amentioning

confidence: 99%

Fluoride Exposure Induces Inhibition of Sodium-and Potassium-Activated Adenosine Triphosphatase (Na+, K+-ATPase) Enzyme Activity: Molecular Mechanisms and Implications for Public Health

Waugh¹

2019

IJERPH

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In this study, several lines of evidence are provided to show that Na + , K + -ATPase activity exerts vital roles in normal brain development and function and that loss of enzyme activity is implicated in neurodevelopmental, neuropsychiatric and neurodegenerative disorders, as well as increased risk of cancer, metabolic, pulmonary and cardiovascular disease. Evidence is presented to show that fluoride (F) inhibits Na + , K + -ATPase activity by altering biological pathways through modifying the expression of genes and the activity of glycolytic enzymes, metalloenzymes, hormones, proteins, neuropeptides and cytokines, as well as biological interface interactions that rely on the bioavailability of chemical elements magnesium and manganese to modulate ATP and Na + , K + -ATPase enzyme activity. Taken together, the findings of this study provide unprecedented insights into the molecular mechanisms and biological pathways by which F inhibits Na + , K + -ATPase activity and contributes to the etiology and pathophysiology of diseases associated with impairment of this essential enzyme. Moreover, the findings of this study further suggest that there are windows of susceptibility over the life course where chronic F exposure in pregnancy and early infancy may impair Na + , K + -ATPase activity with both short- and long-term implications for disease and inequalities in health. These findings would warrant considerable attention and potential intervention, not to mention additional research on the potential effects of F intake in contributing to chronic disease.

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Inhibition of human muscle-specific enolase by methylglyoxal and irreversible formation of advanced glycation end products

Cited by 21 publications

References 50 publications

Proteomic Analysis of Glycated Proteins from Streptozotocin-Induced Diabetic Rat Kidney

Proteomic Analysis of Glycated Proteins from Streptozotocin-Induced Diabetic Rat Kidney

Experimental and bioinformatic approach to identifying antigenic epitopes in human α- and β-enolases

Fluoride Exposure Induces Inhibition of Sodium-and Potassium-Activated Adenosine Triphosphatase (Na+, K+-ATPase) Enzyme Activity: Molecular Mechanisms and Implications for Public Health

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