Polymorphism of Δ3,5-Δ2,4-dienoyl-coenzyme A isomerase (the ECH1 gene product protein) in human striated muscle tissue

Kovalyov, L. I.; Kovalyova, M. A.; Kovalyov, P. L.; Serebryakova, Marina V.; Moshkovskii, Sergei A.; Shishkin, S. S.

doi:10.1134/s0006297906040146

Cited by 10 publications

(10 citation statements)

References 9 publications

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“…Mining coexpression databases, both COQ3 and COQ8A also coexpress with COQ10A (81). The human ECH1 localizes to the matrix of mitochondria and participates in -oxidation of unsaturated fatty acids (82), and the interaction of ECH1 with both COQ10A and COQ10B aligns well with their roles as chaperones to deliver CoQ as a cofactor for the reaction.…”

Section: Coq10 Family Analysismentioning

confidence: 82%

Human COQ10A and COQ10B are distinct lipid-binding START domain proteins required for coenzyme Q function

Tsui

Pham

Amer

et al. 2019

Journal of Lipid Research

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Coenzyme Q (ubiquinone or Q) functions as an essential redox‐active lipid in respiratory electron and proton transport in cellular energy metabolism, and it is an important lipid‐soluble antioxidant in cellular membranes. In Saccharomyces cerevisiae, proteins Coq3‐Coq9, as well as Coq11, assemble into a multi‐subunit protein complex called the CoQ‐synthome, which is required for Q biosynthesis. Coq10, a putative steroidogenic acute regulatory (StAR)‐related lipid transfer (StART) domain protein is not a member of the CoQ‐synthome, but is required for the proper assembly of the CoQ‐synthome, efficient de novo Q biosynthesis during early‐log phase, and the function of Q in respiration and as an antioxidant. Humans possess two isoforms, namely COQ10A and COQ10B. Based on the RNA‐seq data from NCBI, COQ10A is predominantly expressed in heart while COQ10B is present in all tissues, suggesting that COQ10B is probably serving a more general role. Previous studies have shown rescue of S. cerevisiae coq10Δ respiration deficient phenotype by expression of human COQ10A. Here we present new evidence showing rescue of S. cerevisiae coq10Δ by expression of either the human COQ10A or COQ10B homolog, as determined by restoration of respiratory growth on non‐fermentable carbon sources, de novo Q biosynthesis, as well as restoration of the CoQ‐synthome. Support or Funding Information This research was supported by NSF MCB‐1330803 and Ruth L. Kirschstein National Research Service Award GM007185. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.

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Section: Coq10 Family Analysismentioning

confidence: 82%

Human COQ10A and COQ10B are distinct lipid-binding START domain proteins required for coenzyme Q function

Tsui

Pham

Amer

et al. 2019

Journal of Lipid Research

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“…Following reagents were used: urea, acrylamide, methylene bisacrylamide, agarose, Tris, glycine, sodium dodecyl sulfate, ammonium persulfate, Triton X-100, 2-mercaptoetanol, bull serum albumine, ampholines pH 3 -10, 5 -8 (Sigma, United States), amberlite IRN-150L (Amersham Biosciences, Sweden). The subsequent detection of the proteins was carried out by staining with silver nitrate (Panreac, Spain) as described previously (Kovalyov et al, 2006). The resulting digital images were edited in a graphic editor and the quantitative protein content was calculated using ImageMaster 2D Platinum version 7 ("GE Healthcare", Switzerland).…”

Section: Proteomic Studymentioning

confidence: 99%

Influence of technological processing on lipid-lowering activity of substances containing in porcine hearts and aortas

Kotenkova

Чернуха

2019

Potr. S. J. F. Sci.

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Edible by-products are a good source of nutrients and bioactive substances and could be used as functional ingredients or for biopeptides production natively contained in raw materials. A wide range of peptides are also formed during the enzymatic hydrolysis or food processing. The comparative results of the effectiveness of isolated certain protein and peptide fractions by ultrafiltration with the same natively presented in raw tissues, as well as the influence of heat treatment on biological activity of origin active substances are presented. The model of rat alimentary hyperlipidemia was developed by adding cholesterol and fat to the standard diet and vitamin D2 injection per os. Serum lipid profile was determined on automatic analyzer BioChem FC-360. Dynamic of changes in serum lipid profile was assessed as corresponding control group medium results in ratio to certain rat data. Two-dimensional electrophoresis (2DE) was performed according to the method of O’Farrell with isoelectric focusing in ampholine pH gradient (IEF-PAGE) with following identification by MALDI-TOF MS and MS/MS mass spectrometry. Consumption of native pig aorta and pig heart during 14th days led to normalization of lipid profile in serum of hyperlipidemic rats, while low molecular weight (LMUF, MW <5 kDa) and medium molecular weight (MMUF, MW = 5 – 30 kDa) ultrafiltrates of pig aorta extract did not strongly influenced on level of triglicerides and, on contrary, elevated high density cholesterol. Consumption of developed product by hyperlipidemic rats during 28th days did not lead to significant changes in serum lipid profile, while on 42nd day all ratios reached ones in group, which were treated with native raw material or isolated active fractions. The stability of developed product was confirmed by proteomic studies. Obtained results open prospects to modernization the technology, presumably use as a matrix dietary meat (e.g. poultry) with incorporated active identified components.

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“…Two-dimensional IEF/SDS-PAGE was performed using a linear 7.5–0% gradient of acrylamide concentration in the presence of 0.1% SDS in a Helicon (Russia) vertical electrophoretic cell, as described earlier (Kovalyov et al 1995). Protein visualization by Coomassie Blue R-250 and silver nitrate staining as well as the analysis of two-dimensional (2D) electrophoregrams were performed as described earlier (Kovalyov et al 1995; Kovalev et al 2006) with minor modifications (Kovalyova et al 2009). Molecular masses of proteins in the electrophoretic fractions were determined using the kits of highly purified recombinant proteins SM0671 (10–170 kDa) (Fermentas, USA).…”

Section: Methodsmentioning

confidence: 99%

“…The tryptic hydrolysis of single protein fractions followed by an analysis of tryptic peptides using MALDI TOF MS and MS/MS were used for identification of the proteins as described earlier (Govorun et al 2003; Kovalev et al 2006; Shevchenko et al 1996). Mass-spectra were obtained on a MALDI-TOF-mass-spectrometer Reflex III (Bruker, USA) with UV-laser (336 nm) in the regime of positive ions in the range of 500–8000 Da and calibrated in accordance with the known peaks of trypsin autolysis.…”

Section: Methodsmentioning

confidence: 99%

Glutamate contributes to alcohol hepatotoxicity by enhancing oxidative stress in mitochondria

Теплова

Kruglov

Kovalyov

et al. 2017

J Bioenerg Biomembr

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Chronic alcohol intoxication is associated with increased oxidative stress. However, the mechanisms by which ethanol triggers an increase in the production of reactive oxygen species (ROS) and the role of mitochondria in the development of oxidative stress has been insufficiently studied. The biochemical and proteomic data obtained in the present work suggest that one of the main causes of an increase in ROS generation is enhanced oxidation of glutamate in response to long-term alcohol exposure. In the course of glutamate oxidation, liver mitochondria from alcoholic rats generated more superoxide anion and H2O2 than in the presence of other substrates and more than control organelles. In mitochondria from alcoholic rats, rates of H2O2 production and NAD reduction in the presence of glutamate were almost twice higher than in the control. The proteomic study revealed a higher content of glutamate dehydrogenase in liver mitochondria of rats subjected to chronic alcohol exposure. Simultaneously, the content of mitochondrial catalase decreased compared to control. Each of these factors stimulates the production of ROS in addition to ROS generated by the respiratory chain complex I. The results are consistent with the conclusion that glutamate contributes to alcohol hepatotoxicity by enhancing oxidative stress in mitochondria.

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Polymorphism of Δ3,5-Δ2,4-dienoyl-coenzyme A isomerase (the ECH1 gene product protein) in human striated muscle tissue

Cited by 10 publications

References 9 publications

Human COQ10A and COQ10B are distinct lipid-binding START domain proteins required for coenzyme Q function

Human COQ10A and COQ10B are distinct lipid-binding START domain proteins required for coenzyme Q function

Influence of technological processing on lipid-lowering activity of substances containing in porcine hearts and aortas

Glutamate contributes to alcohol hepatotoxicity by enhancing oxidative stress in mitochondria

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