Cancer-Associated Alteration in Fatty Acid Binding to Albumin Studied by Spin-Label Electron Spin Resonance

Gurachevsky, Andrey; Muravskaya, E. V.; Gurachevskaya, Tatjana; Smirnova, Lena; Muravsky, Vladimir

doi:10.1080/07357900701407947

Cited by 16 publications

(25 citation statements)

References 17 publications

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“…Albumin as the major transport protein in the human organism protects these cancer markers from catabolism and significantly amplifies their concentration. It is confirmed [3], [4], [5] that these proteins block the albumin function by changing its conformation. The conformational change of serum albumin, and thus its transport and detoxification properties, can be determined with the help of the ESR spectrum.…”

Section: Introductionmentioning

confidence: 55%

Expectation-maximization-estimation of mixture densities for Electron-Spin-Resonance-analysis of albumin

Schmidt¹,

Krumbiegel

Waterstradt³

et al. 2009

2009 IEEE International Workshop on Genomic Signal Processing and Statistics

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Early diagnosis of human cancer is of crucial importance for successful therapies. Cancer diagnosis via ESR (Electron-Spin-Resonance) spectroscopy of albumin found in human blood provides a new promising approach. The ESR frontend signal processing follows a protocol of our proprietary 'mobility of molecular structure test' (MMSTest) and provides a real-valued 33-dimensional vector representation per sample, which combines a representative feature set of the binding ability (spin-probes) of albumin under investigation. Classical statistical pattern recognition is then applied to the feature vector, including LDA and EM mixture density estimation, leading to a classification error rate of 14% between the two patient classes 'healthy' and 'suspect'. The class 'suspect' includes cancer and other chronic condition. The investigation was performed on a proprietary database of MedInnovation with 1176 cancer and non-cancer patients.

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Section: Introductionmentioning

confidence: 55%

Expectation-maximization-estimation of mixture densities for Electron-Spin-Resonance-analysis of albumin

Schmidt¹,

Krumbiegel

Waterstradt³

et al. 2009

2009 IEEE International Workshop on Genomic Signal Processing and Statistics

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“…For example, electron spin resonance studies of albumin modulation by cancer-related small molecule markers revealed significant differences in binding of albumin-specific 16-doxyl-stearic acid probe. During disease progression the albumin pool saturates with cancer cellular metabolites, thus indicating an affected albumin state [58].…”

Section: Integrative Approaches Applied To Human Diseasesmentioning

confidence: 99%

On Different Aspects of Network Analysis in Systems Biology

et al. 2013

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Network analysis is an essential component of systems biology approaches toward understanding the molecular and cellular interactions underlying biological systems functionalities and their perturbations in disease. Regulatory and signalling pathways involve DNA, RNA, proteins and metabolites as key elements to coordinate most aspects of cellular functioning. Cellular processes depend on the structure and dynamics of gene regulatory networks and can be studied by employing a network representation of molecular interactions. This chapter describes several types of biological networks, how combination of different analytic approaches can be used to study diseases, and provides a list of selected tools for network visualization and analysis. It also introduces proteinprotein interaction networks, gene regulatory networks, signalling networks and metabolic networks to illustrate concepts underlying network representation of cellular processes and molecular interactions. It finally discusses how the level of An erratum to this chapter is available at

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“…This is an efficient and widely used method for studying the binding of FAs to albumin [18][19][20][21][22][23], as well as the competition between FAs and other compounds although its application for metal complexes is fairly rare in the literature [24]. Furthermore, displacement experiments with wellestablished markers for sites I and II, namely warfarin (WF) and dansylglycine (DG), respectively, were also performed and the data is discussed.…”

Section: Interaction Of Anticancer Metallodrugs With Proteins Is Of Cmentioning

confidence: 99%

“…Since complexes 1-5 showed similar binding affinities for HSA (Table 1), the binding of complex 5 was further studied in the presence of a stearic FA, labeled with an aminoxyl radical at position C-16 (16-doxyl stearic acid, 16DS), a spin label that has been used in many previous studies [18][19][20]22,23]. It is important to note that the binding of FAs to HSA is not perturbed by spin labeling of FAs [20], hence the EPR spin labeling technique can provide reliable information about the amount of the FAs bound to HSA.…”

Section: Binding Of Complex 5 In Presence Of Long-chain Fatty Acids: mentioning

confidence: 99%

Investigation of the binding of cis/trans-[MCl4(1H-indazole)(NO)]− (M = Ru, Os) complexes to human serum albumin

Dömötör

Rathgeb

Kuhn

et al. 2016

Journal of Inorganic Biochemistry

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Overall binding affinity of sodium or indazolium cis/trans-[MCl 4 (1H-indazole)(NO)] (M = Ru,Os) complexes towards human serum albumin (HSA) and high molecular mass components of the blood serum was monitored by ultrafiltration. HSA was found to be mainly responsible for the binding of the studied ruthenium and osmium complexes. In other words, this protein can provide a depot for the compounds and can affect their biodistribution and transport processes. In order to elucidate the HSA binding sites tryptophan fluorescence quenching studies and displacement reactions with the established site markers warfarin and dansylglycine were performed. Conditional stability constants for the binding to sites I and II on HSA were computed showing that the studied ruthenium and osmium complexes are able to bind into both sites with moderately strong affinity (logK' = 4.4-5.1). Site I is slightly more favored over site II for all complexes. No significant differences in the HSA binding properties were found for these metal complexes demonstrating negligible influence of the type of counter ion (sodium vs. indazolium), the metal ion center identity (Ru vs. Os) or the position of the nitrosyl group on the binding 2 event. Electron paramagnetic resonance spin labeling of HSA revealed that indazolium trans-[RuCl 4 (1H-indazole)(NO)] and long-chain fatty acids show competitive binding to HSA.Moreover, this complex has a higher affinity for site I, but when present in excess, it is able to bind to site II as well, and displace fatty acids.

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Cancer-Associated Alteration in Fatty Acid Binding to Albumin Studied by Spin-Label Electron Spin Resonance

Cited by 16 publications

References 17 publications

Expectation-maximization-estimation of mixture densities for Electron-Spin-Resonance-analysis of albumin

Expectation-maximization-estimation of mixture densities for Electron-Spin-Resonance-analysis of albumin

On Different Aspects of Network Analysis in Systems Biology

Investigation of the binding of cis/trans-[MCl4(1H-indazole)(NO)]− (M = Ru, Os) complexes to human serum albumin

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