Ultraviolet Irradiation-Dependent Fluorescence Enhancement of Hemoglobin Catalyzed by Reactive Oxygen Species

Pan, Leiting; Wang, Xiaoxu; Yang, Shuying; Wang, Xian; Lee, Imshik; Zhang, Xinzheng; Rupp, R. A.; Xu, Jingyi

doi:10.1371/journal.pone.0044142

Cited by 16 publications

(12 citation statements)

References 27 publications

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“…6). By comparing the spectra of the first and last acquisitions, it is evident that the spectrum is evolving from that of oxy-Hb to a spectrum that represents the spectral features of methemoglobin [58], confirming that the Fe 2+ (ferrous) ion in the heme groups are changing to Fe 3+ (ferric) under UV illumination due to its high oxidation potency [61][62][63][64]. Such temporal dynamics were not observed in any of the other molecules tested in this study.…”

Section: Theory and Data Analysismentioning

confidence: 99%

Deep UV dispersion and absorption spectroscopy of biomolecules

Soltani

Ojaghi

Robles

2019

Biomed. Opt. Express

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Owing to the high precision and sensitivity of optical systems, there is an increasing demand for optical methods that quantitatively characterize the physical and chemical properties of biological samples. Information extracted from such quantitative methods, through phase and/or amplitude variations of light, can be crucial in the diagnosis, treatment and study of disease. In this work we apply a recently developed quantitative method, called ultraviolet hyperspectral interferometry (UHI), to characterize the dispersion and absorbing properties of various important biomolecules. Our system consists of (1) a broadband light source that spans from the deep-UV to the visible region of the spectrum, and (2) a Mach-Zehnder interferometer to gain access to complex optical properties. We apply this method to characterize (and tabulate) the dispersive and absorptive properties of hemoglobin, beta nicotinamide adenine dinucleotide (NAD), flavin adenine dinucleotide (FAD), elastin, collagen, cytochrome c, tryptophan and DNA. Our results shed new light on the complex properties of important biomolecules.

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Section: Theory and Data Analysismentioning

confidence: 99%

Deep UV dispersion and absorption spectroscopy of biomolecules

Soltani

Ojaghi

Robles

2019

Biomed. Opt. Express

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“…It is known that at least two factors should contribute to the periodical changes. Second, our previous results 37 , 40 and other researchers’ work 41 demonstrated that UVA light could lead to hemoglobin decomposition rather than cross-linking. Meanwhile, as the important effector of UV irradiation, ROS was found to degrade hemoglobin.…”

Section: Discussionmentioning

confidence: 77%

Protection of the biconcave profile of human erythrocytes against osmotic damage by ultraviolet-A irradiation through membrane-cytoskeleton enhancement

Xun

et al. 2017

Cell Death Discov.

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To perform various physiological functions, erythrocytes possess a unique biconcave shape provided by a special architecture of the membrane-skeleton system. In the present work, we use a simple irradiation method to treat human erythrocytes with 365 nm ultraviolet-A (UVA) light at the single-cell level in vitro. Depending on the irradiation dose, UVA show protection of the biconcave profile against the detrimental action of distilled water. This protective effect can also be confirmed for saponin that damages the membrane-skeleton by vesiculation and pore formation. Interestingly, at two irradiation doses of UVA pretreatment, erythrocytes still seem to exhibit cell viability as tested by trypan blue assay even if distilled water or saponin is added. The oxidants hydrogen peroxide and cumene hydroperoxide partly simulate the protective effects. Taken together, these results demonstrate that 365 nm UVA irradiation can protect the biconcave profile of human erythrocytes through membrane-skeleton enhancement associated with a production of oxidants.

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“…PKA activity in intact erythrocytes was assessed by using confocal microscopy. Since UV illumination ( % 360 nm) is known to have an immediate untoward impact on hemoglobin biochemistry, [19] we employed a 405 nm laser to convert the DNMB-peptide 3 to its phosphorylatable counterpart. Upon photolysis, a rapid fluorescence response is observed in the interior of erythrocytes (Figure 3 and Figures S22-S25).…”

Section: Methodsmentioning

confidence: 99%

Long‐Wavelength Fluorescent Reporters for Monitoring Protein Kinase Activity

et al. 2014

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In vivo optical imaging must contend with the limitations imposed by the optical window of tissue (600-1000 nm). Although a wide array of fluorophores are available that are visualized in the red and near-IR region of the spectrum, with the exception of proteases, there are few long wavelength probes for enzymes. This situation poses a particular challenge for studying the intracellular biochemistry of erythrocytes, the high hemoglobin content of which optically obscures subcellular monitoring at wavelengths less than 600 nm. To address this, tunable fluorescent reporters for protein kinase activity were developed. The probing wavelength is preprogrammed by using readily available fluorophores, thereby enabling detection within the optical window of tissue, specifically in the far-red and near-IR region. These agents were used to monitor endogenous cAMP-dependent protein kinase activity in erythrocyte lysates and in intact erythrocytes when using a light-activatable reporter.

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Ultraviolet Irradiation-Dependent Fluorescence Enhancement of Hemoglobin Catalyzed by Reactive Oxygen Species

Cited by 16 publications

References 27 publications

Deep UV dispersion and absorption spectroscopy of biomolecules

Deep UV dispersion and absorption spectroscopy of biomolecules

Protection of the biconcave profile of human erythrocytes against osmotic damage by ultraviolet-A irradiation through membrane-cytoskeleton enhancement

Long‐Wavelength Fluorescent Reporters for Monitoring Protein Kinase Activity

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