Singlet Oxygen Toxicity Is Cell Line‐dependent: A Study of Lipid Peroxidation in Nine Leukemia Cell Lines

Schäfer, Freya; Buettner, Garry R.

doi:10.1111/j.1751-1097.1999.tb08294.x

Cited by 35 publications

(9 citation statements)

References 21 publications

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“…As new membrane transport proteins cannot be synthesized and renewed in the mature erythrocyte, it would be predicted that the capacity for zinc and manganese uptake would decline as the cells age. The HEL cell (radius, 12.1 ± 1.8 μm; Schafer & Buettner, 1999) has approximately 3.4 times the surface area of an erythrocyte, and thus our results show that the maximum rate of the histidine‐stimulated zinc uptake per unit of cell surface area in HEL cells is approximately 10 times greater than that in erythrocytes. In addition, the apparent affinities of the uptake site for zinc–, nickel– and cobalt–bis‐histidine complexes in HEL cells are similar to each other and are 50‐ to 100‐fold greater than those found in erythrocytes (Table 1).…”

Section: Discussionmentioning

confidence: 59%

Histidine‐stimulated divalent metal uptake in human erythrocytes and in the erythroleukaemic cell line HEL.92.1.7

Oakley

Horn

Thomas

2004

The Journal of Physiology

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The uptake of 65 Zn by human erythrocytes was investigated in the presence of high (40 mM) and low (5 mM) concentrations of histidine and 0-500 µM cobalt, nickel, manganese and zinc. Varying concentrations of metal mono-and bis-histidine complexes will be formed and the inhibition of 65 Zn uptake could be correlated with the calculated complex concentrations to investigate competition between metals. For each metal, the calculated concentrations of bis-histidine complex giving 50% inhibition of 65 Zn uptake were similar at both 5 mM and 40 mM histidine. Manganese-bis-histidine appeared to have a much higher affinity for the binding site than the other metal-bis-histidine complexes, which had similar affinities to each other. Studies of the inhibition of histidine-stimulated 54 Mn uptake by the addition of manganese confirmed that manganese-bis-histidine does act as a substrate for the transporter in a similar fashion to the other metals studied. In addition, human erythroleukaemic cells (HEL cells) were used as a model for erythroid precursor cells. L-histidine, but not D-histidine, stimulated 65 Zn uptake in a saturable fashion. The other metals competed with zinc in a similar manner to that seen in erythrocytes, and the affinity for manganese-bis-histidine was much greater than for the bis-histidine complexes of the other three metals. Both the capacity for metal transport per cell, and the affinity of the transporter for the metal-bis-histidine complexes, were much greater in the HEL cells than in the erythrocyte. It is suggested that histidine-stimulated metal transport may play a role in the supply of metals to maturing erythroid cells. The normal zinc concentration in human blood plasma is approximately 15 µm. Of this total, about one-third is incorporated within metalloproteins such as α 2 -macroglobulin and is not exchangeable with other plasma components (Giroux, 1975). The remaining zinc is labile and forms possible substrates for cellular uptake mechanisms. Approximately 3% of the total plasma zinc is in the form of coordination complexes formed between zinc, histidine and cysteine (Prasad & Oberleas, 1970;Harris & Keen, 1989). These are in a dynamic equilibrium with free ionic zinc and zinc bound to serum albumin. We have previously investigated the possible role of this amino acid-bound fraction in cellular zinc uptake into human erythrocytes. We reported that l-histidine increased 65 Zn uptake into both rat and human erythrocytes in a dose-dependent fashion, and that the rate of uptake correlated with the calculated concentration of the zinc-bis-histidine complex but not that of the zinc-mono-histidine complex or of free ionic zinc. Stimulation was only seen with the l-enantiomer; d-histidine simply acted as a chelator and reduced uptake. In these experiments, bovine serum albumin (BSA) was present as a metal ion buffer to maintain a low free ionic metal activity even at lower histidine concentrations (Horn et al. 1995). We also reported that the uptake of 109 Cd was stimulated by histidine conce...

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Section: Discussionmentioning

confidence: 59%

Histidine‐stimulated divalent metal uptake in human erythrocytes and in the erythroleukaemic cell line HEL.92.1.7

Oakley

Horn

Thomas

2004

The Journal of Physiology

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“…Superoxide is the most abundant ROS generated under physiological conditions and it is also generated by the auto-oxidation of dopamine [8]. Singlet oxygen, on the other hand, has been paid little attention on the oxidative stress compared with other ROS, although it causes damages DNA [9], PUFA [10], and amino acid [11] at the locus of generation. It is produced by a photosensitized reaction (photodynamic action) and also by enzyme-catalyzed reactions such as myeloperoxidase-hydrogen peroxide-chloride reaction in vivo system [12].…”

Section: Introductionmentioning

confidence: 99%

Structure Effect on Antioxidant Activity of Catecholamines toward Singlet Oxygen and Other Reactive Oxygen Species in vitro

Shimizu

Nakanishi

Nakahara

et al. 2010

J. Clin. Biochem. Nutr.

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The reactivity of catecholamine neurotransmitters and the related metabolites were precisely investigated toward 1,1-diphenyl-2-picrylhydrazyl (DPPH) radicals and reactive oxygen species. Catecholamines reacted immediately with DPPH radicals, their reactivity being stronger than that of ascorbic acid as a reference. Superoxide scavenging activities of catecholamines determined by WST-1 and electron spin resonance (ESR) spin trapping methods were also high. Whereas tyrosine, the dopamine precursor showed no reactivity toward superoxide. The reactivity toward singlet oxygen was evaluated by observing specific photon emission from singlet oxygen. The results revealed that reactivity of catecholamines was markedly higher than that of sodium azide, and catechin as catechol reference. The reaction of catecholamines and singlet oxygen was further studied by ESR using 55-dimethyl-1-pyrroline N-oxide (DMPO) as a spin trapping reagent and rose bengal as photosensitizer. DMPO-OH signal of epinephrine was significantly small compared to other catecholamines, catechin, and 4-methylcatechol as a reference compound and was as small as that of tyrosine. The signal formation was totally dependent on singlet oxygen, and the presence of catechol compounds. These results indicated that epinephrine is the most potent singlet oxygen quencher than other catecholamines, and the secondary amino group in its alkyl side chain could play a role in unique singlet oxygen quenching property of epinephrine.

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“…When the 1 O 2 is generated, it can react with surrounding molecules ("chemical quenching", [62]) or return to its ground triplet state via physical quenching. Chemical quenching in biological systems, in which 1 O 2 reacts with proteins (mainly with Cys, Met, Trp, Tyr, and His), lipid membranes (unsaturated fatty acids and cholesterol [63,64]), DNA (mainly guanine) or carbohydrates, is the main reason for singlet oxygen's cytotoxicity. Regarding physical quenching, there are two major types: energy transfer and charge transfer [65].…”

Section: O 2 Quenchingmentioning

confidence: 99%

Killer Beacons for Combined Cancer Imaging and Therapy

Stefflova¹,

Chen²,

Zheng

2007

CMC

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Cu r r e n t Me d i c i n a l Ch e mi s t r y c o v e r s a l l t h e l a t e s t a n d o u t s t a n d i n g d e v e l o p me n t s i n me d i c i n a l c h e mi s t r y a n d r a t i o n a l d r u g d e s i g n . E a c h i s s u e c o n t a i n s a s e r i e s o f t i me l y i n -d e p t h r e v i e w s a n d g u e s t e d i t e d t h e ma t i c i s s u e s w r i t t e n b y l e a d e r s i n t h e f i e l d c o v e r i n g a r a n g e o f t h e c u r r e n t t o p i c s i n i n me d i c i n a l c h e mi s t r y . Cu r r e n t Me d i c i n a l Ch e mi s t r y i s a n e s s e n t i a l j o u r n a l f o r e v e r y me d i c i n a l c h e mi s t w h o w i s h e s t o b e k e p t i n f o r me d a n d u p -t o -d a t e w i t h t h e l a t e s t a n d mo s t i mp o r t a n t d e v e l o p me n t s .

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Singlet Oxygen Toxicity Is Cell Line‐dependent: A Study of Lipid Peroxidation in Nine Leukemia Cell Lines

Cited by 35 publications

References 21 publications

Histidine‐stimulated divalent metal uptake in human erythrocytes and in the erythroleukaemic cell line HEL.92.1.7

Histidine‐stimulated divalent metal uptake in human erythrocytes and in the erythroleukaemic cell line HEL.92.1.7

Structure Effect on Antioxidant Activity of Catecholamines toward Singlet Oxygen and Other Reactive Oxygen Species in vitro

Killer Beacons for Combined Cancer Imaging and Therapy

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