Transport of d-[1-14C]-amino acids into Chinese hamster ovary (CHO-K1) cells: implications for use of labeled d-amino acids as molecular imaging agents

Shikano, Naoto; Nakajima, Syuichi; Kotani, Takashi; Ogura, Masato; Sagara, Jun‐ichi; Iwamura, Yukio; Yoshimoto, Mitsuyoshi; Kubota, Nobuo; Ishikawa, Nobuyoshi; Kawai, Keiichi

doi:10.1016/j.nucmedbio.2007.05.001

Cited by 9 publications

(10 citation statements)

References 42 publications

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“…Based on the comparability of IC 50 values observed for l –Hcy and l –Met inhibition of [ 14 C]MeAIB uptake, and the relatively high preference of SNAT1 and SNAT2 for l –Met as substrate (Hatanaka et al 2000; Wang et al 2000), we speculate that l –Hcy transport across MVM may involve either, or both, of these two SNAT isoforms. Our observation that the racemic mixture dl –Hcy was equally effective as l –Hcy in inhibiting [ 14 C]MeAIB uptake into MVM is consistent with the demonstration that both enantiomers of Hcy can be transported (Jiang et al 2007) and that d –enantiomers of amino acids can be taken up into cells by various transport mechanisms, including systems A and L, although stereoselectivity usually favours the l –enantiomer (Shikano et al 2007).…”

Section: Discussionsupporting

confidence: 88%

Homocysteine transport by systems L, A and y⁺L across the microvillous plasma membrane of human placenta

Tsitsiou

Sibley

D'Souza

et al. 2009

The Journal of Physiology

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Section: Discussionsupporting

confidence: 88%

Homocysteine transport by systems L, A and y⁺L across the microvillous plasma membrane of human placenta

Tsitsiou

Sibley

D'Souza

et al. 2009

The Journal of Physiology

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“…Moreover, while no specific transporters are known to facilitate penetration of luciferins, D-cysteine could still be a substrate for cysteine transporters, responsible for the uptake of L-cysteine by mammalian cells. 67-70 In addition, better stability of the split luciferin ligation reagents in comparison to luciferins 51,56-60 may also play a significant role in increased light output from live cells.…”

Section: Resultsmentioning

confidence: 99%

“…2b). 67,69,70 In addition, the intensity of the light output resulting from split luciferin ligation reaction could be significantly increased by injection of higher concentration of D-cysteine (Fig. 2, S9).…”

Section: Discussionmentioning

confidence: 97%

A Biocompatible in Vivo Ligation Reaction and Its Application for Noninvasive Bioluminescent Imaging of Protease Activity in Living Mice

et al. 2013

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The discovery of biocompatible reactions has had a tremendous impact on chemical biology, allowing the study of numerous biological processes directly in complex systems. However, despite the fact that multiple biocompatible reactions have been developed in the past decade, very few work well in living mice. Here we report that D-cysteine and 2-cyanobenzothiazoles can selectively react with each other in vivo to generate a luciferin substrate for firefly luciferase. The success of this “split luciferin” ligation reaction has important implications for both in vivo imaging and biocompatible labeling strategies. First, the production of a luciferin substrate can be visualized in a live mouse by bioluminescence imaging (BLI), and furthermore allows interrogation of targeted tissues using a “caged” luciferin approach. We therefore applied this reaction to the real-time non-invasive imaging of apoptosis associated with caspase 3/7. Caspase-dependent release of free D-cysteine from the caspase 3/7 peptide substrate Asp-Glu-Val-Asp-D-Cys (DEVD-(D-Cys)) allowed selective reaction with 6-amino-2-cyanobenzothiazole (NH2-CBT) in vivo to form 6-amino-D-luciferin with subsequent light emission from luciferase. Importantly, this strategy was found to be superior to the commercially-available DEVD-aminoluciferin substrate for imaging of caspase 3/7 activity. Moreover, the split luciferin approach enables the modular construction of bioluminogenic sensors, where either or both reaction partners could be caged to report on multiple biological events. Lastly, the luciferin ligation reaction is three orders of magnitude faster than Staudinger ligation suggesting further applications for both bioluminescence and specific molecular targeting in vivo.

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“…d-Ala is structural component of bacterial cell membranes [140] [141] and is a possible indicator of bacterial contamination, heat treatment, and shelf life of fruit juices and other foods [22] [105]. It can also be used in studies of molecular imaging [142], to induce cytotoxic oxidative stress in brain tumor cells [143], and to treat schizophrenia [144]. Changes in d-Ala content of the rat pancreas are related to their diurnal and nocturnal (circadian) habits [145].…”

Section: 4mentioning

confidence: 99%

Origin, Microbiology, Nutrition, and Pharmacology of D‐Amino Acids

Friedman

2010

Chemistry & Biodiversity

158

108

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Exposure of food proteins to certain processing conditions induces two major chemical changes: racemization of all L-amino acids (LAAs) to D-amino acids (DAAs) and concurrent formation of cross-linked amino acids such as lysinoalanine (LAL). The diet contains both processing-induced and naturally-formed DAA. The latter include those found in microorganisms, plants, and marine invertebrates. Racemization impairs digestibility and nutritional quality. Racemization of LAA residues to their D-isomers in food and other proteins is pH-, time-, and temperature-dependent. Although racemization rates of LAA residues in a protein vary, relative rates in different proteins are similar. The nutritional utilization of different DAAs varies widely in animals and humans. Some DAAs may exert both adverse and beneficial biological effects. Thus, although D-Phe is utilized as a nutritional source of L-Phe, high concentrations of D-Tyr in such diets inhibit the growth of mice. Both D-Ser and LAL induce histological changes in the rat kidney. The wide variation in the utilization of DAAs is illustrated by the fact that, whereas D-Meth is largely utilized as a nutritional source of the L-isomer, D-Lys is not. Similarly, although L-CysSH has a sparing effect on L-Meth when fed to mice, D-CysSH does not. Since DAAs are consumed as part of their normal diet, a need exists to develop a better understanding of their roles in foods, microbiology, nutrition, and medicine. To contribute to this effort, this overview surveys our present knowledge of the chemistry, nutrition, safety, microbiology, and pharmacology of DAAs. Also covered are the origin and distribution of DAAs in food and possible roles of DAAs in human physiology, aging, and the etiology and therapy of human diseases.

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Transport of d-[1-14C]-amino acids into Chinese hamster ovary (CHO-K1) cells: implications for use of labeled d-amino acids as molecular imaging agents

Cited by 9 publications

References 42 publications

Homocysteine transport by systems L, A and y⁺L across the microvillous plasma membrane of human placenta

Homocysteine transport by systems L, A and y⁺L across the microvillous plasma membrane of human placenta

A Biocompatible in Vivo Ligation Reaction and Its Application for Noninvasive Bioluminescent Imaging of Protease Activity in Living Mice

Origin, Microbiology, Nutrition, and Pharmacology of D‐Amino Acids

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Transport of d-[1-14C]-amino acids into Chinese hamster ovary (CHO-K1) cells: implications for use of labeled d-amino acids as molecular imaging agents

Cited by 9 publications

References 42 publications

Homocysteine transport by systems L, A and y+L across the microvillous plasma membrane of human placenta

Homocysteine transport by systems L, A and y+L across the microvillous plasma membrane of human placenta

A Biocompatible in Vivo Ligation Reaction and Its Application for Noninvasive Bioluminescent Imaging of Protease Activity in Living Mice

Origin, Microbiology, Nutrition, and Pharmacology of D‐Amino Acids

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Homocysteine transport by systems L, A and y⁺L across the microvillous plasma membrane of human placenta

Homocysteine transport by systems L, A and y⁺L across the microvillous plasma membrane of human placenta