Syntheses of lactosyl ceramide analogues carrying novel bifunctional BODIPY dyes directed towards the differential analysis of multiplexed glycosphingolipids by MS/MS using iTRAQ

Son, Sang-Hyun; Daikoku, Shusaku; Ohtake, Atsuko; Suzuki, Katsuhiko; Kabayama, Kazuya; Ito, Yukishige; Kanie, Osamu

doi:10.1039/c4cc00112e

Cited by 16 publications

(30 citation statements)

References 18 publications

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“…This alkyne compound was coupled with a bifunctional BODYPY dye carrying an azide group by using copper sulfate to give 11 (quantitative). After activation to the succinimidyl ester ( 12 ), this was coupled with Man 9 GlcNAc 2 ‐Gly‐NH 2 to produce 8 (Scheme ).…”

Section: Resultsmentioning

confidence: 99%

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Endoplasmic Reticulum (ER)‐Targeted, Galectin‐Mediated Retrograde Transport by Using a HaloTag Carrier Protein

et al. 2016

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Investigations into metabolic processes within the cell have often relied on genetic methods such as forced expression and knockout or knockdown techniques. An alternative approach would be introducing a molecule into the desired location inside the cell. To translocate compounds from outside cells into the endoplasmic reticulum (ER), we constructed a delivery carrier protein. This comprised N-terminal galectin-1 for cell-surface binding (G1), a protease cleavable sequence (ps), a HaloTag domain for attaching exogenous compounds (Halo), and a C-terminal KDEL sequence for ER retention. Fluorescently labeled G1-ps-Halo-KDEL passed through the Golgi apparatus and reached the ER. By using Man9 GlcNAc2 -BODIPY as a cargo compound, the carrier protein was also delivered into the ER with concomitant processing of mannose to Man5,6, by the ER-resident α1,2-mannosidase. G1-ps-Halo-KDEL might serve as a new type of delivery carrier protein to direct compounds into the ER.

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Section: Resultsmentioning

confidence: 99%

“…Medium‐pressure liquid column chromatography purifications were performed on a Combi Flash Rf (Teledyne Isco, Lincoln NE). Bifunctional BODIPY dye and Man 9 GluNAc 2 ‐Gly‐NH 2 were prepared as previously reported.…”

Section: Methodsmentioning

confidence: 99%

Endoplasmic Reticulum (ER)‐Targeted, Galectin‐Mediated Retrograde Transport by Using a HaloTag Carrier Protein

et al. 2016

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“…In this respect, BODIPY-labelled LacCer -where the BODIPY dye is attached in place of N-fatty acyl -has been developed as a mimic to the endogenous LacCer and in this way its metabolism in vivo can be traced by fluorescence technique [197,198]. To facilitate quantification, Son and co-workers [199] developed a strategy to add isobaric tags to the fluorophore using click chemistry. Briefly, an azide functional group was first introduced to BODIPY, which serves as an achor for successful attachment of iTRAQ™.…”

Section: Isobaric Labelingmentioning

confidence: 99%

Recent advances in the mass spectrometric analysis of glycosphingolipidome – A review

Barrientos

Zhang

2020

Analytica Chimica Acta

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Aberrant expression of glycosphingolipids has been implicated in a myriad of diseases, but our understanding of the strucural diversity, spatial distribution, and biological function of this class of biomolecules remains limited. These challenges partly stem from a lack of sensitive tools that can detect, identify, and quantify glycosphingolipids at the molecular level. Mass spectrometry has emerged as a powerful tool poised to address most of these challenges. Here, we review the recent developments in analytical glycosphingolipidomics with an emphasis on sample preparation, mass spectrometry and tandem mass spectrometry-based structural characterization, label-free and labeling-based quantification. We also discuss the nomenclature of glycosphingolipids, and emerging technologies like ion mobility spectrometry in differentiation of glycosphingolipid isomers. The intrinsic advantages and shortcomings of each method are carefully critiqued in line with an individual's research goals. Finally, future perspectives on analytical sphingolipidomics are stated, including a need for novel and more sensive methods in isomer separation, low abundance species detection, and profiling the spatial distribution of glycosphingolipid molecular species in cells and tissues using imaging mass spectrometry.

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“…We previously constructed a system to spatio-temporally analyze glycolipid metabolism using LacCer-BODIPY (13-15). We used this exogenous glycolipid probe to perform a detailed time-lapse analysis of the recycling pathway.…”

Section: Introductionmentioning

confidence: 99%

Temporal analysis of localization and trafficking of glycolipids

Arai

Kabayama

Kanie

et al. 2020

Preprint

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Glycolipid metabolism occurs in the Golgi apparatus, but the detailed mechanisms have not yet been elucidated. We used fluorescently labeled glycolipids to analyze glycolipid composition and localization changes and shed light on glycolipid metabolism. In a previous study, the fatty chain of lactosyl ceramide was fluorescently labeled with BODIPY (LacCer-BODIPY) before being introduced into cultured cells to analyze the cell membrane glycolipid recycling process. However, imaging analysis of glycolipid recycling is complicated because of limited spatial resolution. Therefore, we examined the microscopic conditions that allow the temporal analysis of LacCer-BODIPY trafficking and localization. We observed that the glycolipid fluorescent probe migrated from the cell membrane to intracellular organelles before returning to the cell membrane. We used confocal microscopy to observe co-localization of the glycolipid probe with endosomes and Golgi markers, demonstrating that it recycles mainly through the trans-Golgi network (TGN). Here, a glycolipid recycling pathway was observed that did not require the lipids to pass through the lysosome.

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Syntheses of lactosyl ceramide analogues carrying novel bifunctional BODIPY dyes directed towards the differential analysis of multiplexed glycosphingolipids by MS/MS using iTRAQ

Cited by 16 publications

References 18 publications

Endoplasmic Reticulum (ER)‐Targeted, Galectin‐Mediated Retrograde Transport by Using a HaloTag Carrier Protein

Endoplasmic Reticulum (ER)‐Targeted, Galectin‐Mediated Retrograde Transport by Using a HaloTag Carrier Protein

Recent advances in the mass spectrometric analysis of glycosphingolipidome – A review

Temporal analysis of localization and trafficking of glycolipids

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