Amino acid analysis of sub-picomolar amounts of proteins by precolumn fluorescence derivatization with 6-aminoquinolyl-&lt;i&gt;N&lt;/i&gt;-hydroxysuccinimidyl carbamate

Masuda, Akira; Dohmae, Naoshi

doi:10.5582/bst.2011.v5.6.231

Cited by 23 publications

(26 citation statements)

References 25 publications

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“…FMOC amino acids have been reported to be stable. 68 Other fluorescent reagents for precolumn derivatization such as o -phthaldialdehyde (OPA) and 7-fluoro-4-nitrobenzo-2-oxa-1,3-diazol (NBD-F) have been reported to form unstable amino acid adducts. 68 The derivatization of standards was performed in autosampler vials.…”

Section: Methodsmentioning

confidence: 99%

d-Amino Acid Levels in Perfused Mouse Brain Tissue and Blood: A Comparative Study

Weatherly

Parpia

et al. 2017

ACS Chem. Neurosci.

104

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The L-enantiomer is the predominant type of amino acid in all living systems. However, D-amino acids, once thought to be “unnatural”, have been found to be indigenous even in mammalian systems and increasingly appear to be functioning in essential biological and neurological roles. Both D- and L-amino acid levels in the hippocampus, cortex, and blood samples from NIH Swiss mice are reported. Perfused brain tissues were analyzed for the first time, thereby eliminating artifacts due to endogenous blood, and decreased the mouse-to-mouse variability in amino acid levels. Total amino acid levels (L-plus D-enantiomers) in brain tissue are up to 10 times higher than in blood. However, all measured D-amino acid levels in brain tissue are typically ~10 to 2000 times higher than blood levels. There was a 13% reduction in almost all measured D-amino acid levels in the cortex compared to those in the hippocampus. There is an approximate inverse relationship between the prevalence of an amino acid and the percentage of its D-enantiomeric form. Interestingly, glutamic acid, unlike all other amino acids, had no quantifiable level of its D-antipode. The bioneurological reason for the unique and conspicuous absence/removal of this D-amino acid is yet unknown. However, results suggest that D-glutamate metabolism is likely a unidirectional process and not a cycle, as per the L-glutamate/glutamine cycle. The results suggest that there might be unreported D-amino acid racemases in mammalian brains. The regulation and function of specific other D-amino acids are discussed.

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Section: Methodsmentioning

confidence: 99%

d-Amino Acid Levels in Perfused Mouse Brain Tissue and Blood: A Comparative Study

Weatherly

Parpia

et al. 2017

ACS Chem. Neurosci.

104

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“…Seventeen amino acids were determined comprising of Hyp, Asp, Ser, Glu, Gly, Arg, Thr, Ala, Pro, Cys, Tyr, Val, Met, Lys, Ile, Leu and Phe. However, acid hydrolysis process that was conducted at a very high temperature in an extensive period of time had partially destroyed the Cys (Bartolomeo & Maisano, 2006;Masuda & Dohmae, 2011). As a result, His and Cys were excluded, thus making the total number of variables that contributed for gelatin differentiation was 16.…”

Section: Chromatographymentioning

confidence: 99%

RP-HPLC method using 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate incorporated with normalization technique in principal component analysis to differentiate the bovine, porcine and fish gelatins

et al. 2015

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“…The 6-aminoquinolyl-Nhydroxysuccinimidyl carbamate amino acids were separated by ionpair chromatography on a C18 reversed-phase column (InertSustain C18HP, 3.0 mm [ID] × 250 mm, 3 μm; GL Sciences, Tokyo, Japan). Both a laser-induced fluorescence detector (LIF726; GL Sciences) and a fluorescence detector with Xe flush lamp (G1321A; Agilent Technologies, Santa Clara, CA) were used to reveal the existence of monomethylated Lys [35,36].…”

Section: Amino Acid Analysismentioning

confidence: 99%

The Histone Methyltransferase SMYD2 Methylates PARP1 and Promotes Poly(ADP-ribosyl)ation Activity in Cancer Cells

et al. 2014

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Poly(ADP-ribose) polymerase-1 (PARP1) catalyzes the poly(ADP-ribosyl)ation of protein acceptors using NAD(+) as the substrate is now considered as an important target for development of anticancer therapy. PARP1 is known to be post-translationally modified in various ways including phosphorylation and ubiquitination, but the physiological role of PARP1 methylation is not well understood. Herein we demonstrated that the histone methyltransferase SMYD2, which plays critical roles in human carcinogenesis, mono-methylated PARP1. We confirmed lysine 528 to be a target of SMYD2-dependent PARP1 methylation by LC-MS/MS and Edman Degradation analyses. Importantly, methylated PARP1 revealed enhanced poly(ADP-ribose) formation after oxidative stress, and positively regulated the poly(ADP-ribosyl)ation activity of PARP1. Hence, our study unveils a novel mechanism of PARP1 in human cancer through its methylation by SMYD2.

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Amino acid analysis of sub-picomolar amounts of proteins by precolumn fluorescence derivatization with 6-aminoquinolyl-<i>N</i>-hydroxysuccinimidyl carbamate

Cited by 23 publications

References 25 publications

d-Amino Acid Levels in Perfused Mouse Brain Tissue and Blood: A Comparative Study

d-Amino Acid Levels in Perfused Mouse Brain Tissue and Blood: A Comparative Study

RP-HPLC method using 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate incorporated with normalization technique in principal component analysis to differentiate the bovine, porcine and fish gelatins

The Histone Methyltransferase SMYD2 Methylates PARP1 and Promotes Poly(ADP-ribosyl)ation Activity in Cancer Cells

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