• Mass Spectrometry Letters
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• v.3 no.2
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• pp.39-42
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• 2012

Phosphorylation and glycosylation are two of the most important and widespread post-translational modifications (PTMs) in an organism. Proteomics analysis of the PTMs has been challenged by low stoichiometry of the modified proteins and suppression effects by high abundance proteins, typically no-functional house-keeping proteins. In this study, a novel method was applied for not only isolating PTM peptides from intact peptides but also concurrently characterizing of glyco- and phosphoproteome using electrostatic repulsion hydrophilic interaction chromatography (ERLIC) packed with silica coated by crosslinked polyethyleneimine. For 2 mg tryptic digest of mouse proteome of epicardial adipose tissue with fat diet, 802 N-glycosylated peptides of 316 glycoproteins and 159 phosphorylated peptides of 75 phosphoproteins were identified using HPLC chip/quadrupole time-of-flight (Q-OF) tandem mass spectrometer.

• Journal of Applied Biological Chemistry
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• v.66
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• pp.338-344
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• 2023

Curcuma longa is a plant belonging to the genus Curcuma and is distributed across various Asian regions. This plant is widely known for its rhizomes, which possess a variety of pharmacological properties. However, although the leaves and stems of this plant also contain several health-promoting secondary metabolites, very few studies have characterized these compounds. Therefore, our study sought to quantify the secondary metabolites from the leaves and stems of Curcuma longa L. (LSCL) using liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS) and high-performance liquid chromatography (HPLC). Our LC-ESI-MS analyses detected twenty-one phenolic compounds in the LSCL, among which fifteen compounds were detected via HPLC analysis. Four compounds, namely vanillic acid (0.129 mg/g), p-coumaric acid (0.431 mg/g), 4-methylcatechol (0.199 mg/g), and afzelin (0.074 mg/g) were then quantified. These findings suggest that LSCL is rich in secondary metabolites and holds potential as a valuable resource for the development of functional and nutritional supplements in the future.

• Toxicological Research
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• v.33 no.1
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• pp.63-69
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• 2017

Transmembrane protein 39A (TMEM39A) belongs to the TMEM39 family. TMEM39A gene is a susceptibility locus for multiple sclerosis. In addition, TMEM39A seems to be implicated in systemic lupus erythematosus. However, any possible involvement of TMEM39A in cancer remains largely unknown. In the present report, we provide evidence that TMEM39A may play a role in brain tumors. Western blotting using an anti-TMEM39A antibody indicated that TMEM39A was overexpressed in glioblastoma cell lines, including U87-MG and U251-MG. Deep-sequencing transcriptomic profiling of U87-MG and U251-MG cells revealed that TMEM39A transcripts were upregulated in such cells compared with those of the cerebral cortex. Confocal microscopic analysis of U251-MG cells stained with anti-TMEM39A antibody showed that TMEM39A was located in dot-like structures lying close to the nucleus. TMEM39A probably located to mitochondria or to endosomes. Immunohistochemical analysis of glioma tissue specimens indicated that TMEM39A was markedly upregulated in such samples. Bioinformatic analysis of the Rembrandt knowledge base also supported upregulation of TMEM39A mRNA levels in glioma patients. Together, the results afford strong evidence that TMEM39A is upregulated in glioma cell lines and glioma tissue specimens. Therefore, TMEM39A may serve as a novel diagnostic marker of, and a therapeutic target for, gliomas and other cancers.