A simple, rapid and sensitive high-performance liquid chromatography method with electrochemical detection was developed for the determination of glucosamine in human plasma. Plasma samples were analyzed after a simple two-step procedure of protein precipitation with subsequent dilution. The chromatographic separation was performed on a Carbopack column (3 mm x 150 mm) with a mobile phase consisting of water and 200 mM sodium hydroxide. Detection was performed electrochemically in a pulsed voltammetry mode. The limit of detection was 2.0 ng/ml, inter- and intra-day precision were less than 10%. The method was successfully applied to the investigation of the pharmacokinetics of glucosamine in healthy man volunteers.
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http://dx.doi.org/10.1016/j.jpba.2009.01.031 | DOI Listing |
Cells
January 2025
Key Laboratory of Resource Biology and Biotechnology Western China, Ministry of Education, Provincial Key Laboratory of Biotechnology, College of Life Sciences, Northwest University, Xi'an 710069, China.
Glycosylation plays a critical role in various biological processes, yet identifying specific glycosyltransferase substrates remains a challenge due to the complexity of glycosylation. Here, we employ proximity labeling with biotin ligases BASU and TurboID to map the proximitome of MGAT3, a glycosyltransferase responsible for the biosynthesis of the bisecting GlcNAc structure, in HEK293T cells. This approach enriched 116 and 189 proteins, respectively, identifying 17 common substrates shared with bisecting GlcNAc-bearing proteome obtained via intact glycopeptide enrichment methods.
View Article and Find Full Text PDFStem Cell Res Ther
January 2025
Key Laboratory of Resource Biology and Biotechnology in Western China, Provincial Key Laboratory of Biotechnology, College of Life Sciences, Ministry of Education, Northwest University, Xi'an, China.
Background: The senescence of bone marrow mesenchymal stem cells (BMMSCs) is increasingly recognized as a critical factor contributing to the pathophysiology of age-related diseases. Recent studies suggest that small extracellular vesicles (sEVs) derived from the serum of elderly individuals may play a pivotal role in promoting BMMSC senescence. Glycoprotein non-metastatic melanoma protein B (GPNMB), a type I transmembrane glycoprotein, is upregulated during cellular senescence and can regulate stem cell ageing.
View Article and Find Full Text PDFCell Commun Signal
January 2025
Key Laboratory of Resource Biology and Biotechnology in Western China, Ministry of Education, Provincial Key Laboratory of Biotechnology, College of Life Sciences, Northwest University, 229 Taibai North Road, Xi'an, Shaanxi, 710069, P. R. China.
Background: Cancer-associated fibroblasts (CAFs) are a pivotal component of the tumor microenvironment (TME), playing key roles in tumor initiation, metastasis, and chemoresistance. While glycosylation is known to regulate various cellular processes, its impact on CAFs activation remains insufficiently explored.
Methods: We assessed the correlation between bisecting GlcNAc levels and CAFs markers (α-SMA, PDGFRA, PDGFRB) in breast cancer tissues.
Scientifica (Cairo)
January 2025
Department of Food and Nutritional Sciences, Graduate School of Humanities and Sciences, Ochanomizu University, Tokyo 1128610, Japan.
Although glucosamine (GlcN) exhibits antitumor effects, its mechanism of action remains controversial. Additionally, its impact on hepatocellular carcinoma (HCC) is not well understood. This study aimed to investigate the antitumor effects of GlcN and its underlying mechanism in a mouse HCC cell line, Hepa1-6.
View Article and Find Full Text PDFCarbohydr Res
March 2025
Department of Molecular Biochemistry, Nagoya University Graduate School of Medicine, 65 Tsurumai-Cho, Showa-Ku, Nagoya, Aichi, 466-8550, Japan; Institute for Glyco-core Research (iGCORE), Nagoya University, Furo-Cho, Chikusa-Ku, Nagoya, Aichi, 464-8601, Japan. Electronic address:
Extracellular O-GlcNAc is a unique post-translational modification that occurs in the epidermal growth factor-like (EGF) domain of the endoplasmic reticulum (ER) lumen. The EGF domain-specific O-GlcNAc transferase (EOGT), catalyzes the transfer of O-GlcNAc to serine/threonine residues of the C-terminal EGF domain. Thus, EOGT-dependent O-GlcNAc modifications are mainly found in selective proteins that are localized in the extracellular spaces or extracellular regions of membrane proteins.
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