1.Response: The Association between Serum Endogenous Secretory Receptor for Advanced Glycation End Products and Vertebral Fractures in Type 2 Diabetes (Endocrinol Metab 2012;27:289-94, Cheol Ho Lee et al.).
Cheol Ho LEE ; Min Kyung LEE ; Hyun Jeong HAN ; Tae Ho KIM ; Jae Hyuk LEE ; Se Hwa KIM
Endocrinology and Metabolism 2013;28(1):78-79
No abstract available.
Glycosylation End Products, Advanced
2.Letter: The Association between Serum Endogenous Secretory Receptor for Advanced Glycation End Products and Vertebral Fractures in Type 2 Diabetes (Endocrinol Metab 2012;27:289-94, Cheol Ho Lee et al.).
Endocrinology and Metabolism 2013;28(1):76-77
No abstract available.
Glycosylation End Products, Advanced
3.Chemical approaches for the stereocontrolled synthesis of 1,2-cis-β-D-rhamnosides.
Juntao CAI ; Xin YUAN ; Yuanfang KONG ; Yulong HU ; Jieming LI ; Shiqing JIANG ; Chunhong DONG ; Kan DING
Chinese Journal of Natural Medicines (English Ed.) 2023;21(12):886-901
In carbohydrate chemistry, the stereoselective synthesis of 1,2-cis-glycosides remains a formidable challenge. This complexity is comparable to the synthesis of 1,2-cis-β-D-mannosides, primarily due to the adverse anomeric and Δ-2 effects. Over the past decades, to attain β-stereoselectivity in D-rhamnosylation, researchers have devised numerous direct and indirect methodologies, including the hydrogen-bond-mediated aglycone delivery (HAD) method, the synthesis of β-D-mannoside paired with C6 deoxygenation, and the combined approach of 1,2-trans-glycosylation and C2 epimerization. This review elaborates on the advancements in β-D-rhamnosylation and its implications for the total synthesis of tiacumicin B and other physiologically relevant glycans.
Glycosides
;
Mannosides
;
Glycosylation
;
Stereoisomerism
4.Glyceraldehyde-Derived Advanced Glycation End Products Accumulate Faster Than N(ε)-(Carboxymethyl) Lysine.
Mami YOKOTA ; Marie SEKITA ; Yuri OKANO ; Hitoshi MASAKI ; Masayoshi TAKEUCHI ; Yoshihiro TOKUDOME
Annals of Dermatology 2017;29(4):508-511
No abstract available.
Glycosylation End Products, Advanced*
;
Lysine*
5.Rapid N-glycosylation profiling of glycoprotein based on ultrafiltration-devices.
Cai TIE ; Ting HU ; Jin-lan ZHANG
Acta Pharmaceutica Sinica 2015;50(6):755-759
With development of bio-technique, more and more proteins were applied as clinical approaches. However, the protein homogeneity, especially the N-glycosylation limited the further research and application of these protein drugs. The analysis method for N-glycans is believed to be critical in protein drugs development. To enhance the N-glycans isolation efficiency and accelerate the pretreatment, a new strategy was built on ultrafiltration-devices. New methods increased the isolation efficiency of N-glycans containing N-acetylglucosa mine with 10%-20%. The degrading of N-glycans containing sialic acids was also minimized with this method. 20%-100% more N-glycans with sialic acids were isolated. The pretreatment was finished within 30 min. Coupled with HPLC-HRMS, an effective and reliable strategy designed for protein drugs N-glycans analysis were developed.
Glycoproteins
;
chemistry
;
Glycosylation
;
Polysaccharides
;
chemistry
;
Ultrafiltration
;
instrumentation
6.Mac-2 Binding Protein Glycosylation Isomer: Emerging Non-Invasive Serum Marker for Liver Fibrosis.
Annals of Laboratory Medicine 2018;38(4):289-290
No abstract available.
Biomarkers*
;
Carrier Proteins*
;
Glycosylation*
;
Liver Cirrhosis*
;
Liver*
7.Advances in the diagnosis and treatment of phosphomannomutase 2 deficiency.
Chinese Journal of Contemporary Pediatrics 2023;25(2):223-228
Phosphomannomutase 2 deficiency is the most common form of N-glycosylation disorders and is also known as phosphomannomutase 2-congenital disorder of glycosylation (PMM2-CDG). It is an autosomal recessive disease with multi-system involvements and is caused by mutations in the PMM2 gene (OMIM: 601785), with varying severities in individuals. At present, there is still no specific therapy for PMM2-CDG, and early identification, early diagnosis, and early treatment can effectively prolong the life span of pediatric patients. This article reviews the advances in the diagnosis and treatment of PMM2-CDG.
Humans
;
Child
;
Congenital Disorders of Glycosylation/therapy*
;
Mutation
8.Engineering the 182 site of cyclodextrin glucosyltransferase for glycosylated genistein synthesis.
Baocheng CHAI ; Yulin JIANG ; Ye NI ; Ruizhi HAN
Chinese Journal of Biotechnology 2022;38(2):749-759
Genistein and its monoglucoside derivatives play important roles in food and pharmaceuticals fields, whereas their applications are limited by the low water solubility. Glycosylation is regarded as one of the effective approaches to improve water solubility. In this paper, the glycosylation of sophoricoside (genistein monoglucoside) was investigated using a cyclodextrin glucosyltransferase from Penibacillus macerans (PmCGTase). Saturation mutagenesis of D182 from PmCGTase was carried out. Compared with the wild-type (WT), the variant D182C showed a 13.42% higher conversion ratio. Moreover, the main products sophoricoside monoglucoside, sophoricoside diglucoside, and sophoricoside triglucoside of the variant D182C increased by 39.35%, 56.05% and 64.81% compared with that of the WT, respectively. Enzymatic characterization showed that the enzyme activities (cyclization, hydrolysis, disproportionation) of the variant D182C were higher than that of the WT, and the optimal pH and temperature of the variant D182C were 6 and 40℃, respectively. Kinetics analysis showed the variant D182C has a lower Km value and a higher kcat/Km value than that of the WT, indicating the variant D182C has enhanced affinity to substrate. Structure modeling and docking analysis demonstrated that the improved glycosylation efficiency of the variant D182C may be attributed to the increased interactions between residues and substrate.
Cyclodextrins
;
Genistein
;
Glucosyltransferases/metabolism*
;
Glycosylation
;
Kinetics
9.Identification of the glycosylation sites of Opsin3 and its glycosylation modification function.
Zhongjing LIU ; Li QIAO ; Zhaoyang YE ; Wenxiu YANG
Chinese Journal of Biotechnology 2022;38(3):1173-1182
Opsin3 (OPN3) is a photoreceptor membrane protein with a typical seven-alpha helical transmembrane structure that belongs to the G-protein-coupled receptor (GPCR) superfamily and is widely expressed in brain. In recent years, it has been reported that OPN3 is also highly expressed in adipose tissue, and the protein is associated with the production of skin melanin. We found that the N82 site is the glycosylation site of OPN3. SNAP-tagTM has diverse functions and can be applied to a variety of different studies. By constructing a SNAP-tagged OPN3 recombinant protein, the distribution position of SNAP-OPN3 in cells can be clearly observed by fluorescence confocal microscopy using SNAP-Surface® 549 and SNAP-Cell® OregonGreen®, which provides a new method for studying the function of OPN3. It also shows that SNAP-tag does not affect the function of OPN3. Using the SNAP tag we found that OPN3 cannot be taken up to the cell membrane after glycosylation site mutation.
Cell Membrane
;
Glycosylation
;
Melanins
;
Membrane Proteins
;
Skin
10.Application of StrucGP in medical immunology: site-specific N-glycoproteomic analysis of macrophages.
Pengfei LI ; Zexuan CHEN ; Shanshan YOU ; Yintai XU ; Zhifang HAO ; Didi LIU ; Jiechen SHEN ; Bojing ZHU ; Wei DAN ; Shisheng SUN
Frontiers of Medicine 2023;17(2):304-316
The structure of N-glycans on specific proteins can regulate innate and adaptive immunity via sensing environmental signals. Meanwhile, the structural diversity of N-glycans poses analytical challenges that limit the exploration of specific glycosylation functions. In this work, we used THP-1-derived macrophages as examples to show the vast potential of a N-glycan structural interpretation tool StrucGP in N-glycoproteomic analysis. The intact glycopeptides of macrophages were enriched and analyzed using mass spectrometry (MS)-based glycoproteomic approaches, followed by the large-scale mapping of site-specific glycan structures via StrucGP. Results revealed that bisected GlcNAc, core fucosylated, and sialylated glycans (e.g., HexNAc4Hex5Fuc1Neu5Ac1, N4H5F1S1) were increased in M1 and M2 macrophages, especially in the latter. The findings indicated that these structures may be closely related to macrophage polarization. In addition, a high level of glycosylated PD-L1 was observed in M1 macrophages, and the LacNAc moiety was detected at Asn-192 and Asn-200 of PD-L1, and Asn-200 contained Lewis epitopes. The precision structural interpretation of site-specific glycans and subsequent intervention of target glycoproteins and related glycosyltransferases are of great value for the development of new diagnostic and therapeutic approaches for different diseases.
Humans
;
B7-H1 Antigen
;
Glycosylation
;
Polysaccharides/metabolism*