Yu Torizuka, Shogo Nakamura, Hitoshi Tsugawa, Hidekazu Suzuki, Toshinori Sato
{"title":"Mechanism analysis of transgene expression induced by chitosan/hyaluronic acid nanoparticles in CD44v9/RHAMM co-expressed gastric cancer cells: contribution of hyaluronic acid to RHAMM-mediated intracellular transport.","authors":"Yu Torizuka, Shogo Nakamura, Hitoshi Tsugawa, Hidekazu Suzuki, Toshinori Sato","doi":"10.1007/s10719-026-10218-0","DOIUrl":"10.1007/s10719-026-10218-0","url":null,"abstract":"<p><p>Optimizing non-viral vectors for gene therapy requires elucidating the molecular mechanisms underlying vector uptake and intracellular delivery. In this study, cell transfection using pDNA/polysaccharide complexes was investigated to develop a gene delivery system specific for gastric tumor cells that express hyaluronic acid (HA) receptors such as CD44 variant 9 (CD44v9) and receptor for hyaluronan-mediated motility (RHAMM). pDNA/chitosan/HA complexes showed specific transgene expression activity in CD44v9(+) cells, mediated by CD44v9-dependent cell uptake and microtubule-dependent transport. Particularly, RHAMM was involved in intracellular transport of pDNA/chitosan/HA complexes. We demonstrated that HA drives CD44v9-mediated internalization, RHAMM-mediated, and microtubule-dependent intracellular transport, which are essential for enhanced pDNA complex-driven gene expression in gastric cancer cells co-expressing CD44v9 and RHAMM.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"43 1","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-05-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147959682","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Łukasz F Sobala, Katarzyna Szymczak-Kulus, Łukasz Kasper, Marta Kasper, Radoslaw Kaczmarek, Marcin Czerwinski
{"title":"Alpha-Gal syndrome unveiled: decoding the glycan-driven red meat allergy.","authors":"Łukasz F Sobala, Katarzyna Szymczak-Kulus, Łukasz Kasper, Marta Kasper, Radoslaw Kaczmarek, Marcin Czerwinski","doi":"10.1007/s10719-026-10215-3","DOIUrl":"10.1007/s10719-026-10215-3","url":null,"abstract":"<p><p>α-Gal syndrome (AGS) is a type of allergy to red meat and other mammalian products that develops after a tick bite. Symptoms may include urticaria, angioedema, gastrointestinal and respiratory symptoms, and, most dangerously, anaphylactic shock. Among food allergies, it is considered unusual because: (i) the major allergen is not a protein, but a carbohydrate moiety Galα-1,3-Gal, which humans do not synthesize; (ii) it is caused by α-Gal-containing glycoconjugates injected during a tick bite; (iii) the hypersensitivity is effected by IgE antibodies which arise after a class switch from IgG and IgM-class antibodies; (iv) it seems to be triggered by α-Gal-containing glycolipids present in red meat, with delayed onset. Here, we evaluate glycans that may cause AGS, review the data about glycosyltransferases that synthesize α-Gal and related antigens and describe the immune mechanism behind AGS: sensitization and host response to ticks' saliva. In addition, we consider future research avenues that may lead to a better understanding and management of AGS as a modern dietary affliction rooted in an old evolutionary trade-off.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"43 1","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-05-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147940898","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Peter Chinedu Agu, Patrick Maduabuchi Aja, Boniface Anthony Ale, Kehinde Ross, Jun Lu
{"title":"Conceptual and Mechanistic Links between glycated hemoglobin and glycosylated RNA: An insight into glycosylation biology in metabolic disease pathophysiology.","authors":"Peter Chinedu Agu, Patrick Maduabuchi Aja, Boniface Anthony Ale, Kehinde Ross, Jun Lu","doi":"10.1007/s10719-026-10217-1","DOIUrl":"10.1007/s10719-026-10217-1","url":null,"abstract":"<p><p>Glycated hemoglobin (HbA1c) is a well-established biomarker reflecting chronic glycemic control in diabetes. It accumulates through non-enzymatic glycation of hemoglobin under sustained hyperglycemia and serves as a surrogate of metabolic memory. Emerging in parallel, glycosylated RNA (glycoRNA), small noncoding RNAs bearing covalently attached N-linked glycans, has revealed unexpected roles in immune signaling and glycoimmunomodulation. While glycation and glycosylation represent distinct biochemical processes, both are modulated by glucose availability and cellular stress. This opinion paper aimed to explore the conceptual parallels between HbA1c and glycoRNA, proposing that hyperglycemia-induced metabolic changes may simultaneously influence both processes. In light of these, glycoRNA represents an emerging biomarker as a functional effector in metabolic disease, mirroring the hyperglycemia-driven immunological dimensions of HbA1c with a further advantage of a defined metabolic sequence, which can deepen diagnostics towards disease progression patterns. Though direct experimental evidence is currently limited, we outline plausible mechanistic intersections and suggest methodological frameworks for future research. Therefore, this perspective aims to stimulate interdisciplinary investigation into glycoRNA biology within the broader context of glycemic dysregulation and immune modulation in diabetes.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"43 1","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-05-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147928537","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Waliza Ansar, Sumi Mukhopadhyay, S K Hasan Habib, Shyamasree Basu, Bibhuti Saha, Asish Kumar Sen, C N Mandal, Chitra Mandal
{"title":"Editorial Expression of Concern: Disease-associated glycosylated molecular variants of human C-reactive protein activate complement-mediated hemolysis of erythrocytes in tuberculosis and Indian visceral leishmaniasis.","authors":"Waliza Ansar, Sumi Mukhopadhyay, S K Hasan Habib, Shyamasree Basu, Bibhuti Saha, Asish Kumar Sen, C N Mandal, Chitra Mandal","doi":"10.1007/s10719-026-10214-4","DOIUrl":"https://doi.org/10.1007/s10719-026-10214-4","url":null,"abstract":"","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"43 1","pages":""},"PeriodicalIF":3.1,"publicationDate":"2026-04-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147769575","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Huiai Lu, Yuanyuan Liu, Yi Wang, Jiajing Lin, Liming Cheng, Xin Liu, Si Liu, At
{"title":"N-glycan signatures of immunoglobulins-depleted serum proteins in colorectal cancer.","authors":"Huiai Lu, Yuanyuan Liu, Yi Wang, Jiajing Lin, Liming Cheng, Xin Liu, Si Liu, At","doi":"10.1007/s10719-026-10216-2","DOIUrl":"10.1007/s10719-026-10216-2","url":null,"abstract":"<p><p>Protein glycosylation has been implicated in the pathogenesis of cancer, with colorectal cancer (CRC) strongly associated with serum N-glycosylation and IgG N-glycosylation. However, the N-glycosylation profile of non-immunoglobulin serum proteins (IgS-D) in CRC progression remains largely unexplored. Serum IgS-D was isolated using affinity chromatography, followed by the release of N-glycans, methylamidation, and MALDI-MS analysis. The potential of the IgS-D N-glycome profile to reflect CRC progression was assessed through Mann-Whitney U tests and multivariate analysis. A total of 43 distinct N-glycans were identified in IgS-D. Notably, a significant reduction in serum IgS-D mannosylated N-glycans was observed in CRC patients compared to healthy controls. Further analysis of individual N-glycans revealed significant differences and diagnostic potential in five specific N-glycans: H5N2 (AUC = 0.868), H6N2 (AUC = 0.73), H5N4S1 (AUC = 0.800), H5N5S1F1 (AUC = 0.713), and H5N4S2F1 (AUC = 0.689). A panel comprising these five N-glycans demonstrated high diagnostic accuracy for CRC (AUC = 0.924). The N-glycosylation profile of serum IgS-D is closely associated with CRC progression. Specific N-glycan signatures provide robust discrimination between CRC patients and healthy controls, warranting further investigation into the underlying molecular mechanisms.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"43 1","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-04-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147769658","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Albert M Wu, Tanuja Singh, Jia Hau Liu, Yung Liang Chen
{"title":"The structural units, recognition factors (RFs) and their codes of a LFuc Recognition Protein (FRP)<sup />.","authors":"Albert M Wu, Tanuja Singh, Jia Hau Liu, Yung Liang Chen","doi":"10.1007/s10719-025-10208-8","DOIUrl":"10.1007/s10719-025-10208-8","url":null,"abstract":"<p><p>Avidities and intensities of the Structural units, Glycotopes and their polyvalencies in the LFuc Recognition Protein (FRP)-glycan interactions have not been well defined and organized. This is due to the absence of the special glycan reagents and insufficient experiences. In this report, one of the best LFuc Recognition Proteins (FRPs) was analyzed by the enzyme-linked lectinosorbent and inhibition assays. From the data provided, it is found that the polyvalencies of the Fucα1→2Gal related structural units and their glycotopes are the dominant ones, especially these units of the human blood group H, Leb/Ley-tetra saccharide and AB-Leb/Ley-penta active glycans, but not the Lea/Lex-tri ligands and Man related units. When their intensities are expressed by Mass Relative Potency (Mass R.P.), it can be up to 5.0×105 fold higher than their key monomer (LFuc). In addition to this FRP can be a used as a powerful tool to detect the presence of the H, Leb/Ley-tetra and AB-Leb/Ley-penta glycotopes in the mammalian glycoconjugates, the theme of this report is the first constructive work of its structural units and codes for the LFuc Recognition Protein (FRP) system. It is expected to expand to reveal more others in the future.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"43 1","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-04-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147769679","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Jien-Lian Chen, Hsien-Wei Tseng, Chun-Cheng Lin, Chi-Kung Ni
{"title":"De novo determination of fucose linkages in N-glycans using logically derived sequence tandem mass spectrometry.","authors":"Jien-Lian Chen, Hsien-Wei Tseng, Chun-Cheng Lin, Chi-Kung Ni","doi":"10.1007/s10719-026-10213-5","DOIUrl":"10.1007/s10719-026-10213-5","url":null,"abstract":"<p><p>N-linked glycosylation is one of the most important post-translational modification of proteins. Fucosylated N-glycans are related to many biological processes and they are commonly used as biomarkers. However, determining fucose linkages in N-glycans remains challenging. Most of the fucose linkages, particularly the linkages in the antennas of N-glycans, remain unidentified. In this work, a simple multi-stage tandem mass spectrometry based on dissociation mechanisms, namely logically derived sequence tandem mass spectrometry, was developed for the de novo determination of fucose linkages in N-glycans. Using the N-glycans extracted from pine nuts, human milk, and bee venom, we demonstrated that fucose linkages in intact N-glycans, including the 1→3 or 1→6 linkage in the core and the linkage in the α(1→3) or α(1→6) antenna were identified. The procedure does not require the N-glycan standards, and the entire process is summarized in a flowchart for automation. The CID mass spectra acquired with low resolution linear ion trap mass spectrometer (peak width 0.3 Da) are very similar to those obtained with high resolution Orbitrap mass spectrometer (R = 100,000 FWHM at m/z 400), indicating that the choice of mass analyzer does not affect carbohydrate structural elucidation.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"43 1","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13099784/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147769562","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"GlycoRNA biology, a naive field with unlimited horizons.","authors":"Amit Ranjan, Rajesh Kumar Gupta","doi":"10.1007/s10719-026-10212-6","DOIUrl":"10.1007/s10719-026-10212-6","url":null,"abstract":"","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"43 1","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-03-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147467745","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Enhanced anti-proliferative activity of Jacalin, a plant lectin in combination with taxol in MDA-MB-468 triple-negative breast cancer cells.","authors":"Bommanaboina Anil Kumar, Thaslima B, Lavanya V, Shazia Jamal, Neesar Ahmed","doi":"10.1007/s10719-026-10210-8","DOIUrl":"10.1007/s10719-026-10210-8","url":null,"abstract":"<p><p>Plant lectins derived from a variety of plant sources can inhibit the proliferation of certain types of human cancer cells and have been studied extensively. In the present study, the effects of Jacalin, a Thomsen–Friedenreich disaccharide-binding lectin isolated from jackfruit seeds, on the triple-negative breast cancer (TNBC) cell line MDA-MB-468 was investigated in combination with Taxol. It was observed that Jacalin inhibited the proliferation of these cancer cells. The antiproliferative effect of Jacalin on MDA-MB-468 was found to be reversible. However, when Jacalin was removed from the cell culture after the treatment for the given time, the cancer cells recovered back and started proliferating again. Importantly, Jacalin has minimum effect on PBMCs proliferation taken as primary cell line control. Additionally, MDA-MB-468 cells were treated with a combination of Taxol (25 µM) and Jacalin (40 µg/mL). This shows that Jacalin and Taxol work better when used together, leading to a stronger inhibition in cancer cell growth. These results suggest that Jacalin shows in-vitro potential and requires further mechanistic and in-vivo evaluation before therapeutic relevance can be established.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"43 1","pages":""},"PeriodicalIF":3.0,"publicationDate":"2026-03-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147354568","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Salmon proteoglycan modulates TIMP-gelatinase regulation in intestinal epithelial cells.","authors":"Shintaro Hirasawa, Tomio Yabe","doi":"10.1007/s10719-026-10211-7","DOIUrl":"10.1007/s10719-026-10211-7","url":null,"abstract":"<p><p>Chondroitin sulfate (CS) and CS proteoglycans (CSPGs) are increasingly used in nutritional and biomedical applications. Although their functional benefits have traditionally been attributed to their translocation into the bloodstream after oral administration, their poor bioavailability, due to high molecular weight and strong negative charge, has prompted substantial debate. In this study, we examined the possibility that CS and CSPG act directly on intestinal epithelial cells, thereby providing an alternative explanation for their physiological effects under non-absorptive conditions. Differentiated Caco-2 cells (human enterocyte) were employed as an in vitro model of the intestinal epithelium. Administration of CS and CSPG modulated tissue inhibitor of metalloproteinase gene expression and altered gelatinase activity in the basolateral compartment. While the two glycans shared some overlapping actions, each also exerted distinct effects reflective of their structural features. These findings suggest that CS and CSPG directly modulate epithelial signaling and reshape the basement membrane microenvironment. Overall, this study suggests a mechanism by which CS/CSPG exerts physiological actions in the intestinal tract independent of systemic absorption, providing a new perspective on the functional outcomes of oral administration.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"43 1","pages":"11"},"PeriodicalIF":3.0,"publicationDate":"2026-02-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12904971/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146179174","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}