Glycoconjugate Journal最新文献

Asparagine-linked glycosylation protein 1 (ALG1) promotes aggressive phenotypes of lung adenocarcinoma cells, A549, via modulating N-linked glycosylation and ER-Stress. 天冬酰胺连接糖基化蛋白1 （ALG1）通过调节n -连接糖基化和内质网应激促进肺腺癌细胞A549的侵袭性表型。

IF 3.1 4区生物学

Glycoconjugate Journal Pub Date : 2025-10-09 DOI: 10.1007/s10719-025-10198-7

Kanadit Piriyapairoje, Marta Baro, Aanchal Katoch, Bryce De Muth, Ludovica Villanti, Charupong Saengboonmee, Sopit Wongkham, Joseph N Contessa, Chatchai Phoomak

{"title":"Asparagine-linked glycosylation protein 1 (ALG1) promotes aggressive phenotypes of lung adenocarcinoma cells, A549, via modulating N-linked glycosylation and ER-Stress.","authors":"Kanadit Piriyapairoje, Marta Baro, Aanchal Katoch, Bryce De Muth, Ludovica Villanti, Charupong Saengboonmee, Sopit Wongkham, Joseph N Contessa, Chatchai Phoomak","doi":"10.1007/s10719-025-10198-7","DOIUrl":"https://doi.org/10.1007/s10719-025-10198-7","url":null,"abstract":"Glycosylation plays a critical role in various biological processes and is essential for cell survival. Aberrant glycosylation has been implicated in numerous diseases, including cancer. Lung cancer remains the leading cause of cancer-related mortality worldwide. The correlation between lung cancer progression and abnormal glycosylation has been demonstrated previously. Asparagine-linked glycosylation protein 1 (ALG1) is a key enzyme involved in the N-linked glycosylation process; however, its role in cancer progression remains unclear. In this study, we investigated the function of ALG1 in lung cancer progression. Analysis of the Cancer Genome Atlas (TCGA) dataset revealed that ALG1 expression was significantly upregulated in lung tumor tissues and was associated with poor patient prognosis. To explore its functional relevance, ALG1 expression was depleted in A549 lung adenocarcinoma cells using CRISPR-Cas9-mediated knockout. Loss of ALG1 led to reduced levels of protein N-linked glycosylation and induced an endoplasmic reticulum (ER)-stress response. Functionally, ALG1 knockout significantly impaired A549 cell proliferation, migration, and invasion, as evidenced by phenotypic assays and molecular markers. Moreover, the extent of glycosylation deficiency was positively correlated with ER-stress activation and inversely associated with cancer cell aggressiveness. These findings suggest that ALG1 promotes lung cancer aggressiveness through the regulation of protein glycosylation and modulation of ER-stress pathways. Overall, this study highlights the potential of ALG1 as a therapeutic target and a prognostic biomarker for lung adenocarcinoma patients.","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":" ","pages":""},"PeriodicalIF":3.1,"publicationDate":"2025-10-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145250824","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}

引用次数: 0

Eukaryotic expression and characterization of two α1,2-fucosyltransferase genes in the histo-blood group antigens synthesis pathway of the Pacific oyster (Crassostrea gigas). 两个α1,2-聚焦转移酶基因在太平洋牡蛎（长牡蛎）组织血型抗原合成途径中的真核表达及特性研究。

IF 3.1 4区生物学

Glycoconjugate Journal Pub Date : 2025-10-01 DOI: 10.1007/s10719-025-10195-w

Junxia Hu, Meng Qu, Weiran Zhang, Binbin Gui, Yanhua Jiang, Lin Yao, Shixin Wang, Dapeng Wang

{"title":"Eukaryotic expression and characterization of two α1,2-fucosyltransferase genes in the histo-blood group antigens synthesis pathway of the Pacific oyster (Crassostrea gigas).","authors":"Junxia Hu, Meng Qu, Weiran Zhang, Binbin Gui, Yanhua Jiang, Lin Yao, Shixin Wang, Dapeng Wang","doi":"10.1007/s10719-025-10195-w","DOIUrl":"https://doi.org/10.1007/s10719-025-10195-w","url":null,"abstract":"Norovirus (NoV), an important cause of human viral gastroenteritis worldwide, recognizes human histo-blood group antigens (HBGAs) as receptors. Oysters are a vector of foodborne transmission of NoV, and HBGAs have been found in oyster tissues. In this study, CgFUT1 and CgFUT2, the key genes involved in the synthesis of HBGAs in Crassostrea gigas, were successfully expressed in Pichia pastoris, and 32.6 kDa target proteins were obtained after purification, concentration, and dialysis treatments. Western blot analysis using FUT1 and FUT2 antibodies showed that CgFUT1 and CgFUT2 have antigenic similarity as human FUT1 and FUT2. Enzyme catalysis assays using Galβ1-3GlcNAc and Galβ1-4GlcNAc as substrates showed that these substrates react with GDP-Fuc to generate Fucα1-2GalβGlcNAc under the action of CgFUT1 and CgFUT2. High-resolution mass spectrometry analysis revealed that CgFUT1 and CgFUT2 have the same substrate specificity, both reacting with Galβ1-3GlcNAc and Galβ1-4GlcNAc. The results of this study demonstrate the probable role of CgFUT1 and CgFUT2 in regulating substrates for H antigen synthesis in oysters and provide a reference for future studies into the functions of these genes. The study also lays a foundation for further exploration of the molecular mechanisms underlying NoV accumulation in oysters.","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":" ","pages":""},"PeriodicalIF":3.1,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145199079","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}

引用次数: 0

Monoclonal antibody-based assay to identify compounds that inhibit N^δ-(5-hydro-4-imidazolon-2-yl)ornithine (G-H1) formation. 基于单克隆抗体的鉴定抑制Nδ-（5-氢-4-咪唑-2-基）鸟氨酸（G-H1）形成的化合物的方法。

IF 3.1 4区生物学

Glycoconjugate Journal Pub Date : 2025-10-01 DOI: 10.1007/s10719-025-10193-y

Hikari Sugawa, Noriyoshi Manabe, Yoshitaka Hiraoka, Yoshiki Yamaguchi, Ryoji Nagai

{"title":"Monoclonal antibody-based assay to identify compounds that inhibit Nδ-(5-hydro-4-imidazolon-2-yl)ornithine (G-H1) formation.","authors":"Hikari Sugawa, Noriyoshi Manabe, Yoshitaka Hiraoka, Yoshiki Yamaguchi, Ryoji Nagai","doi":"10.1007/s10719-025-10193-y","DOIUrl":"https://doi.org/10.1007/s10719-025-10193-y","url":null,"abstract":"The advanced glycation end-product Nδ-(5-hydro-4-imidazolon-2-yl)ornithine (G-H1) accumulates during the progress of atherosclerosis with type 2 diabetes. Therefore, G-H1 might serve as early diagnostic marker of atherosclerosis, and its inhibition could become a strategy to prevent the pathogenesis of this disease. This study therefore aimed to determine the feasibility of an anti-G-H1 monoclonal antibody-based screen for G-H1 inhibitors. Mice were immunized with G-H1-keyhole limpet hemocyanin prepared with synthesized G-H1 standards to produce an anti-G-H1 monoclonal antibody (1E9). The specificity of 1E9 and levels of G-H1 were determined using an enzyme-linked immunosorbent assay (ELISA). The G-H1 levels correlated with those measured using liquid chromatography (LC)-tandem mass spectrometry (MS). We then mixed arginine with various glyoxal (GO) concentrations and applied GO-modified collagen and albumin to determine the conditions required for G-H1 formation. To screen for G-H1 inhibitors, an ELISA-based protocol was developed and leveraged with aminoguanidine to determine the inhibitory effect of screening compounds on G-H1 formation. The specificity of 1E9 for G-H1 was high. The abundance of G-H1 formation in glyoxal-modified arginine was maximal with 2 mM GO, which aligned with the LC-MS/MS and ELISA results. However, G-H1 was below the detection limit for the GO-modified proteins. Aminoguanidine inhibited G-H1 formation in ribose-modified arginine in a concentration-dependent manner. Overall, our findings emphasize the potential of 1E9 to specifically detect free G-H1 and its value for screening G-H1 inhibitors.","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":" ","pages":""},"PeriodicalIF":3.1,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145199073","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}

引用次数: 0

Advanced glycation end products (AGEs) and their role in diabetes mellitus and related complications: mechanisms and therapeutic insights. 晚期糖基化终产物（AGEs）及其在糖尿病和相关并发症中的作用：机制和治疗见解。

IF 3.1 4区生物学

Glycoconjugate Journal Pub Date : 2025-09-22 DOI: 10.1007/s10719-025-10194-x

Eskandar Qaed, Waleed Aldahmash, Mueataz A Mahyoub

{"title":"Advanced glycation end products (AGEs) and their role in diabetes mellitus and related complications: mechanisms and therapeutic insights.","authors":"Eskandar Qaed, Waleed Aldahmash, Mueataz A Mahyoub","doi":"10.1007/s10719-025-10194-x","DOIUrl":"https://doi.org/10.1007/s10719-025-10194-x","url":null,"abstract":"Diabetes mellitus (DM) is marked by prolonged elevated blood glucose levels, which lead to the formation of covalent adducts between glucose and plasma proteins through a non-enzymatic reaction called glycation. This biochemical process plays a crucial role in the development of DM complications, including retinopathy, nephropathy, neuropathy, and cardiomyopathy, while also impacting conditions such as rheumatoid arthritis, osteoporosis, and aging. Glycation alters the molecular structure, enzymatic activity, and receptor interactions of proteins, affecting their normal functions. Advanced glycation end products (AGEs) arise from these modifications, forming cross-links within and between cells, which affect proteins and other vital biomolecules, such as lipids and nucleic acids. This contributes significantly to the complex complications associated with DM. Recent studies highlight the interaction between AGEs and their specific receptors, receptor for advanced glycation end products (RAGE), located on the plasma membrane. This involvement initiates changes in intracellular signaling, alters gene expression, and stimulates the release of pro-inflammatory cytokines and reactive oxygen species. This review examines the glycation of key plasma proteins albumin, fibrinogen, globulins, and collagen and discusses the various AGEs formed. Furthermore, it elucidates the role of AGEs in the exacerbation of DM complications, providing a comprehensive overview of the molecular pathways involved and the systemic impact of these glycation products.","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":" ","pages":""},"PeriodicalIF":3.1,"publicationDate":"2025-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145112885","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}

引用次数: 0

Cell cycle regulation in cancer cells by O-GlcNAcylation. o - glcn酰化对癌细胞周期的调控。

IF 3.1 4区生物学

Glycoconjugate Journal Pub Date : 2025-08-18 DOI: 10.1007/s10719-025-10189-8

Ulises González-González, María Cristina Castañeda-Patlán, María Teresa Hernández-Huerta, Jesús Hernández-Juárez, Edgar Zenteno-Galindo, Carlos Josué Solórzano-Mata

引用次数: 0

Molecular expression of glycosaminoglycans modifies the plasticity of biphasic mesothelioma in favor of tumor progression. 糖胺聚糖的分子表达改变了双期间皮瘤的可塑性，有利于肿瘤的进展。

IF 3.1 4区生物学

Glycoconjugate Journal Pub Date : 2025-08-13 DOI: 10.1007/s10719-025-10192-z

Camila Machado Baldavira, Aline Nery Qualiotto, Tabatha Gutierrez Prieto, Sandra de Morais Fernezlian, Aline Assato, Marcelo Balancin, Teresa Takagaki, Alexandre Ab'Saber, Ana Paula Pereira Velosa, Walcy Rosolia Teodoro, Vera Luiza Capelozzi

{"title":"Molecular expression of glycosaminoglycans modifies the plasticity of biphasic mesothelioma in favor of tumor progression.","authors":"Camila Machado Baldavira, Aline Nery Qualiotto, Tabatha Gutierrez Prieto, Sandra de Morais Fernezlian, Aline Assato, Marcelo Balancin, Teresa Takagaki, Alexandre Ab'Saber, Ana Paula Pereira Velosa, Walcy Rosolia Teodoro, Vera Luiza Capelozzi","doi":"10.1007/s10719-025-10192-z","DOIUrl":"https://doi.org/10.1007/s10719-025-10192-z","url":null,"abstract":"The study aimed to verify whether the expression of glycosaminoglycans (GAGs) and proteoglycans (PGs) in the tumor matrix affects the plasticity of mesothelioma and its relationship with the phenotype, progression, and resistance to treatment of malignant mesothelioma (MM). As MM is highly aggressive, understanding the molecular mechanisms that regulate the abilities of tumor cells to alter their behaviors and shapes is essential to the development of new therapeutic strategies. To test this hypothesis, we studied 66 samples of human biphasic MM. The expression levels of the GAGs heparan sulfate (HS) and chondroitin sulfate (SC), as well as the PGs versican, biglycan, and perlecan were detected using immunohistochemistry, and their expression was quantified using semi-automated digital analysis. We found that the fusiform phenotype of MM cells was associated with higher expression levels of HS, versican, and biglycan (all P-values < 0.001) in the extracellular matrix. This suggests that the increase and eventual rapid turnover of cell membrane PGs resulted in a variation in shape from polygonal to fusiform phenotypes, whereas GAGs were associated with cell aggregation-thus indicating the distinct functions of different GAGs. Multivariate Cox regression analysis showed that non-surgical patients (hazard ratio [HR]: 4.03 (1.26-12.82); P = 0.02), whose tumors presented necrosis (P < 0.001), high HS expression (P = 0.02), and low biglycan expression (HR: 2.68 [1.16-6.18]; P = 0.02) had significantly worse overall survival rates. We concluded that the expression of GAGs and PGs in the ECM affects the plasticity of MM, modifies its phenotype, and facilitates both its progression and resistance to treatment.","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":" ","pages":""},"PeriodicalIF":3.1,"publicationDate":"2025-08-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144834849","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}

引用次数: 0

Characterization of bacterial glycolipids in Pediococcus pentosaceus for fermented soybean paste (miso) and Tetragenococcus halophilus for soy sauce, in comparison with those in Lactobacillus, Streptococcus and Staphylococcus species. 发酵大豆酱中戊糖球菌和酱油中嗜盐四小球菌的糖脂质特征，并与乳酸菌、链球菌和葡萄球菌的糖脂质进行比较。

IF 3.1 4区生物学

Glycoconjugate Journal Pub Date : 2025-08-01 Epub Date: 2025-07-15 DOI: 10.1007/s10719-025-10190-1

Masao Iwamori, Kyoko Tanaka

{"title":"Characterization of bacterial glycolipids in Pediococcus pentosaceus for fermented soybean paste (miso) and Tetragenococcus halophilus for soy sauce, in comparison with those in Lactobacillus, Streptococcus and Staphylococcus species.","authors":"Masao Iwamori, Kyoko Tanaka","doi":"10.1007/s10719-025-10190-1","DOIUrl":"10.1007/s10719-025-10190-1","url":null,"abstract":"Gram-positive bacterial biomembranes are composed of phosphatidyl glycerol (PG), cardiolipin (CL), and dihexaosyl diglycerides (DH-DG) as the major lipid constituents. The carbohydrate structures of DH-DG are specific to the particular bacterial species and we previously revealed them to have immunologically active properties. To characterize the species-structure relationship of glycolipids in Gram-positive bacteria, the structures of DH-DG in Pediococcus pentosaceus (PP) for producing fermented soybean paste (miso) and Tetragenococcus halophilus (TH) for soy sauce were determined in comparison with those in Lactobacillus, Streptococcus and Staphylococcus species. They were shown to be Glcα1-2Glcα1-3'DG (kojibiosyl DG) with 18:1(oleic acid) and 18:1 as the fatty acids for PP, and that with 16:0 (palmitic acid) and 18:1 for TH, and their carbohydrate structures were identical to that in Streptococcus salivarius, a symbiotic bacterium in the human oral cavity. Additionally, both bacteria contained an acidic glycolipid, in which glycerol phosphate was attached to the 6-position of the nonreducing terminal Glc residue of DH-DG. TLC immunostaining with human sera revealed antibodies to Galα1-2Glcα1-3'DG (LacDH-DG) from Lactobacillus species and Glcβ1-6Glcβ1-3'DG (StaDH-DG) from Staphylococcus species, but not to Glcα1-2Glcα1-3'DG (StrDH-DG) from Streptococcus species, in 2 out of 20 human sera. Given that one serum sample with anti-StaDH-DG antibodies was from a patient who had suffered from food poisoning due to Staphylococcus aureus 6 months previously, the antibodies to bacterial DH-DG were thought to have arisen via bacterial infection.","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":" ","pages":"199-207"},"PeriodicalIF":3.1,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144636796","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}

引用次数: 0

Anti-GalNAcα (anti-Tn) antibody repertoire differs between individuals with blood groups A and B. 抗galnacα（抗tn）抗体库在A型血和B型血的个体之间存在差异。

IF 3.1 4区生物学

Glycoconjugate Journal Pub Date : 2025-08-01 Epub Date: 2025-04-26 DOI: 10.1007/s10719-025-10184-z

Polina Obukhova, Nadezhda Shilova, Galina Pazynina, Svetlana Tsygankova, Inna Popova, Jacques Le Pendu, Nicolai Bovin

{"title":"Anti-GalNAcα (anti-Tn) antibody repertoire differs between individuals with blood groups A and B.","authors":"Polina Obukhova, Nadezhda Shilova, Galina Pazynina, Svetlana Tsygankova, Inna Popova, Jacques Le Pendu, Nicolai Bovin","doi":"10.1007/s10719-025-10184-z","DOIUrl":"10.1007/s10719-025-10184-z","url":null,"abstract":"Recently, Breiman et al. (2021) reported that the level of anti-Tn in the blood of healthy donors and COVID-19 patients is significantly lower in individuals of blood group A than B. This prompted us to look for qualitative differences in the repertoire of anti-Tn like specificity in individuals of different blood groups (BG). To this end, we isolated antibodies from the pooled sera of BG A and BG B healthy donors using GalNAcα-sepharose, followed by Printed Glycan Array analysis. As expected, antibodies affinity isolated from BG A donors completely lack species directed to canonical (GalNAcα-transferase dependent) A-glycans, such as A (types 1, 2 and 4), GalNAcα1-3(Fucα1-2)Gal, GalNAcα1-3Galβ1-4GlcNAc (linear A), and ALeY. Unexpectedly, GalNAcα1-4Galβ1-4GlcNAc, glycan with an unnatural 1-4 bond fell into the same group, i.e., antibodies to it were found only in BG B donors. Other unexpected results include the following: (1) for GalNAcα1-OCH2CH(COOH)NH2 (GalNAcα-OSer, immobilized by NH2 group) the opposite result was observed, i.e. affinity isolated anti-Tn antibodies of BG A donors demonstrated significantly higher titer than of BG B; (2) in BG A donors, the level of antibodies to GalNGcα1-3GalNAcα (i.e. disaccharide in N-glycolyl form) is close to background, while there is a significant level of these antibodies in the BG B donors. Since antiglycan antibodies are known to play both a protective role in antimicrobial immunity and to promote infectivity, the knowledge gained about the difference in the specificity profiles of anti-Tn antibodies signals the need to take blood group into account in developing therapeutic strategies.","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":" ","pages":"137-146"},"PeriodicalIF":3.1,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143997497","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}

引用次数: 0

GM1 oligosaccharide-mediated rescue in GBA-linked Parkinson's disease via modulation of lysosomal and mitochondrial dysfunctions. GM1寡糖通过调节溶酶体和线粒体功能障碍介导的gba相关帕金森病的救援。

IF 3.1 4区生物学

Glycoconjugate Journal Pub Date : 2025-08-01 Epub Date: 2025-06-04 DOI: 10.1007/s10719-025-10185-y

Giulia Lunghi, Carola Pedroli, Ilaria Tagliabue, Dorina Dobi, Maria Grazia Ciampa, Laura Mauri, Laura Rouvière, Alexandre Henriques, Noelle Callizot, Sandro Sonnino, Elena Chiricozzi, Maria Fazzari

{"title":"GM1 oligosaccharide-mediated rescue in GBA-linked Parkinson's disease via modulation of lysosomal and mitochondrial dysfunctions.","authors":"Giulia Lunghi, Carola Pedroli, Ilaria Tagliabue, Dorina Dobi, Maria Grazia Ciampa, Laura Mauri, Laura Rouvière, Alexandre Henriques, Noelle Callizot, Sandro Sonnino, Elena Chiricozzi, Maria Fazzari","doi":"10.1007/s10719-025-10185-y","DOIUrl":"10.1007/s10719-025-10185-y","url":null,"abstract":"Mutations in the glucocerebrosidase GBA gene, encoding the lysosomal enzyme β-glucocerebrosidase, represent the most frequent genetic risk factor for Parkinson's disease, leading to lysosomal dysfunction, α-synuclein aggregation, and mitochondrial impairment. In this study, we investigated the therapeutic potential of GM1 ganglioside and its oligosaccharide portion (OligoGM1) in a cellular model of GBA-associated Parkinson's disease, using SH-SY5Y neuroblastoma cells carrying the L444P GBA mutation. We observed that both GM1 and OligoGM1 reduced α-synuclein accumulation and improved cell viability. Notably, only OligoGM1 attenuated lysosomal overload and restored mitophagy. Additionally, OligoGM1 significantly prevented 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced toxicity, including lysosomal dysfunction, reactive oxidative species-overproduction, and mitochondrial energy failure, whereas GM1 failed to provide protection. These findings highlight the selective and multifaceted neuroprotective actions of OligoGM1 under both genetic conditions and environmental stress. Due to its small, hydrophilic nature and capacity to cross the blood-brain barrier, OligoGM1 emerges as a promising therapeutic candidate for GBA-related and potentially idiopathic forms of Parkinson's Disease.","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":" ","pages":"159-171"},"PeriodicalIF":3.1,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144215652","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}

引用次数: 0

Detection of antibodies against the African parasite Trypanosoma brucei using synthetic glycosylphosphatidylinositol oligosaccharide fragments. 合成糖基磷脂酰肌醇低聚糖片段检测非洲寄生虫布氏锥虫抗体。

IF 3.1 4区生物学

Glycoconjugate Journal Pub Date : 2025-08-01 Epub Date: 2025-06-24 DOI: 10.1007/s10719-025-10186-x

Maurice Michel, Benoit Stijlemans, Dana Michel, Monika Garg, Andreas Geissner, Peter H Seeberger, Daniel Varón Silva

引用次数: 0