Glycobiology最新文献_第5页

Impact of sialyltransferase deletion in mature T cells on control of subcutaneous and metastatic cancers. 成熟T细胞唾液基转移酶缺失对皮下和转移性癌症控制的影响。

IF 3.3 3区生物学

Glycobiology Pub Date : 2026-08-23 DOI: 10.1093/glycob/cwag065

Xiaoshuang Wang, James C Paulson

{"title":"Impact of sialyltransferase deletion in mature T cells on control of subcutaneous and metastatic cancers.","authors":"Xiaoshuang Wang, James C Paulson","doi":"10.1093/glycob/cwag065","DOIUrl":"10.1093/glycob/cwag065","url":null,"abstract":"To investigate the roles of the α2,3-sialyltransferase ST3Gal1 and the α2,6-sialyltransferase ST6Gal1 in T cell-mediated tumor control, we generated mice with mature T cell-specific deletion of ST3Gal1 (T-ST3KO) or ST6Gal1 (T-ST6KO) using distal Lck-Cre-mediated recombination. Deletion of ST3Gal1 in mature T cells did not affect thymic T cell development but resulted in a reduction of peripheral CD8+ T cells. In contrast, ST6Gal1 deletion had minimal impact on T cell development and peripheral T cell abundance. Following in vitro stimulation of isolated T cells from T-ST3KO and parental wild type (WT) mice with anti-CD3 plus anti-CD28/CD80-Fc, CD8+ T cells from T-ST3KO mice exhibited enhanced activation and an increased frequency of CD44 positive memory-like T cells, while comparison of T cells from T-ST6KO and the parental WT mice showed no significant changes. Despite the activated CD8+ T cell phenotype in T-ST3KO mice, subcutaneous MC38 tumors displayed accelerated growth. In contrast, tumor progression in T-ST6KO mice was unchanged from the parental WT mice. Notably, T-ST6KO mice developed increased pulmonary metastases following intravenous challenge with B16F10 melanoma cells, whereas metastatic burden was unaffected in T-ST3KO mice. These findings demonstrate distinct and non-redundant roles for ST3Gal1- and ST6Gal1-mediated sialylation in regulating T cell function and antitumor immunity and reveal context-dependent effects of T cell intrinsic sialylation in controlling primary tumor growth and metastatic dissemination.","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-08-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13513753/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148792146","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Glyco you should know. 你应该知道的糖。

IF 3.3 3区生物学

Glycobiology Pub Date : 2026-08-23 DOI: 10.1093/glycob/cwag074

Tiandi Yang

引用次数: 0

N-glycan mass spectrometry imaging - a valuable tool for biomarker discovery and validation. n -聚糖质谱成像-生物标志物发现和验证的宝贵工具。

IF 3.3 3区生物学

Glycobiology Pub Date : 2026-07-31 DOI: 10.1093/glycob/cwag014

Anand S Mehta, Peggi M Angel, Richard R Drake

{"title":"N-glycan mass spectrometry imaging - a valuable tool for biomarker discovery and validation.","authors":"Anand S Mehta, Peggi M Angel, Richard R Drake","doi":"10.1093/glycob/cwag014","DOIUrl":"10.1093/glycob/cwag014","url":null,"abstract":"Matrix-assisted laser desorption/ionization mass spectrometry imaging (MALDI-MSI) enables spatially resolved detection of diverse biomolecules directly from tissues, supporting pathology-guided and unbiased biomarker discovery. By maintaining spatial context, MALDI-MSI overcomes key limitations of bulk omics approaches, which obscure the cellular origins of analytes, particularly in heterogeneous tumors containing abundant normal tissue or extracellular matrix. Complementary biofluids such as serum, urine, saliva, or cerebrospinal fluid are valuable for biomarker validation yet similarly lack spatial information when used as primary discovery materials. Integrating spatially defined diseased tissues with matched proximal biofluids therefore represents a powerful strategy for biomarker development. N-glycan mass spectrometry imaging (N-glycan MSI) has emerged as a versatile platform for characterizing N-glycan distributions in tissues and for quantifying glycan compositions in cells, antibodies, and biofluids. This method relies on on-tissue application of peptide N-glycosidase F (PNGase F) to liberate N-linked glycans, which are subsequently detected by MALDI-MSI to generate micron-scale, two-dimensional glycan maps. The workflow is highly modular, accommodating tissues, cultured cells, arrays, membranes, and isotopic or label-free quantification approaches. Recent advances also include the use of specialized glycosidases to resolve glycan isomers. This review highlights established and emerging N-glycan MSI strategies for biomarker discovery and validation, with applications in liver, brain, breast, and other clinically relevant tissues.","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-07-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147377138","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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

Revisiting the roles of N-acetylglucosaminyltransferase III (GnT-III/MGAT3) in cancer cell behavior and cellular signaling. 重新审视n -乙酰氨基葡萄糖转移酶III （GnT-III/MGAT3）在癌细胞行为和细胞信号传导中的作用

IF 3.3 3区生物学

Glycobiology Pub Date : 2026-07-31 DOI: 10.1093/glycob/cwaf058

Jianguo Gu

{"title":"Revisiting the roles of N-acetylglucosaminyltransferase III (GnT-III/MGAT3) in cancer cell behavior and cellular signaling.","authors":"Jianguo Gu","doi":"10.1093/glycob/cwaf058","DOIUrl":"https://doi.org/10.1093/glycob/cwaf058","url":null,"abstract":"Glycosylation is a common post-translational modification in mammalian cells. Abnormal glycosylation is a universal feature of cancer cells, regarded as a hallmark of cancer, and can influence tumor progression, including cell adhesion, migration, growth, differentiation, and invasion. A key change in N-glycosylation involves the modification of bisecting N-acetylglucosamine (GlcNAc), which is catalyzed by N-acetylglucosaminyltransferase III (GnT-III, encoded by the MGAT3 gene). GnT-III is widely regarded as a key glycosyltransferase in N-glycan biosynthesis. The addition of a bisecting GlcNAc prevents further processing of N-glycans, thereby blocking the synthesis of GlcNAc-branched N-glycans by N-acetylglucosaminyltransferase IV (GnT-IV) and N-acetylglucosaminyltransferase V (GnT-V). These branched N-glycans are strongly associated with cancer invasion and metastasis. For example, in many cases, integrins and E-cadherin are modified by GnT-V, which promotes cell migration and cancer invasion. In contrast, those modified by GnT-III tend to inhibit cell migration and metastasis. Recent studies also show that GnT-III expression suppresses cancer chemoresistance caused by prolonged exposure to anticancer drugs and enhances the differentiation capacity of leukemia cells. This review will discuss the roles of GnT-III in cancer cell behavior and cellular signaling, with a particular focus on some potential target proteins.","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":"36 9","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-07-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148630268","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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

Short mucin-type O-glycans in cancer: biomarker and therapeutic potential amid analytical barriers. 肿瘤中的短粘蛋白型o -聚糖：分析障碍中的生物标志物和治疗潜力。

IF 3.3 3区生物学

Glycobiology Pub Date : 2026-07-31 DOI: 10.1093/glycob/cwaf077

Henrique Sousa, Inês A B Ribeiro, Marta Falcão, Daniela F Barreira, Mariana Barbosa, Shally Sharma, Manfred Wuhrer, Noortje de Haan, Paula A Videira

{"title":"Short mucin-type O-glycans in cancer: biomarker and therapeutic potential amid analytical barriers.","authors":"Henrique Sousa, Inês A B Ribeiro, Marta Falcão, Daniela F Barreira, Mariana Barbosa, Shally Sharma, Manfred Wuhrer, Noortje de Haan, Paula A Videira","doi":"10.1093/glycob/cwaf077","DOIUrl":"10.1093/glycob/cwaf077","url":null,"abstract":"Mucin-type O-glycans are abundant protein modifications that regulate cell signalling, adhesion, and immune interactions. In cancer, their biosynthetic pathways are frequently disrupted, leading to the accumulation of truncated structures, such as Tn antigen and sialyl-Tn (STn). These aberrant glycans remodel the glycocalyx, alter receptor clustering, and drive key hallmarks of malignancy, including immune evasion, invasion, and therapy resistance. Over the past decade, increasing evidence has linked short O-glycans to poor prognosis across multiple tumour types, highlighting their potential as diagnostic and prognostic biomarkers. Moreover, their restricted expression in normal tissues positions them as attractive targets for therapeutic intervention, including monoclonal antibodies, antibody-drug conjugates, and CAR-T cell strategies. However, clinical translation remains limited by major analytical challenges. The structural diversity of O-glycans, their low abundance, and the lack of broadly specific enzymes for glycan release hinder comprehensive characterization. Recent advances in glycoproteomics, glycomics, and antibody engineering are beginning to overcome these barriers, enabling site-specific mapping and improved detection of cancer-associated glycoforms. This review summarizes current knowledge on the biosynthetic origins, biological roles, and clinical relevance of truncated O-glycans in cancer, while critically discussing emerging technologies and future directions for their integration into precision oncology.","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-07-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145563592","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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

Sugar storm: O-GlcNAc signaling amid the clouds of cancer complexity. 糖风暴：癌症复杂性云中的O-GlcNAc信号。

IF 3.3 3区生物学

Glycobiology Pub Date : 2026-07-31 DOI: 10.1093/glycob/cwag026

Nusaiba N Ahmed, Riley G Young, Jessica Merzy, Mauricio J Reginato

{"title":"Sugar storm: O-GlcNAc signaling amid the clouds of cancer complexity.","authors":"Nusaiba N Ahmed, Riley G Young, Jessica Merzy, Mauricio J Reginato","doi":"10.1093/glycob/cwag026","DOIUrl":"10.1093/glycob/cwag026","url":null,"abstract":"Cancer is a systemic disease driven not only by cell-intrinsic alterations, but also by system-wide factors that regulate its initiation and progression. Among the key regulators of these processes are nutrient-sensing pathways, which coordinate both cellular and systemic responses. One such pathway involves O-linked N-acetylglucosaminylation (O-GlcNAcylation), a nutrient-responsive and reversible post-translational modification that has emerged as a critical driver of cancer progression. Catalyzed by O-GlcNAc transferase (OGT), O-GlcNAcylation integrates signals from glucose, glutamine, and other nutrients to regulate the activity of cytoplasmic, nuclear, and mitochondrial proteins. Recent studies demonstrate that O-GlcNAcylation influences multiple dimensions of cancer progression, including metabolic adaptation, transcriptional plasticity, immune evasion, metastasis, cancer stem-like states, and therapy resistance. Beyond its cell-intrinsic effects, O-GlcNAcylation also interfaces with broader systemic processes. In this review, we position O-GlcNAcylation within the framework of the \"clouds of cancer complexity,\" highlighting its roles across the metabolic effects, inception and promotion, pleiotropic immune responses, and aging systems and tissues clouds. We propose that O-GlcNAcylation functions as a systems-level integrator that embeds metabolic, environmental, and temporal signals into tumor evolution, revealing new conceptual and therapeutic opportunities.","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-07-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147672468","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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

Cancer-associated alterations in O-GalNAc glycosylation. O-GalNAc糖基化的癌症相关改变

IF 3.3 3区生物学

Glycobiology Pub Date : 2026-07-31 DOI: 10.1093/glycob/cwag049

José Pires, Eric Rochat, Ieva Bagdonaite, Sally Dabelsteen, Hans H Wandall

{"title":"Cancer-associated alterations in O-GalNAc glycosylation.","authors":"José Pires, Eric Rochat, Ieva Bagdonaite, Sally Dabelsteen, Hans H Wandall","doi":"10.1093/glycob/cwag049","DOIUrl":"10.1093/glycob/cwag049","url":null,"abstract":"Aberrant O-GalNAc glycans such as Tn, STn, and T are among the most consistent tumor-associated carbohydrate antigens, broadly expressed on carcinomas but largely absent from healthy epithelia. In parallel, O-glycans can also be modified to carry functional motifs, such as Lewis antigens. Rather than a simple shift from elongated to truncated structures, cancer-associated O-glycans form a heterogeneous repertoire of truncated and elongated glycoforms that coexist across the tumor glycocalyx. Collectively, both short and elongated cancer-associated O-glycans co-drive tumor formation through their simultaneous influence on multiple cancer hallmarks, including adhesion, receptor signaling, dissemination, and immune evasion. The latter occurs through interactions with glycan-binding proteins including Selectins, Siglecs, macrophage galactose-type lectin (MGL), and galectins. The stable expression of especially truncated O-glycans across cancer stages, as well as their driving influence on cancer progression, make short, truncated O-glycans attractive therapeutic targets. While early vaccine approaches had limited efficacy, strategies that couple O-glycan recognition with potent effector mechanisms have shown promise. This includes O-glycan-directed chimeric antigen receptor T cells (CARTs), T-cell bispecifics (TCBs), and particularly antibody-drug conjugates (ADCs), which have demonstrated strong preclinical activity. Looking forward, multi-specific antibodies, bio-orthogonal chemistry, and artificial intelligence-driven engineering are expected to enhance safety, selectivity, and improve patient stratification, helping to further exploit O-GalNAc glycans in precision oncology.","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-07-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13424894/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148307878","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Introduction to Special Issue Glycobiology Reviews Cancer. 糖生物学特刊导论-糖生物学评论癌症。

IF 3.3 3区生物学

Glycobiology Pub Date : 2026-07-31 DOI: 10.1093/glycob/cwag052

Richard D Cummings, Susan L Bellis

引用次数: 0

Glyco you should know. Glyco你应该知道。

IF 3.3 3区生物学

Glycobiology Pub Date : 2026-07-30 DOI: 10.1093/glycob/cwag063

Sonal Mahajan

引用次数: 0

Glyco-Forum.