{"title":"Possible regulation of ganglioside GD3 synthase gene expression with DNA methylation in human glioma cells.","authors":"Yurie Yamamoto, Ken Higashimoto, Yuki Ohkawa, Hidenobu Soejima, Kei Kaneko, Yuhsuke Ohmi, Keiko Furukawa, Koichi Furukawa","doi":"10.1007/s10719-023-10108-9","DOIUrl":"https://doi.org/10.1007/s10719-023-10108-9","url":null,"abstract":"<p><p>Gangliosides are expressed in nervous systems and some neuroectoderm-derived tumors at high levels and play pivotal roles. However, mechanisms for the regulation of glycosyltransferase genes responsible for the ganglioside synthesis are not well understood. In this study, we analyzed DNA methylation patterns of promoter regions of GD3 synthase (ST8SIA1) as well as mRNA levels and ganglioside expression using human glioma cell lines. Among 5 cell lines examined, 4 lines showed changes in the expression levels of related genes after treatment with 5-aza-dC. LN319 showed up-regulation of St8sia1 and increased b-series gangliosides after 5-aza-dC treatment, and an astrocytoma cell line, AS showed high expression of ST8SIA1 and b-series gangliosides persistently before and after 5-Aza-2'-deoxycytidine treatment. Using these 2 cell lines, DNA methylation patterns of the promoter regions of the gene were analyzed by bisulfite-sequencing. Consequently, 2 regions that were methylated before 5-Aza-2'-deoxycytidine treatment were demethylated in LN319 after the treatment, while those regions were persistently demethylated in AS. These 2 regions corresponded with sites defined as promoter regions by Luciferase assay. Taken together, it was suggested that ST8SIA1 gene is regulated by DNA methylation at the promoter regions, leading to the regulation of tumor phenotypes.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"40 3","pages":"323-332"},"PeriodicalIF":3.0,"publicationDate":"2023-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9515333","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}
Sepideh Hosseini, Saeid Abediankenari, Mehdi Rasouli
{"title":"Serum total carbohydrates, conjugated carbohydrates and total protein glycation index in diabetes mellitus.","authors":"Sepideh Hosseini, Saeid Abediankenari, Mehdi Rasouli","doi":"10.1007/s10719-023-10115-w","DOIUrl":"https://doi.org/10.1007/s10719-023-10115-w","url":null,"abstract":"<p><strong>Background: </strong>Diabetes mellitus is defined according to fasting blood glucose and clinical signs. But, the markers of glycation have been used recently as a criterion to diagnose and monitor the therapy.</p><p><strong>Objectives: </strong>To measure serum total- and conjugated- saccharides and to define the new marker as serum total protein glycation index (sTPGI ) for diabetes.</p><p><strong>Design and methods: </strong>The study population consisted of 172 subjects who were divided to control and diabetic cases. Serum total and conjugated saccharides were measured and sTPGI was defined to discriminate serum glycosylated and glycated saccharides.</p><p><strong>Results: </strong>Patients with diabetes compared with the controls had increased levels of serum (free) glucose, HbA1c, serum total carbohydrates, total conjugated carbohydrates and sTPGI. All three indices of serum carbohydrates showed significant positive correlation with serum glucose, HbA1c and diabetes. The equations: sTPGI = 0.12 Glucose (mg/dL) + 12 and sTPGI = 3.5HbA1c (%) + 5, were deduced for the association of sTPGI with serum free glucose and HbA1c. In ROC analysis, both HbA1c (AUC = 0.965, p ≤ 0.001) and sTPGI (AUC = 0.734, p ≤ 0.001) had strong and significant efficiency to discriminate diabetic cases from control subjects.</p><p><strong>Conclusions: </strong>The results confirm that sTPGI obtained by indirect assay has high significant efficiency comparable to HbA1c to diagnose diabetes. sTPGI relative to HbA1c indicates the mean level of glycaemia over a shorter period of about one month so it responds more quickly to changes in therapy.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"40 3","pages":"375-381"},"PeriodicalIF":3.0,"publicationDate":"2023-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9885302","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":"Alkali-labile gangliosides.","authors":"Laura Mauri, Sandro Sonnino","doi":"10.1007/s10719-023-10103-0","DOIUrl":"https://doi.org/10.1007/s10719-023-10103-0","url":null,"abstract":"<p><p>The structure and properties of a group of gangliosides modified by mild alkaline treatment are discussed. We will present the occurrence and the structure of gangliosides carrying the N-acetyneuraminic acid O-acetylated in position 9, the Neu5,9Ac<sub>2</sub>, and of gangliosides carrying a sialic acid that forms a lactone ring. Starting from biochemical data we will discuss the possible biochemical role played by these gangliosides in the processes of cell signaling and maintenance of brain functions.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"40 3","pages":"269-276"},"PeriodicalIF":3.0,"publicationDate":"2023-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10202986/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9517402","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":"Advances in protein glycosylation and its role in tissue repair and regeneration.","authors":"Zhongyu Yue, Yajie Yu, Boyuan Gao, Du Wang, Hongxiao Sun, Yue Feng, Zihan Ma, Xin Xie","doi":"10.1007/s10719-023-10117-8","DOIUrl":"https://doi.org/10.1007/s10719-023-10117-8","url":null,"abstract":"<p><p>After tissue damage, a series of molecular and cellular events are initiated to promote tissue repair and regeneration to restore its original structure and function. These events include inter-cell communication, cell proliferation, cell migration, extracellular matrix differentiation, and other critical biological processes. Glycosylation is the crucial conservative and universal post-translational modification in all eukaryotic cells [1], with influential roles in intercellular recognition, regulation, signaling, immune response, cellular transformation, and disease development. Studies have shown that abnormally glycosylation of proteins is a well-recognized feature of cancer cells, and specific glycan structures are considered markers of tumor development. There are many studies on gene expression and regulation during tissue repair and regeneration. Still, there needs to be more knowledge of complex carbohydrates' effects on tissue repair and regeneration, such as glycosylation. Here, we present a review of studies investigating protein glycosylation in the tissue repair and regeneration process.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"40 3","pages":"355-373"},"PeriodicalIF":3.0,"publicationDate":"2023-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9885328","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":"Improved synthesis of CD22-binding sialosides and its application for further development of potent CD22 inhibitors.","authors":"Yuki Suganuma, Akihiro Imamura, Hiromune Ando, Makoto Kiso, Hiromu Takematsu, Takeshi Tsubata, Hideharu Ishida","doi":"10.1007/s10719-023-10098-8","DOIUrl":"https://doi.org/10.1007/s10719-023-10098-8","url":null,"abstract":"<p><p>CD22, one of the sialic acid-binding immunoglobulin-like lectins (Siglecs), regulates B lymphocyte signaling via its interaction with glycan ligands bearing the sequence Neu5Ac/Gcα(2→6)Gal. We have developed the synthetic sialoside GSC-718 as a ligand mimic for CD22 and identified it as a potent CD22 inhibitor. Although the synthesis of CD22-binding sialosides including GSC-718 has been reported by our group, the synthetic route was unfortunately not suitable for large-scale synthesis. In this study, we developed an improved scalable synthetic procedure for sialosides which utilized 1,5-lactam formation as a key step. The improved procedure yielded sialosides incorporating a series of aglycones at the C2 position. Several derivatives with substituted benzyl residues as aglycones were found to bind to mouse CD22 with affinity comparable to that of GSC-718. The new procedure developed in this study affords sialosides in sufficient quantities for cell-based assays, and will facilitate the search for promising CD22 inhibitors that have therapeutic potential.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"40 2","pages":"225-246"},"PeriodicalIF":3.0,"publicationDate":"2023-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9648544","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":"Twin research shows glycan changes are more susceptible to environmental factors than their carrier glycoproteins.","authors":"Tatsuya Asuka, Yoshihiro Kamada, Koichi Morishita, Tomoya Fukuoka, Shinji Takamatsu, Jumpei Kondo, Mikio Watanabe, Norio Sakai, Kazuo Hayakawa, Eiji Miyoshi","doi":"10.1007/s10719-023-10099-7","DOIUrl":"https://doi.org/10.1007/s10719-023-10099-7","url":null,"abstract":"<p><p>Changes in protein glycosylation are clinically used as biomarkers. In the present study, we employed a twin cohort to investigate the contributions of genetic and environmental factors to glycan modifications of glycoproteins. Mac-2 binding protein (Mac-2 bp), haptoglobin (Hp), and their glycosylated forms are liver fibrosis and cancer biomarkers. Sera from 107 twin pairs without clinical information were used as a training cohort for the Mac-2 bp and Mac-2 bp glycosylation isomer (M2BPGi) assay. As a validation cohort, 22 twin pairs were enrolled in the study. For each twin pair, one twin was diagnosed with liver or pancreatic disease. For the training cohort, the correlation ratios of serum Mac-2 bp and M2BPGi levels in twin sera with random sequences were 0.30 and 0.018, respectively. The correlation ratios between twin pairs in the validation cohort for serum Mac-2 bp and M2BPGi levels were 0.75 and 0.35, respectively. In contrast, correlation ratios of serum Hp and fucosylated haptoglobin (Fuc-Hp) levels between twin sera with liver and pancreatic disease were 0.49 and 0.16, respectively. Although serum protein levels of glycoproteins are susceptible to genetic factors, characteristic glycan changes of these glycoproteins are more susceptible to environmental factors, including liver and pancreatic disease.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"40 2","pages":"191-198"},"PeriodicalIF":3.0,"publicationDate":"2023-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9649063","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}
Roopa Kenoth, Arya K Sreekumar, A Sukanya, A Anand Prabu, Ravi Kanth Kamlekar
{"title":"Interaction of sugar stabilised silver nanoparticles with Momordica charantia seed lectin, a type II ribosome inactivating protein.","authors":"Roopa Kenoth, Arya K Sreekumar, A Sukanya, A Anand Prabu, Ravi Kanth Kamlekar","doi":"10.1007/s10719-023-10107-w","DOIUrl":"https://doi.org/10.1007/s10719-023-10107-w","url":null,"abstract":"<p><p>Sugar-stabilised nanomaterials have received a lot of attention in cancer therapy in recent years due to their pronounced application as specific targeting agents and maximizing their therapeutic potential while bypassing off-target effects. Lectins, the carbohydrate-binding proteins, are capable of binding to receptors present on the target cell/tissue and interact with transformed glycans better than normal cells. Besides some of the lectins exhibit anticancer activity. Conjugating sugar-stabilised NPs with lectins there for is expected to multiply the potential for the early diagnosis of cancer cells and the specific release of drugs into the tumor site. Because of the prospective applications of lectin-sugar-stabilised nanoparticle conjugates, it is important to understand their molecular interaction and physicochemical properties. Momordica charantia Seed Lectin (MCL) is a type II RIP and has been known as an anti-tumor agent. Investigation of the interaction between sugar-stabilised silver nanoparticles and MCL has been performed by fluorescence spectroscopy to explore the possibility of creating an effective biocompatible drug delivery system against cancer cells. In this regard interaction between lectin and NPs should be well-preserved, while recognizing the specific cell surface sugar. Therefore experiments were carried out in the presence and absence of specific sugar galactose. Protein intrinsic fluorescence emission is quenched at ~ 20% at saturation during the interaction without any significant shift in fluorescence emission maximum. Binding experiments reveal a good affinity. Tetrameric MCL binds to a single nanoparticle. Stern-Volmer analysis of the quenching data suggests that the interaction is via static quenching leading to complex formation. Hemagglutination experiments together with interaction studies in the presence of specific sugar show that the sugar-binding site of the lectin is distinct from the nanoparticle-binding site and cell recognition is very much intact even after binding to AgNPs. Our results propose the possibility of developing MCL-silver nanoparticle conjugate with high stability and multiple properties in the diagnosis and treatment of cancer.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"40 2","pages":"179-189"},"PeriodicalIF":3.0,"publicationDate":"2023-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9333554","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}
Yaoyao Cai, Zhen Sun, Chen Shao, Zhongqun Wang, Lihua Li
{"title":"Role of galectin-3 in vascular calcification.","authors":"Yaoyao Cai, Zhen Sun, Chen Shao, Zhongqun Wang, Lihua Li","doi":"10.1007/s10719-023-10106-x","DOIUrl":"https://doi.org/10.1007/s10719-023-10106-x","url":null,"abstract":"<p><p>Vascular calcification is an abnormal process in which bone specific hydroxyapatite crystals are actively deposited on the vascular wall mediated by phenotypic differentiated smooth muscle cells and other mesenchymal cells under various pathological conditions. It is one of the important characteristics in the occurrence and development of atherosclerosis, prevalent in patients with type 2 diabetes and advanced chronic kidney disease, especially those requiring maintenance hemodialysis, with severely threatening human health. Previous studies have shown that the early diagnosis and control of vascular calcification is of great significance for cardiovascular risk stratification, prevention of acute cardiovascular events, which can greatly improve the prognosis and quality of life of patients. Galectins are a family of lectin superfamily. It is widely distributed in various animals and plays an important role in many physiological and pathological processes, such as cell adhesion, apoptosis, inflammatory response, tumor metastasis and so on. Many biomarker-and association-related studies and Preclinical-mechanistic studies have suggested that galactose-specific lectin-3 (galectin-3) plays an important role in vascular calcification and vascular intimal calcification (VIC) calcification induced by Wnt/βcatenin signaling pathway, NF-κB signaling pathway and ERK1/2 signaling pathway. This paper mainly expounds the role and mechanism of galectin-3 in vascular calcification under different pathological conditions including atherosclerosis, diabetes and chronic kidney disease.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"40 2","pages":"149-158"},"PeriodicalIF":3.0,"publicationDate":"2023-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9273390","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}
Glycoconjugate JournalPub Date : 2023-04-01Epub Date: 2023-01-26DOI: 10.1007/s10719-023-10101-2
Ronald L Schnaar
{"title":"Gangliosides as Siglec ligands.","authors":"Ronald L Schnaar","doi":"10.1007/s10719-023-10101-2","DOIUrl":"10.1007/s10719-023-10101-2","url":null,"abstract":"<p><p>The structure of a sialoglycan can be translated into to a biological response when it binds to a specific endogenous lectin. Among endogenous sialic acid-binding lectins in humans are those comprising the 15-member Siglec family, most of which are expressed on overlapping sets of immune cells. Endogenous Siglec ligands are sialoglycolipids (gangliosides) and/or sialoglycoproteins, on cell surfaces or in the extracellular milieu, that bind to and initiate signaling by cell surface Siglecs. In the nervous system, where gangliosides are the predominant sialoglycans, Siglec-4 (myelin-associated glycoprotein) on myelinating cells binds to gangliosides GD1a and GT1b on nerve cell axons to ensure stable and productive axon-myelin interactions. In the immune system, Siglec-7 on natural killer cells binds to gangliosides GD3 and GD2 to inhibit immune signaling. Expression of GD3 and GD2 on cancer cells can lead to tumor immune evasion. Siglec-1 (sialoadhesin, CD169) on macrophages binds to gangliosides on tumors and enveloped viruses. This may enhance antigen presentation in some cases, or increase viral distribution in others. Several other Siglecs bind to gangliosides in vitro, the biological significance of which has yet to be fully established. Gangliosides, which are found on all human cells and tissues in cell-specific distributions, are functional Siglec ligands with varied roles driving Siglec-mediated signaling.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"40 2","pages":"159-167"},"PeriodicalIF":3.0,"publicationDate":"2023-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11000168/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9524085","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}
Eriko Yamaguchi, Naoko Komura, Hide-Nori Tanaka, Akihiro Imamura, Hideharu Ishida, Sophie Groux-Degroote, Martina Mühlenhoff, Kenichi G N Suzuki, Hiromune Ando
{"title":"Fluorescent GD2 analog for single-molecule imaging.","authors":"Eriko Yamaguchi, Naoko Komura, Hide-Nori Tanaka, Akihiro Imamura, Hideharu Ishida, Sophie Groux-Degroote, Martina Mühlenhoff, Kenichi G N Suzuki, Hiromune Ando","doi":"10.1007/s10719-023-10102-1","DOIUrl":"https://doi.org/10.1007/s10719-023-10102-1","url":null,"abstract":"<p><p>Ganglioside GD2 is associated with the proliferation and migration of breast cancer cells. However, the precise role of GD2 is unclear because its tendency to form dynamic and transient domains in cell plasma membranes (PMs), called lipid rafts, makes it difficult to observe. Previously, we developed fluorescent analogs of gangliosides (e.g., GM3 and GM1), which enabled the observation of lipid raft formation for the first time using single-molecule imaging. In this report, we describe the first chemical synthesis of a fluorescent ganglioside, GD2. A biophysical analysis of the synthesized analog revealed its raft-philic character, suggesting its potential to aid single-molecule imaging-based investigations into raft-associated interactions.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"40 2","pages":"247-257"},"PeriodicalIF":3.0,"publicationDate":"2023-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9633788","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}