Journal of glycobiology最新文献

{"title":"Increased Sialylation of N- and O-Glycans on Serum Maackia amurensis Lectin II Binding Glycoproteins in Autistic Spectrum Disorder","authors":"Yannan Qin, Yanni Chen, Ganglong Yang, Lingyu Zhao, Zhuoyue Shi, Chen Huang","doi":"10.4172/2168-958X.1000137","DOIUrl":"https://doi.org/10.4172/2168-958X.1000137","url":null,"abstract":"Background: The pathophysiology of Autistic Spectrum Disorder (ASD) is not fully understood and there are no diagnostic or predictive biomarkers. In our previous study we found that expression of serum Siaα2-3 Gal/ GalNAc recognized by Maackia amurensis Lectin II (MAL-II) as well as MAL-II Binding Glycoproteins (MBGs) were significantly increased in ASD compared to Typically Developing (TD) children; however the specific glycoforms of MBGs remain unclear. Method: In this study, N- and O-glycans on sera MAL-II binding glycoproteins (MBGs) from 60 children with ASD and 60 age-matched TD children were profiled by using lectin-magnetic particle conjugate assisted MALDI-TOF/ TOF-MS analysis. Results: A total of 16 representative N-glycans including high-mannose, complex and hybrid, bi-/tri-antennary structures and bisecting GlcNAc glycoforms and 20 representative O-glycans derived from core structures 1, 2, 3, and 4 were annotated in TD and ASD sera. Among these, 6 sialylated or disialylated N-glycans were specifically observed in ASD sera, such as disialylated bi-antennary complex N-glycan (m/z 2061.356). The proportion of total sialylated and disialylated O-glycans were also apparently increased in ASD (63.2% and 15.8%) vs. TD (50.5% and 10.0%) sera respectively, which was most obvious in core 3 and 4 (e.g., sialylated monofucosylated core 4 [m/z 1470.358]). Conclusion: This study can facilitate the discovery of specific sialylated glycans of MBGs that might have much higher sensitivity and specificity as serum biomarkers for ASD diagnosis of children at the earliest age, which might also provide pivotal information for understanding the pathogenesis of ASD.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"8 1","pages":"1-10"},"PeriodicalIF":0.0,"publicationDate":"2019-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70860026","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A High-level Over-Expression of N-and O-Glycan Glycosyltransferases in Pancreatic Tumors and Diabetic Neutrophils: An Unique Pathological Situation in Pancreatic Cancer and Diabetic Retinopathy","authors":"rasekaran Ev, Dhananjay DMarathe, S. Neelamegham, J. Lau, K. Matta","doi":"10.24105/2168-958X.8.138","DOIUrl":"https://doi.org/10.24105/2168-958X.8.138","url":null,"abstract":"Diabetes is a widely existing disease in patients at risk of pancreatic cancer. It originates from pancreatic endocrine gland whereas pancreatic cancer develops from exocrine glands. Leukocyte cell surface glycans are involved in leukocyte-endothelial cell adherence and retinal endothelial cell death in diabetic retinopathy. A stimulation of hexosamine biosynthesis pathway occurs in diabetes and in pancreatic cancer controlled by oncogene KRAS variant. We examined 5 pancreatic non-tumor and 14 pancreatic tumor tissue specimens for quantitative changes in glycosyltransferse (GTs) activities in pancreatic tumorigenesis by following the incorporation of 14C or 3H monosaccharide (CPM) into specific acceptor catalyzed by 1 mg protein of Triton X-100 solubilized tissue extract. As compared to pancreatic non-tumor tissue specimens with a very low level of GTs activities, pancreatic tumor specimens on average contained 26.0, 42.9, 331.7, 121.0 and 62.8-fold of α1-2, α1-3, α1-4, α1-6 FTs and FTVI activities respectively. The major sialyltransferase α2-3 (O)ST and sialomucin glycoproteins increased 95.4 and 4.0-fold; N-glycan αMan: β1-2GlcNAc-T, chain elongating βGal: β1-3 GlcNAc-T and N-glycan GalNAc capping β1-3/1-4 GalNAc-T were respectively 95.0, 2.7 and 14.8-fold and the mRNAs of FUT-4, β1-3 and β1-4 GalNAc-Ts were 8.3, 12.0 and 2.4-fold respectively. The increase in activity in neutrophils of retinopathy vs. normal was: β1-2-GlcNAc-T (9.0 fold), β1-3-GlcNAc-T (2.5), α1-3- FT (3.5), α1-6-FT (3.3), FTVII (1.9), αGalNAc: β1-3-GalT (1.4), βGlcNAc: β1-4-Gal-T (2.1), α2-3-(O)ST (2.1), α2-3-(N)ST (4.5), α2-6-(N)ST (8.1). GalNAc replacing Gal in LacNAc terminals results in changes of glycosyltransferase specificities and the modified GalNAc β1-4GlcNAc by FTs and STs bind to lectins such as WGA. In contrast to a low-level expression-difference of glycosyltransferases between tumor and non-tumor specimens from stomach, prostate and colon, a multifold increase in GTs in pancreatic tumor would indicate their significant role in invasion and intractability of pancreatic cancer.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"8 1","pages":"1-15"},"PeriodicalIF":0.0,"publicationDate":"2019-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69014938","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Enzymes as powerful biocatalysts for precision synthesis of oligo and polysaccharides","authors":"pJunichi Kadokawap","doi":"10.4172/2168-958X-C1-010","DOIUrl":"https://doi.org/10.4172/2168-958X-C1-010","url":null,"abstract":"","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2018-11-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70863030","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Isomalto polysaccharides: Soluble food fibers made from starch and their probiotic effects","authors":"pPiet L Buwaldap","doi":"10.4172/2168-958X-C1-011","DOIUrl":"https://doi.org/10.4172/2168-958X-C1-011","url":null,"abstract":"","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2018-11-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48506134","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Development of a reverse lectin ELISA for detecting fucosylated forms of 1-acid glycoprotein associated with hepatocellular carcinoma","authors":"pEva Astromp","doi":"10.4172/2168-958X-C2-015","DOIUrl":"https://doi.org/10.4172/2168-958X-C2-015","url":null,"abstract":"","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2018-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70863085","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Kinetic basis for DNA target specificity of CRISPR-Cas12a","authors":"Isabel Strohkendl","doi":"10.4172/2168-958x-c1-012","DOIUrl":"https://doi.org/10.4172/2168-958x-c1-012","url":null,"abstract":"","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"07 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2018-07-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42682955","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A High-Yielding Enzymatic Process for Production of Bioactive β-1,3-Glucan Oligosaccharides with Defined Size","authors":"Ningzi Guan, Juping Yu, Wei Liu, Rachel Chen","doi":"10.4172/2168-958X.1000131","DOIUrl":"https://doi.org/10.4172/2168-958X.1000131","url":null,"abstract":"The study is to develop a bioprocess to depolymerize curdlan for production of β-1,3 oligosaccharides with a uniform size. A codon-optimized Streptomyces laminarinase was expressed in an E. coli system, resulting in an enzyme preparation (19.1 U/L) highly active on solid curdlan substrate without any pre-treatment. In a preparative scale reaction at pH 5.5 and 55°C, 90% conversion and a product concentration close to 27 g/L were achieved within 6 hours. The major product was identified as β3-glucan pentasaccharide based on HPLC, TLC, and MS analyses. A single-enzyme based bioprocess was highly efficient in deriving β3-glucan pentasaccharide from solid curdlan. Enzyme to curdlan ratio and reaction time are critical parameters for high-yield production of β3-glucan pentasaccharide from curdlan.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"7 1","pages":"1-4"},"PeriodicalIF":0.0,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70859642","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mannose in Complex with Colocasia esculenta Tuber Agglutinin","authors":"R. Chattopadhyaya, Avisek Mondal","doi":"10.4172/2168-958X.1000132","DOIUrl":"https://doi.org/10.4172/2168-958X.1000132","url":null,"abstract":"The major tuber storage protein of Colocasia esculenta is a monocot mannose-binding, widely used, dietarylectin, for which a crystal structure was previously shown to consist of four β-prism II domains or two αβheterodimers, each forming a α2β2 heterotetramer with a symmetry related unit. In the present study, the same lectincrystallized in the presence of a 50 molar excess of free mannose, persists in forming such α2β2 heterotetramers.Lectin crystals apparently complexed to mannose were obtained by hanging-drop, vapor-diffusion method at roomtemperature and high-resolution X-ray diffraction data were collected using a home X-ray source. Using the crystalstructure of the Remusatia vivipara lectin, the structure of the complex has been solved by molecular replacementand subsequent crystallographic refinement. Five different mannose binding sites per heterodimer with partialoccupancy have been found, among which only one appears to bind close to a classical carbohydrate recognitionsite characterized earlier for these lectins. Mannose binding at these five sites is described.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"7 1","pages":"1-10"},"PeriodicalIF":0.0,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70859727","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The Carbohydrate Structure of the Hormone hCG, the Autocrine Hyper Glycosylated hCG, and the Extravillous Cytotrophoblast Hyperglycosylated hCG","authors":"L. Cole","doi":"10.4172/2168-958X.1000136","DOIUrl":"https://doi.org/10.4172/2168-958X.1000136","url":null,"abstract":"Objective: Carbohydrate structure has been determined for pregnancy hCG, hydatidiform mole hCG and choriocarcinoma hCG by multiple authors. It has not, however, been discriminated for the three hCG components, the hormone hCG, the autocrine hyperglycosylated hCG or for invasive cell hyperglycosylated hCG. This is determined here. Methods: Three methodologies were used to discriminate the three components of hCG. The B152 immunoassay specifically determines the concentration of hyperglycosylated hCG. Matrigel invasion chambers determine invasiveness of first trimester trophoblast Results: B152 immunoassay binds only hyperglycosylated hCG, and identified all hyperglycosylated hCG in pregnancy hCG, hydatidiform mole hCG and choriocarcinoma hCG preparations. Distribution of triantennary sugar structures same as percent invasion of Matrigel membrane, indicating distribution of invasive extravillous cytotrophoblast component. Recombinant hCG is only hormone hCG, contains 100% Type 1 O-linked oligosaccharides. Identifies Type 1 O-linked oligosaccharide hCG as hormone hCG. Discussion: As determined, first trimester trophoblast cells produced 86.3% hormone hCG (biantennary N-linked and Type 1 O-linked oligosaccharides), 3.5% hyperglycosylated hCG (biantennary N-linked and Type 2 O-linked oligosaccharides) and 13.7% invasive extravillous cytotrophoblast hCG (triantennary N-linked and Type 2 O-linked oligosaccharides). Invasive extravillous cytotrophoblast cells produce 50.4% hormone hCG, 6.0% hyperglycosylated hCG and 42% invasive extravillous cytotrophoblast hCG. Hydatidiform mole cells produce 73.2% hormone hCG, 5.4% hyperglycosylated hCG and 23.4% invasive extravillous cytotrophoblast hCG. Choriocarcinoma cells produce 38.6% hormone hCG, 17.6% hyperglycosylated hCG and 42.8% invasive extravillous cytotrophoblast hCG.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"07 1","pages":"1-5"},"PeriodicalIF":0.0,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70859975","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Infrared Spectra for Alfa Fibers Treated with Thymol","authors":"Arwa Turki, A. Oudiani, S. Msahli, F. Sakli","doi":"10.4172/2168-958X.1000130","DOIUrl":"https://doi.org/10.4172/2168-958X.1000130","url":null,"abstract":"In this work, we attempt to analyze the hydrogen bond network of cellulose by comparing the 2nd derivative infrared spectra of alfa fiber treated with different concentrations of thymol. It was proved, from this study, that the 2nd derivative infrared spectrum is a useful method for identifying the least changes incurred in the cellulosic supramolecular structure. It can be considered as an effective method to gain further insight on OH bond system of cellulosic materials and to clarify some grey areas in terms of infrared band assignment. The careful analysis of 2nd derivative infrared spectra of untreated and thymol treated alfa fibers revealed an increase in band intensity related to both intermolecular and intramolecular hydrogen bonds and a decrease in bands related to free hydroxyl groups.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"7 1","pages":"1-8"},"PeriodicalIF":0.0,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4172/2168-958X.1000130","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70859504","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}