Journal of glycobiology最新文献

{"title":"Cyclodextrin Glycosides as Materials for Removal of Pathogenic Materials from the Human Environment","authors":"R. Engel, W. Blanford","doi":"10.4172/2168-958x.1000135","DOIUrl":"https://doi.org/10.4172/2168-958x.1000135","url":null,"abstract":"Cyclodextrins provide an intriguing agent system for the removal of a host of materials from aqueous media in order to prevent pathogens from affecting humans. In the current effort cyclodextrins have been chemically modified such that they may be used efficaciously for the removal of a wide range of harmful materials from aqueous environments impinging on human activities. Among these modifications are those that involve selective targeting of the upper and lower rims of the cyclodextrin species for selective encapsulation of organic chemical toxins of appropriate size, shape, and hydrophobicity, as well as the generation of hyperbranched polymers from the cyclodextrins for enhanced encapsulation, and the functionalization of cyclodextrins for the facilitated destruction of pathogenic bacterial agents. Utility of the constructed cyclodextrin materials for a variety of situations is considered.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"07 1","pages":"1-3"},"PeriodicalIF":0.0,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70860328","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":"Automated Microbioreactors and the Characterization of Media Dependent Changes in Antibody Product Glycosylation and Aglycosylation","authors":"David N. Powers, Sai Rashmika Velugula-Yellela, Nicholas Trunfio, Phillip Angart, Anneliese M. Faustino, C. Agarabi","doi":"10.4172/2168-958X.1000133","DOIUrl":"https://doi.org/10.4172/2168-958X.1000133","url":null,"abstract":"The glycosylation state of therapeutic antibodies is a critical quality attribute due to its effect on product efficacy and safety. With the advent of the biosimilar development and the need to match the glycan profile of the originator product, better understanding of how the variables of the bioprocessing procedure control glycosylation is critical. To this effect, we used automated microbioreactors with our in-house model CHO DG 44 cell line and different media types to study differences in antibody outcomes, specifically focusing on N-glycosylation profiles and aglycosylation rates. We observed that different media types resulted in vastly different amounts of high mannose and terminal galactosylation of N-glycans. By measuring the percentage of antibodies that was not N-glycosylated we observed that high mannose outcomes were not correlated to aglycosylation rates. For further analysis, we utilized multivariate data analysis to determine the process variables that best explained our glycan profile findings. Factors linked to glutamine consumption were determined to be the most important in predicting high mannose outcomes, while factors related to the temporal aspects of cell growth rate were linked to terminal galactosylation. Our work discovered in-process parameters in the cell culture process that have significant effects on the glycan profile of an antibody product, further elucidating the link between the biomanufacturing process and product quality outcomes.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"7 1","pages":"1-9"},"PeriodicalIF":0.0,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4172/2168-958X.1000133","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70859954","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":"Differences of Mice Gut Microbiota between SPF and Clean Environment","authors":"Yingying Su, Xiaomeng Ren, Yuan Li, W. Song","doi":"10.4172/2168-958X.1000134","DOIUrl":"https://doi.org/10.4172/2168-958X.1000134","url":null,"abstract":"Objective: Compare the difference of intestinal microbiota between Specific Pathogen Free (SPF) mice andclean environment mice. Methods: Twelve mice were divided into two groups. One group is Specific Pathogen Free (SPF) mice, anotheris clean environment mice. The stool samples were collected for nine and eighteen days both in SPF and cleanenvironment, and the total DNA was extracted. PCR-DGGE technology were used to obtain microbial florafingerprint, Quantity one software were used to build phylogenetic tree, the similarity and diversity of the map can beused for analysis, differential bands were selected for sequencing. Results: Under the conditions of SPF, the intestinal microbiota of mice were significantly different (p<0.05) fromthat of the clean grade, and the Enterobacteria were specific in SPF mice. With the passage of time, Lactobacilluswere decreased in SPF mice. Conclusion: Differences exist in intestinal microbiota of mice under different feeding conditions.","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":"70860237","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 Minute Structural Difference between the Hormone hCG and the Autocrine Hyperglycosylated hCG","authors":"L. Cole","doi":"10.4172/2168-958X.1000127","DOIUrl":"https://doi.org/10.4172/2168-958X.1000127","url":null,"abstract":"Introduction: In 1997 I discovered hyperglycosylated hCG, a separate and independent molecule to the hormone hCG. The structure of hyperglycosylated hCG was also examined, it was a molecule varying from hCG by just 3 or 4 small sugar side chains, or 2.8% of molecular weight. While the hormone hCG binds a luteinizing hormone (LH)/hCG hormone receptor, hyperglycosylated hCG and its β-subunit are autocrines binding and antagonizing a TGF-β-II receptor. Here structural differences between the two molecules are investigated. Methods: Nicking or cleavage of the hormone hCG and the autocrine hyperglycosylated hCG, and dissociation of subunits were carefully investigated using sequence analysis. Results: Research showed that hyperglycosylated hCG was much more rapidly nicked or cleaved at β47-48 than the hormone hCG. And that nicked hCG was much more rapidly dissociated into subunits than non-nicked hCG. Discussion: A model was generated. As proposed, hyperglycosylated hCG is first rapidly nicked or cleaved at β47-48 and then rapidly dissociated. The nicked hyperglycosylated hCG β-subunit antagonizes the TGF-β-ll receptor. In contrast, the endocrine hCG is blocked from nicking, which limits dissociation, only intact hCG binds the LH/hCG hormone receptor.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"6 1","pages":"1-6"},"PeriodicalIF":0.0,"publicationDate":"2017-10-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"45826389","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":"Glycosylation affects the bioavailability of saponins in herbal extracts","authors":"pMirosawa FerensSieczkowskap","doi":"10.4172/2168-958X-C1-008","DOIUrl":"https://doi.org/10.4172/2168-958X-C1-008","url":null,"abstract":"","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2017-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70863256","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":"Glycosylation and development of atherosclerosis","authors":"Yu-Xin Xu","doi":"10.4172/2168-958X-C1-009","DOIUrl":"https://doi.org/10.4172/2168-958X-C1-009","url":null,"abstract":"P is a major heparan sulfate (HS) proteoglycan in the arterial wall. Previous studies have localized perlecan to atherosclerotic lesions and its expression correlates with lesion progression. The retention of atherogenic lipoproteins in the arterial wall is an early step in the development of atherosclerosis and this retention is presumably mediated by the ionic interaction between the negatively charged HS and the basic amino acids of apolipoprotein B-100. Perlecan contains a core protein and three HS side chains. Its core protein has five domains (I-V) with disparate structures and domain II is highly homologous to the ligand-binding portion of low-density lipoprotein receptor (LDLR). The functional significance of this domain has been unknown. Here, we show that the perlecan domain II interacts with LDL. Importantly, the interaction largely relies on O-linked glycans that are only present in the secreted domain II. Among the five repeat units of domain II, most of the glycosylation sites are from the second unit, which is highly divergent and rich in serine/threonine but no cysteine residues. Interestingly, most of the glycans are capped by the negatively charged sialic acids, which are critical for LDL binding. We further demonstrate an additive effect of HS and domain II on LDL binding. Unlike LDLR, which directs LDL uptake through endocytosis, this study uncovers a novel feature of the perlecan LDLR-like domain II in receptor-mediated lipoprotein retention, which depends on its glycosylation. Thus, the arterial perlecan glycosylation may provide an attractive non-lipid target to decrease the progression of atherosclerosis.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2017-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70862969","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":"Glycosylated ribosomal protein S3, secreted from various cancer cells is a possible cancer biomarker","authors":"J. Kim","doi":"10.4172/2168-958X-C1-007","DOIUrl":"https://doi.org/10.4172/2168-958X-C1-007","url":null,"abstract":"Ribosomal protein S3 (rpS3) is a genuine component of the 40S ribosomal small subunit. However, it has been known as a versatile protein with multiple other extra-ribosomal functions in apoptosis, cell cycle control, DNA repair, etc. It has a DNA repair endonuclease activity which is related with various cancers. Recently, we have discovered that this protein forms a dimer and is secreted after N-glycosylation. It is secreted only from various cancer cells but not in normal cells. We also have confirmed that rpS3 is secreted more into media when cancer cells are more invasive. The secretion pathway turned out to be a standard ER-Golgi dependent pathway. We are currently developing various antibodies against rpS3 which could be used as useful reagents for future cancer biomarkers. Ribosomal protein S3 (rpS3) is a 243 amino acid component of the 40S ribosomal small subunit. It has multiple roles in translation and extra-ribosomal functions like apoptosis and DNA repair. RpS3 is secreted only in cancer cell lines. Presently, mass spectrometry analysis revealed rpS3 to be glycosylated at the Asn165 residue. A point mutation at this residue decreased secretion of rpS3 in cancer cell lines. Secretion was also inhibited by the endoplasmic reticulum (ER)-Golgi transport inhibitor Brefeldin A and by Tunicamycin, an inhibitor of N-linked glycosylation. N-linked glycosylation of rpS3 was confirmed as necessary for rpS3 secretion into culture media via the ER-Golgi dependent pathway. RpS3 bound to Concanavalin A, a carbohydrate binding lectin protein, while treatment with peptide-Nglycosidase F shifted the secreted rpS3 to a lower molecular weight band. In addition, the N165G mutant of rpS3 displayed reduced secretion compared to the wild-type. An in vitro binding assay detected rpS3 homodimer formation via the N-terminal region (rpS3:1–85) and a middle region (rpS3:95– 158). The results indicate that the Asn 165 residue of rpS3 is a critical site for N-linked glycosylation and passage through the ER-Golgi secretion pathway. Ribosomal protein S3 (rpS3/RPS3/Ribosomal Protein S3) is a constituent of the 40 S ribosomal small subunit, which functions in translation. Extra-ribosomal functions include DNA repair, apoptosis and transcriptional regulation. RpS3 interacts with nm23-H1, which acts as a suppressor of metastasis in certain human tumors and prevents the invasive potential in HT1080 cells. Furthermore, rpS3 is overexpressed in colorectal cancer cells, suggesting that the level of rpS3 may be related to tumorigenesis. A previous study showed that rpS3 was secreted into the extracellular environment in a dimeric form. The level of rpS3 secretion was prominently increased in highly malignant cells when compared to normal parent cells. This suggests that secreted rpS3 may be a putative marker for malignant tumors. About 10% of all human proteins are secretory proteins. These include cytokines, hormones, digestive enzymes and immunoglobulins. Their various fun","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2017-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70863404","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":"Crystal Structure of Colocasia esculenta Tuber Agglutinin at 1.74 Å Resolution and Its Quaternary Interactions","authors":"R. Chattopadhyaya, Himadri Biswas, A. Sarkar","doi":"10.4172/2168-958X.1000126","DOIUrl":"https://doi.org/10.4172/2168-958X.1000126","url":null,"abstract":"Many members of the monocot mannose-binding lectin family, characterized by specificity towards mannose have been characterized and cloned. A majority of these lectins molecules contain 1-4 polypeptides of about 110 residues each. From the previously solved crystal structures of a few such lectins, mostly from non-edible plants, these lectins are thought to possess a common β-prism II fold structure. The major tuber storage protein of Colocasia esculenta is a monocot mannose-binding, widely used, dietary lectin. This tuber agglutinin contains two polypeptides of 12.0 and 12.4 kDa by matrix assisted laser desorption ionisation time-of-flight mass spectrometry. By gel filtration at pH 7.2, the purified lectin has a α2β2 form of apparent molecular mass of 48.2 kDa in solution but at pH 3, it has the heterodimeric αβ form. Lectin crystals were obtained by hanging-drop, vapor-diffusion method at room temperature and high-resolution X-ray diffraction data were collected using a home X-ray source. Among previously solved crystal structures of this family are garlic, Solomon’s seal, snowdrop, daffodil and Spanish blue-bell lectins, but the protein sequence of the Colocasia esculenta tuber agglutinin was found to be closest to that of the Remusatia vivipara lectin having no simple mannose-binding property. Using the previously solved 2.4A crystal structure of the Remusatia vivipara lectin, that of Colocasia esculenta has been solved by molecular replacement and subsequent crystallographic refinement and root mean square deviations between various lectins are tabulated and rationalized. The asymmetric unit in our lectin crystal structure contains four β-prism II domains or two αβ heterodimers, each forming a α2β2 heterotetramer with a symmetry related unit. The tetrameric interface obtained from our crystal structure is used to explain the conversion to dimers in acidic pH. Five ordered magnesium ions were located in the asymmetric unit and the presence of magnesium verified by atomic absorption spectroscopy.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"6 1","pages":"1-12"},"PeriodicalIF":0.0,"publicationDate":"2017-04-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4172/2168-958X.1000126","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42699885","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":"Current Insights in Mammalian Glycosylation: Implication of Glycoproteomics as Next-Generation Biomarkers in Diabetes Mellitus","authors":"A. Raghav, J. Ahmad, Z. A. Khan, B. Mishra, R. P. Anirudh","doi":"10.4172/2168-958X.1000125","DOIUrl":"https://doi.org/10.4172/2168-958X.1000125","url":null,"abstract":"Glycosylation, an enzyme-directed, site-specific process is one of the major co-translational and post-translational modifications in proteins. So formed product, glycoproteins, mediate multiple functions of signal transductions, cell association, and inter and intra cell signalling. Glycoproteomics exploits all these biological functions and serves as the next generation diagnostic marker for analyzing proteins that are associated with micro- and macro-vascular complication of diabetes mellitus. This tool can unreveal the secrets of the patterned expression of glycoproteins in healthy and patients with diabetes with secondary complications. The expression profile of several O-linked and Nlinked mammalian glycoproteins delivers the knowledge and helps to create a database for expression in diabetes mellitus, for proposing a mechanistic approach to understanding the cellular pathway severely involved in the regulation of all glycoproteins. This future next generation glycopeptides tool will describe a novel strategy for the quantification of the several glycoproteins based on a specific chemical ligation described as reverse glycoblotting techniques, two-dimensional gel electrophoresis, western blotting, multiple reaction monitoring, LC-MS/MS analysis of glycosylated peptides along with lectin chromatography. These recent tools will reveal the expression pattern of several glycoproteins that will serve as a power tool precise diagnosis of diabetes associated complications.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"6 1","pages":"1-7"},"PeriodicalIF":0.0,"publicationDate":"2017-03-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4172/2168-958X.1000125","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44869905","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":"Neutrophil Adhesion and Migration: Another Role of the Glucose-6-Phosphate Transporter","authors":"H. Jun, J. Chou","doi":"10.4172/2168-958X.1000124","DOIUrl":"https://doi.org/10.4172/2168-958X.1000124","url":null,"abstract":"Glycogen storage disease type Ib (GSD-Ib) is caused by a deficiency in a glucose-6-phosphate transporter (G6PT) that belongs to the solute-carrier-37 family of endoplasmic reticulum (ER)-associated sugar-phosphate/phosphate exchangers [1,2]. The primary in vivo function of the ubiquitously expressed G6PT protein is to translocate G6P from the cytoplasm into the ER lumen where it couples with either the liver/kidney/intestine-restricted glucose-6-phosphatase-α (G6Pase-α) or the ubiquitously expressed G6Pase-ß to hydrolyze G6P to glucose and phosphate [3,4]. The G6PT/G6Pase-α complex maintains interprandial glucose homeostasis and the G6PT/G6Pase-ß complex maintains neutrophil energy homeostasis and functionality. Therefore, GSD-Ib is an autosomal recessive metabolic and immune disorder characterized by impaired glucose homeostasis, neutropenia and neutrophil dysfunction [3,4]. Recently, we showed that G6PTdeficient neutrophils from GSD-Ib patients receiving granulocytecolony stimulating factor (G-CSF) therapy exhibited impaired energy homeostasis and function [5], suggesting that G6PT-regulated G6P metabolism is important for neutrophil function. However, G-CSF failed to correct impaired neutrophil energy homeostasis in GSD-Ib [5].","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"6 1","pages":"1-2"},"PeriodicalIF":0.0,"publicationDate":"2017-02-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44259915","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}