Journal of glycobiology最新文献

{"title":"A Commentary on Development of Efficient Enzyme Cocktails for the Bioconversion of Hemicelluloses","authors":"Jian Liu, Hailong Li, L. Gan, M. Long","doi":"10.4172/2168-958x.1000123","DOIUrl":"https://doi.org/10.4172/2168-958x.1000123","url":null,"abstract":"The construction of minimum enzymes cocktails could facilitate the bioconversion of specified feedstocks into monosaccharides or XOS. In recent reported researches, the hemicelluloses and recombinant hemicellulases, including endo-s-1,4-xylanases, s-xylosidases, α-L-arabinofuranosidases, acetyl xylan esterase, feruloyl esterase and mannanase as well as their interaction mechanisms were investigated by enzymatic hydrolysis. Four representative interesting works on exploring the synergistic mechanisms and effects between enzymes were reported in this paper. Recombinant enzymes expressed from Pichia pastoris were characterized to reveal the mechanism during the process. This study contributes to the development of efficient enzyme cocktails for the bioconversion of hemicelluloses into monosaccharides and XOS.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":" ","pages":"1-2"},"PeriodicalIF":0.0,"publicationDate":"2017-01-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4172/2168-958x.1000123","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48402298","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":"Flow Lectin Affinity Chromatography-A Model with Sambucus nigraAgglutinin","authors":"M. L. Silva, C. Gomes, M. B. Q. Garcia","doi":"10.4172/2168-958X.1000121","DOIUrl":"https://doi.org/10.4172/2168-958X.1000121","url":null,"abstract":"The study of proteomes has become an important way to assess changes occurring in disease conditions. Nonetheless, the dominance of highly abundant serum proteins significantly complicates the discovery and analysis of low-abundant glycoproteins that may constitute potential disease biomarkers. Several techniques have been used to perform serum proteome partitioning such as affinity chromatography based on protein A and G, avian IgY, monoclonal antibodies and lectins. Lectins are particularly well-suited to bind and selectively isolate certain glycan structures present in complex samples like biological ones. The lectin reversibly captures glycoproteins with a particular glycostructure present in the sample in different abundance rates, yielding, after elution, an enriched pool of glycoproteins for glycoproteomic studies. However, lectin affinity chromatography (LAC) for biochemical applications is mainly carried out in batch conditions, which implies a long procedure time, expensive reagents or columns and special equipments or installations. This work proposes the development of a lab-made and easy to implement flow LAC procedure, using Sambucus nigra agglutinin (SNA) immobilized on agarose beads to isolate the STn glycan (a pan-carcinoma biomarker) present in glycoproteins of cancer patients serum. Under flow conditions, the proposed LAC procedure allows the automation of the process, especially important when several samples need to be run. Additionally, the flow system does not require expensive installations or experienced personnel, and it can be tailored to perform LAC with any lectin, according to the purpose of the glycoproteomic analysis. Significance: This work aims to demonstrate the feasibility and the benefits of performing lectin affinity chromatography under flow conditions and with a very simple flow manifold, when compared with the batch procedure usually carried out in Biochemistry and Molecular Biology laboratories. The easiness to implement this simple manifold, without requiring expensive equipments or installations, allows its use in any laboratory, even in those with financial limitations. Several advantages of the developed methodology are pointed out, versus the use of batch procedures or commercial kits or columns, especially when routine analyses need to be performed.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"6 1","pages":"1-7"},"PeriodicalIF":0.0,"publicationDate":"2017-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70859759","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":"Membrane Distribution and Activity of a Neuronal Voltage-Gated K+ Channel is Modified by Replacement of Complex Type N-Glycans with Hybrid Type.","authors":"M Kristen Hall,&nbsp;Douglas A Weidner,&nbsp;Sahil Dayal,&nbsp;Elena Pak,&nbsp;Alexander K Murashov,&nbsp;Ruth A Schwalbe","doi":"10.4172/2168-958X.1000128","DOIUrl":"https://doi.org/10.4172/2168-958X.1000128","url":null,"abstract":"<p><p>Abnormal modifications in N-glycosylation processing are commonly associated with neurological disorders, although the impact of specific N-glycans on neuronal excitability is unknown. By replacement of complex types of N-glycans with hybrid types in neuroblastoma cells, we provide the first study that addresses how distinct N-glycan types impact neuronal excitability. Using CRISPR/Cas9 technology, NB_1, a clonal cell line derived from rat neuroblastoma cells (NB), was modified to create an N-glycosylation mutant cell line, NB_1 (-Mgat2), which expresses predominantly hybrid type N-glycans. Western and lectin blotting, flow cytometry, TIRF and DIC microscopy, and patch clamp studies were conducted. Lectin binding revealed the predominant type of N-glycans expressed in NB_1 (-Mgat2) is hybrid while those of NB and NB_1 are complex. Kv3.1 b-expressing cells with complex N-glycans localized more glycosylated Kv3.1b to the neurites than cells with hybrid N-glycans. Further the absence of N-glycan attachment to Kv3.1b was critical for sub-plasma distribution of Kv3.1b to neurites in primary adult mammalian neurons, along with NB cells. Replacement of complex type N-glycans with hybrid type hindered the opening and closing rates of outward ionic currents of Kv3.1 b-expressing NB cells. The lacks of N-glycan attachment hindered the rates even more but were not significantly different between the NB cell lines. Taken together, our evidence supports N-glycosylation impacts the sub-plasma membrane localization and activity of Kv3.1 b-containing channels. We propose that N-glycosylation processing of Kv3.1 b-containing channels contributes to neuronal excitability, and abnormal modifications in N-glycosylation processing of Kv3.1b could contribute to neurological diseases.</p>","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"6 3","pages":""},"PeriodicalIF":0.0,"publicationDate":"2017-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4172/2168-958X.1000128","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36539687","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Pro-angiogenic Activity Assay of Chondroitin Sulfate and Glucosamine Sulfate on Vascular Network of Mouse and of Chick Embryo Chorioallantoic Membrane","authors":"Fernanda Katharine de Souza Lins Borba, Edbhergue Ventura Lola Costa, Viviane Aparecida Balvedi Polli, Daniela Sousa Coelho, M. Maraschin, Paulo Fernando Dias, Romildo Albuquerque Nogueira","doi":"10.4172/2168-958X.1000129","DOIUrl":"https://doi.org/10.4172/2168-958X.1000129","url":null,"abstract":"Objective: Target of this study was to test the capacity of chondroitin sulfate (CS) and glucosamine sulfate (GS) to induce in vivo angiogenesis. Methods: The proangiogenic activity of these compounds was analyzed through the assays in chorioallantoic membrane (CAM) of chick embryo and dorsal skin vascularization in mice, but before was realized a cell viability assay with human umbilical veins endothelial cells (HUVEC). Results: In the viability assay, concentrations tested between 30 and 3000 μg/ml showed a reduction of viable HUVEC number. In the CAM assay, CS and GS in an amount 2.0 mg/implant increased the vessels number as compared to control (phosphate buffered saline-PBS). In the assay of the dorsal skin vascularization of adult Swiss mice, the groups treated with CS (2 mg/implant; Gelfoam plug) exhibited an increase in the vessels number into plugs (0.52 ± 0.08 g/dl; measured as plug-hemoglobin content), a similar effect to that promoted by Fibroblast growth factor-2 (FGF-2; 50 ng/implant) (0.53 ± 0.1 g/dl). However the group treated with GS did not exhibit significant effect on mice skin vascularization. Conclusion: CS was capable to promote angiogenesis on CAM and dorsal skin vascularization, but GS only had pro-angiogenic activity in CAM vascular network.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"6 1","pages":"1-6"},"PeriodicalIF":0.0,"publicationDate":"2017-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4172/2168-958X.1000129","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70859821","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":"Effects of temperature and sodium hyaluronate on fluorescence of type-I calf skin solutions at physiological pH","authors":"J. Menter","doi":"10.4172/2168-958X.C1.004","DOIUrl":"https://doi.org/10.4172/2168-958X.C1.004","url":null,"abstract":"","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"04 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2016-09-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70860463","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":"Vitamin D3 deficiency in the aged","authors":"M. Anderson, Jelon Swope","doi":"10.4172/2168-958X.C1.005","DOIUrl":"https://doi.org/10.4172/2168-958X.C1.005","url":null,"abstract":"","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2016-09-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70860726","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":"Analytical glycomics: Biopharmaceutical applications","authors":"András Guttman","doi":"10.4172/2168-958X.C1.006","DOIUrl":"https://doi.org/10.4172/2168-958X.C1.006","url":null,"abstract":"","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2016-09-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70860952","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":"Parasite Lectins: More than Adhesion Molecules?","authors":"E. A. M. Silva, Thaís Viana Fialho Martins","doi":"10.4172/2168-958X.1000120","DOIUrl":"https://doi.org/10.4172/2168-958X.1000120","url":null,"abstract":"Several studies demonstrate the involvement of lectins in the recognition of carbohydrates present on the surface of different kinds of pathogens [1-3], including parasites of the genus Leishmania [4,5]. The recognition often involves the modulation of the host immune response due to the activation of signaling pathways initiated by the stimulation of lectins present on the surface of cells from immune system by carbohydrates from pathogens [1,2]. On the other hand, lectins from microorganisms are also involved in infections: HeparinBinding Protein (HBP) from Trypanosoma cruzi are involved in processes of amastigote and epimastigotes adhesion to the mammalian host cells and to the intestinal epithelium of insects, respectively [6-8]. Furthermore, galactose/N-acetylgalactosamine (Gal/GalNAc) lectin is involved in the infection by Entamoeba histolytica, responsible for the third highest number of death from parasitic diseases in the world [9-11]. Other relevant lectins from parasites are involved in mediating protozoa attachment to the host cells, acting as valuable tools to study pathogenesis of infection: mannose lectin (MBP) from Acanthamoeba, causative agent of keratitis, mediates parasite adhesion to the host cells, and may serve as a marker of pathogenicity of this parasite; micronemal protein (MIC1), a Toxoplasma gondii adhesin, bind to host sialic acid moieties, playing role in the parasite invasion and virulence; Tritrichomonas foetus lectin (TFL), a sialic acid specific lectin, is involved in mucosal surface attachment and immunogenicity of Tritrichomonas foetus, a protozoan parasite of the bovine urogenital tract; and Cryptosporidium parvum Clec (CpClec), a novel mucin-like glycoprotein with a C-type lectin domain (CTLD), is involved in Cryptosporidium-host cell interactions [12].","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"114 1","pages":"1-2"},"PeriodicalIF":0.0,"publicationDate":"2016-08-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70859699","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":"Influence of the Macro- and/or Microstructure of Cross-Linked Hyaluronic Acid Hydrogels on the Release of Two Model Drugs","authors":"K. Mondon, M. Dadras, J. Tillier, Samuel Gavard Molliard","doi":"10.4172/2168-958X.1000119","DOIUrl":"https://doi.org/10.4172/2168-958X.1000119","url":null,"abstract":"Injectable hyaluronic acid (HA) hydrogels, crosslinked with 1,4-butanediol diglycidyl ether (BDDE), are widely used in aesthetic medicine. Due to their high clinical tolerance, HA hydrogels are thought to be applicable as injectable drug delivery systems. Here, HA matrix structures of BDDE-crosslinked HA hydrogels were analysed, and the effects of the structures on the release of two model drugs were assessed. Seven crosslinked HA hydrogels were observed by optical microscopy and cryo scanning electron microscopy (cryo-SEM). We observed three specific matrix macrostructures under optical microscopy: two had a “spider web”-like structure, three had a particulate structure, and two had an intermediate structure. These differences were less evident under cryo-SEM, where all hydrogels exhibited fibrous microstructures of different homogeneity levels, with pore sizes between 0.5 and 18 μm. Three cross-linked HA hydrogels with different macrostructures were loaded with bovine serum albumin (BSA) and lidocaine to assess their capacities to release drug over 4 days. No differences in drug release were observed between gels, and BSA was released for up to 4 days, which was four times longer than lidocaine. Thus, BDDEcrosslinked HA hydrogels could be applied as an injectable drug delivery system, particularly for the delivery of high-molecular-weight molecules.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"5 1","pages":"1-7"},"PeriodicalIF":0.0,"publicationDate":"2016-08-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4172/2168-958X.1000119","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70859634","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 7D4, 4C3 and 3B3 (-) Chondroitin Sulphation Motifs are expressed at Sites of Cartilage and Bone Morphogenesis during Foetal Human Knee Joint Development","authors":"J. Melrose, Susan M. Smith, C. Hughes, C. Little, B. Caterson, A. Hayes","doi":"10.4172/2168-958X.1000118","DOIUrl":"https://doi.org/10.4172/2168-958X.1000118","url":null,"abstract":"Novel sulphation motifs within the glycosaminoglycan (GAG) chain structure of chondroitin sulphate (CS)- containing s are associated with sites of growth and differentiation in many biological systems where they function as molecular recognition sites involved in the binding, sequestration or presentation of soluble signalling molecules (e.g. growth factors, cytokines, morphogens). The specific sulphation motifs on CS identified by monoclonal antibodies 3-B-3(-), 4-C-3 and 7-D-4 are also associated with distinct cohorts of cells in areas of tissue morphogenesis in human foetal knee joint development. We hypothesize that such motifs may have roles to play in the regulation of proliferative/differentiative events during tissue morphogenesis. In the present investigation we have examined the distribution of these CS motifs within the rudiment cartilage, stromal connective tissues surrounding the rudiment cartilages and developing growth plates of the human foetal knee joint. These CS motifs had broad, overlapping distributions throughout the differentiating connective tissues undergoing morphogenesis and after joint cavitation were localised very specifically to the rudiment cartilage destined to form the permanent articular cartilage postnatally, and to the terminally differentiated chondrocytes and calcified cartilage-bone interface in the growth plate cartilages. The overlapping distributions of these molecules within the presumptive articular cartilage, prior to secondary ossification, suggests that they participate in early signalling events involved in tissue development and indicates that the cells within this zone are phenotypically distinct from those of the underlying rudiment cartilage.","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"5 1","pages":"1-9"},"PeriodicalIF":0.0,"publicationDate":"2016-07-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4172/2168-958X.1000118","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70859585","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}