Journal of glycomics & lipidomics最新文献

{"title":"Podocalyxin-Targeting Comparative Glycan Profiling Reveals Difference between Human Embryonic Stem Cells and Embryonal Carcinoma Cells","authors":"Yoko Itakura, A. Kuno, M. Toyoda, A. Umezawa, J. Hirabayashi","doi":"10.4172/2153-0637.S5-004","DOIUrl":"https://doi.org/10.4172/2153-0637.S5-004","url":null,"abstract":"Background: Human embryonic stem cells (hESCs) and human embryonal carcinoma cells (hECCs) have been extensively used for stem cell research. Although these cells are known to share many properties including high developmental capability and cell surface antigens, their origins are basically different: hECSs are derived from inner cell mass of blastocysts, while hECCs are from malignant tumors. Thus, the lack of a good method to differentiate these pluripotent cells remains a critical issue to diagnose tumorigenic potential of pluripotent stem cells for their medical applications. In this context, development of specific markers to distinguish hESCs from hECCs is also of clinical value. \u0000Method: In this study, we focused our glycan analysis on a carbohydrate-rich glycoprotein, podocalyxin, known as a carrier of TRA-1-60 and TRA-1-81 antigens, which represent hESC glycan markers. The target glycoprotein semi-quantified by immunoblotting was enriched from the cell extracts by immunoprecipitation, and the glycosylation differences occurring between hESCs and hECCs were systematically analyzed by an advanced technology of lectin microarray, antibody-overlay lectin profiling (ALP). Profiles of human embryonic bodies (hEBs) differentiated from hESCs were also analyzed. \u0000Results and Conclusion: A glycan profile of podocalyxin from hECCs was significantly different from that of hESCs. Lectin signals corresponding to α2-6 linked sialic acid were elevated in the hECCs, and glycosidase digestions further revealed significant difference in the non-reducing terminal and penultimate structures. These results demonstrate that the present procedure with focus on a particular glycoprotein could enhance relatively small but significant differences between closely related cells like hESCs and hECCs at the glycome level. The present finding will be helpful to develop a diagnostic method to distinguish undifferentiated stem cells from differentiated ones used for regenerative therapy.","PeriodicalId":89585,"journal":{"name":"Journal of glycomics & lipidomics","volume":"2012 1","pages":"1-10"},"PeriodicalIF":0.0,"publicationDate":"2013-02-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70234739","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":"Thyroid Status in Diabetes Mellitus","authors":"Bharat, Davina Hijam, David Gangte, Lalnunpui, Premch, I. Swarnalatha Devi, G. Singh","doi":"10.4172/2153-0637.1000106","DOIUrl":"https://doi.org/10.4172/2153-0637.1000106","url":null,"abstract":"The study was carried out to estimate thyroid hormones (T3, T4 and TSH) level in diabetic patients and to compare it with normal controls in an attempt to find out the importance of thyroid hormone estimation in diabetic cases. Sixty cases of diabetes mellitus who attended Diabetic Clinic, RIMS during the period from October 2008 to March 2010 were taken as the cases and 30 healthy individuals were selected as control group. Serum total Tri-iodothyronine (T3), thyroxine (T4), thyroid stimulating hormone and blood sugar were estimated in the cases and controls. The study showed that diabetes was more prevalent in the age group of 51-65 years, and more in males (52%). The mean fasting blood sugar (126.17 ± 37.92 mg%) and serum TSH level (4.58 ± 2.90 mIU/L)were increased significantly (r=0.884, p>0.05) whereas serumT4 level (5.79 ± 4.39 μg/dl) was decreased significantly in diabetic cases when compared with controls. Mean T3 level of diabetic cases was higher than controls but it was insignificant. Diabetes mellitus cases with statistically significant higher TSH value have complications like hypertension, retinopathy, nephropathy etc. A statistically significant, negative correlation (r=-0.942, p<0.05) was seen between Serum T4 and blood sugar in the cases. Therefore, routine assessment of thyroid hormone level in addition to other biochemical variables in the early stage of diabetes will help in the management of these patients.","PeriodicalId":89585,"journal":{"name":"Journal of glycomics & lipidomics","volume":"3 1","pages":"1-4"},"PeriodicalIF":0.0,"publicationDate":"2013-01-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70229947","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":"Quantitative Matrix-assisted Laser Desorption/ionization Mass Spectrometry of Pyrene-derivatized Glycopeptides for Investigation of Mammalian Cell Glycomics","authors":"Toshio Nakamura, Takashi Nishikaze, Hiroshi Jinmei, Fumio Tougasaki, Ichiro Sugimoto, J. Amano","doi":"10.4172/2153-0637.S5-001","DOIUrl":"https://doi.org/10.4172/2153-0637.S5-001","url":null,"abstract":"Glycan is one of the major information-rich biomolecules. Alterations in N-glycans can be associated with many diseases including cancer, and are often observed in the serum of affected patients. As an example, prostate-specific antigen (PSA) is a glycoprotein secreted by prostatic epithelial cells. The serum PSA assay is widely used for detection of prostate cancer (PCa). Detection of altered PSA glycan is regarded as a precise diagnosis. However, the limited amount of serum PSA available makes it difficult to determine detailed glycan structures, as the PSA level in serum is very low. Mass spectrometry (MS) is a powerful tool for analyzing glycan structures. We have recently established a highly sensitive MS for both glycans and glycopeptides by pyrene derivatization. Matrix-assisted laser desorption/ionizationquadrupole ion trap-time of flight (MALDI-QIT-TOF) mass spectra of glycans derivatized with pyrene butanoic acid hydrazide (PBH) were compared with those of pyridylaminated (PA) glycans. Each derivatized glycan was prepared from the same amount of commercial PSA. PBH-labeled PSA glycans showed higher signal intensity with less fragmentation compared with PA-glycans, and gave spectra with high s/n ratio (in both positive- and negative-ion modes). For derivatization of the glycopeptides, pyrenyl diazomethane (PDAM) was used. The glycopeptide signals were greatly enhanced by this derivatization. PDAM-glycopeptides prepared from about 10 ng of PSA could be determined. In this study, we demonstrated that MS analysis using pyrene derivatization provides higher sensitivity and stability for both glycans and glycopeptides, compared with HPLC and lectin affinity chromatography; furthermore comparable results were obtained to those seen with the other methods. We therefore conclude that our method is useful for investigation of mammalian cell glycomics.","PeriodicalId":89585,"journal":{"name":"Journal of glycomics & lipidomics","volume":"2012 1","pages":"1-5"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70234549","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":"Explaining the Recent Fish Oil Trial \"Failures\"","authors":"J. DiNicolantonio, A. Niazi, J. O’Keefe, C. Lavie","doi":"10.4172/2153-0637.1000E112","DOIUrl":"https://doi.org/10.4172/2153-0637.1000E112","url":null,"abstract":"1Department of Medicine, Wegmans Pharmacy, Ithaca, New York, USA 2Department of Medicine, Shifa College of Medicine, Islamabad, Pakistan 3Department of Medicine, Mid American Heart Institute, University of Missouri-Kansas City, Kansas City, Missouri, USA 4Department of Medicine, John Ochsner Heart and Vascular Institute, Ochsner Clinical SchoolThe University of Queensland School of Medicine, New Orleans, LA and Pennington Biomedical Research Center, Baton Rouge, Louisiana, USA","PeriodicalId":89585,"journal":{"name":"Journal of glycomics & lipidomics","volume":"2013 1","pages":"1-4"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70233449","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":"Mammalian Cell Glycomics","authors":"Koichi Kato","doi":"10.4172/2153-0637.S5-E001","DOIUrl":"https://doi.org/10.4172/2153-0637.S5-E001","url":null,"abstract":"","PeriodicalId":89585,"journal":{"name":"Journal of glycomics & lipidomics","volume":"2012 1","pages":"1-1"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70234983","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":"GnT V-Catalyzed N-glycan Products are not increased in Hepatomas","authors":"Akihiro Deguchi, S. Hitoshi, Takeshi Yoshimura, I. Fujimoto, T. Ikeda, A. Ishii, Mikito Higashi, T. Masaki, S. Kuriyama, K. Ikenaka","doi":"10.4172/2153-0637.S5-003","DOIUrl":"https://doi.org/10.4172/2153-0637.S5-003","url":null,"abstract":"Sugar chains envelop the vast majority of the cell surface and thus have been considered to play pivotal roles in cell-to-cell and cell-to-extracellular matrix interactions. Recent studies have shown that expression of N-acetylglucosaminyltransferase (GnT) V is induced in hepatomas, and high-branched N-linked sugar chains play important roles in carcinogenesis and metastasis. However, the precise structural changes have not yet been studied in detail. Here, we compared sugar chains expressed in normal mouse liver, regenerating liver, three mouse hepatoma cell lines and Hepa 1-6-related tumors obtained by inoculation of Hepa 1-6 cells into liver or subcutaneous tissue of BALB/c nu/nu mice. The products of GnT V were found to be present in similar proportions in the mouse liver and in hepatomas, while there was a big difference in the amount of GnT IV products in these organs. Normal mouse liver and regenerating mouse liver contained small amounts of sugar chains produced by the action of GnT IV, while such chains were abundant in hepatoma cell lines and in Hepa 1-6-related tumors. Analysis of N-linked sugar chains in human livers and in hepatocellular carcinoma (HCC) revealed that both GnT IV and GnT V products are present in human liver, but their total content did not change during malignant transformation. Thus there was no increase in GnT V N-glycan products in hepatoma tissues in the mouse model or in humans.","PeriodicalId":89585,"journal":{"name":"Journal of glycomics & lipidomics","volume":"2012 1","pages":"1-6"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70234185","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":"N-Glycosylation Profiles of Chicken Immunoglobulin Y Glycoproteins Expressed by Different Production Vehicles","authors":"Sachiko Kondo, H. Yagi, Y. Kamiya, Akihiko Ito, Motoki Kuhara, Ayako Kudoh, N. Takahashi, Koichi Kato","doi":"10.4172/2153-0637.S5-002","DOIUrl":"https://doi.org/10.4172/2153-0637.S5-002","url":null,"abstract":"Immunoglobulin Y (IgY), abundant in egg yolk, is widely used as an immunochemical reagent and has been recently appreciated as a potential therapeutic tool. The Fc portion of IgY conserves an N-glycosylation site at Asn407, which is structurally equivalent to conserved glycosylation sites of other Ig classes in mammals. Despite such similarities, IgYs from chicken serum and egg yolk have been shown to be distinct glycoforms, best exemplified by the high incidence of monoglucosylated high mannose-type oligosaccharides, which are rarely found in mammalian glycoproteins. To gain further insight into the glycosylation properties of IgY, we report a comparative N-glycosylation profiling of recombinant chicken IgYs that have identical amino acid sequences in their variable regions but are expressed by different production vehicles. The N-linked oligosaccharides cleaved from these IgYs were subjected to multidimensional HPLC mapping in conjunction with mass spectrometric analyses. N-glycosylation profiles of the IgYs showed obviously different patterns depending on the production vehicle. While IgY expressed by chicken hybridoma cells retained the premature high mannose-type oligosaccharides, IgY expressed by CHO cells experienced extensive N-glycan processing and displayed high antennary oligosaccharides. Significant differences were also observed in the levels of core fucosylation and bisecting N-acetylglucosaminylation and in sialyl linkage types among the IgYs expressed by different vehicles. Despite such differences, the recombinant IgY antibodies commonly expressed considerable populations of monoglucosylated glycoforms, suggesting that this glycosylation feature is, to some extent, associated with the distinctive quaternary structure of IgY-Fc, which, at least partially, masks the Asn407 N-glycans and sequesters them from chaperone mechanisms in the endoplasmic reticulum. We suggest that the timing and efficiency of N-glycan processing and the quaternary structure formation of IgY are considerably different from those of IgE and depend on the vehicles used for recombinant IgY production, resulting in varying incidence of monoglucosylated species.","PeriodicalId":89585,"journal":{"name":"Journal of glycomics & lipidomics","volume":"2012 1","pages":"1-5"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70234175","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":"Ceramide Profiles of Human Serum Gangliosides GM2 and GD1a exhibit Cancer-associated Alterations","authors":"Stephan Kirsch, Jamal Souady, Michael Mormann, L. Bindila, JasnaPeter-KataliniÄ","doi":"10.4172/2153-0637.S2-005","DOIUrl":"https://doi.org/10.4172/2153-0637.S2-005","url":null,"abstract":"Human serum gangliosides were analyzed by nano-HPLC/MS to characterize their glycoforms and ceramide profiles within a single experiment. This unbiased glycosphingolipidomics approach was successfully applied to a set of clinical samples of gastric and pancreatic cancer patients and related control cohorts. Evaluation of acquired data revealed no clear differences with respect to ganglioside glycoforms among the patient groups investigated. However, significant alterations were observed within the ceramide profiles of different ganglioside structures, particularly pronounced for gangliosides GM2 and GD1a. Based on the increase of palmitic acid-comprising structures and the concurrent decrease of stearic acid-comprising ganglioside signals observed for both glycoforms, the ceramide ratio of these signals was applied for discrimination of cancer patients from control sample cohorts. Based on the performance evaluated in statistical analyses, the GM2-related ceramide ratio is proposed as a potential biomarker in particular for pancreatic cancer. Although further validation is required to determine its capability for cancer detection in mass screenings and its applicability for clinical routine, the data presented here support a promising perspective for applications.","PeriodicalId":89585,"journal":{"name":"Journal of glycomics & lipidomics","volume":"470 1","pages":"1-10"},"PeriodicalIF":0.0,"publicationDate":"2012-12-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70234473","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":"Opportunities in Bacterial Cell Wall Biogenesis","authors":"C. Reid, Danielle Gutelius","doi":"10.4172/2153-0637.1000E110","DOIUrl":"https://doi.org/10.4172/2153-0637.1000E110","url":null,"abstract":"One of the foremost challenges in the management of infectious diseases is antimicrobial resistance. The manifestation of multidrug resistance in bacteria, over the past several decades has resulted in one of the most pressing clinical problems in modern medicine. The Infectious Disease Society of America has identified a number of Grampositive and Gram-negative human pathogens that pose a significant \u0000challenge in infectious disease management.","PeriodicalId":89585,"journal":{"name":"Journal of glycomics & lipidomics","volume":"2 1","pages":"1-3"},"PeriodicalIF":0.0,"publicationDate":"2012-09-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70233037","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":"In situ Monitoring of In vitro Sialylation by Inclusion Bodies","authors":"Klaudia Talafová, Jozef Nahalka","doi":"10.4172/2153-0637.1000105","DOIUrl":"https://doi.org/10.4172/2153-0637.1000105","url":null,"abstract":"Sialic acids usually terminate oligosaccharide chains expressed on the cell surfaces and glycoproteins of vertebrates, higher invertebrates and some microorganisms. They have various important biological roles. Two of these roles, determination of anti-inflammatory activity of IgG antibodies and increasing the circulating half-life of glycoproteins and blood cells, can find application in pharmaceutical industry and medicine. For this reason, there is a need for efficient in vitro protein sialylation processes. To evaluate the efficiency of in vitro sialylation, a method for in situ monitoring in high throughput screens has been developed. It is represented by hemagglutination caused by inclusion bodies of SabA lectin. SabA lectins are proteins expressed on the cell surface of bacteria Helicobacter pylori and bind to sialic acids on the host cell surfaces. They are responsible for H. pylori mediated agglutination of erythrocytes in vitro. This presented method is fast, simple and one can avoid time-consuming purification of analyzed glycoprotein. In addition, it could provide a basic diagnostic method for determination of sialylation level of erythrocytes.","PeriodicalId":89585,"journal":{"name":"Journal of glycomics & lipidomics","volume":"2012 1","pages":"1-5"},"PeriodicalIF":0.0,"publicationDate":"2012-09-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70229852","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}