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Pine Brook, NJ, United States

Hirose K.,Hokkaido University | Amano M.,Hokkaido University | Hashimoto R.,Hokkaido University | Lee Y.C.,Johns Hopkins University | And 3 more authors.
Biochemistry | Year: 2011

A large set of glycome information was obtainedfrom egg white proteins of 88 samples from Galloanserae (63 Anseriformes and 25 Galliformes). The data were obtained on whole N-glycan structures and types of sialic acids of these egg whites by glycoblotting-based high-throughput and quantitative glycomics. The results revealed clear trends and complexity patterns as well as diversity among taxonomic groups. It is wellknown that chicken, a representative domesticated poultry involved in Galliformes, can become an influenza host.However, our data demonstrate that duck, wild goose, and swan of Anseriformes are representative migratory birds that are known as natural hosts of the influenza virus. Hierarchical clustering analysis of the expression pattern of N-glycome (total of 61 N-glycan peaks) revealed that the members of Galloanserae can be classified into two major groups and five submajor clusters (clusters 1-5) on the basis of simple m/z values obtained by MALDITOF MS. It is clear that expression patterns of N-glycomes in the five clusters are influenced significantly by the features such as the body size of the birds, rather than by the difference of the family. On the other hand, quantitative analysis showed that the total amounts of sialic acids in egg whites of Galliformes were distinctly larger than those of Anseriformes. However, it was also revealed in Anseriformes that Neu5Gc and KDN, in addition to common Neu5Ac, were expressed significantly in both N- and O-glycans of glycoproteins and glycosphingolipids, suggesting the influence of their lifestyles and diet. This is the first report that KDN exists in egg white. These results and the environmental factors are discussed preliminarily with respect to their evolutionary lineage. © 2011 American Chemical Society.


Nakahara T.,Ezose Sciences
Trends in Glycoscience and Glycotechnology | Year: 2013

Research in glycomics and glycoproteomics is making rapid progress as a result of technological advances in mass spectrometry. Bioinformatics is an indispensable discipline for analyzing overwhelming amounts of information generated by mass spectrometry. This minireview summarizes bioinformatics contributions to glycan mass spectrometry data analysis. To simplify the discussion on the wide range of bioinformatics contributions to this field, the research shown here will be categorized into three areas; "Calculator-type tools," "Technologies for glycan structure determination by tandem MS" and "Other noteworthy bioinformatics technologies for MS." Lastly, future prospects of the contribution of bioinformatics to glycobiology will be discussed. © 2013 FCCA (Forum: Carbohydrates Coming of Age).


Kurogochi M.,Hokkaido University | Matsushista T.,Hokkaido University | Amano M.,Hokkaido University | Furukawa J.-I.,Hokkaido University | And 4 more authors.
Molecular and Cellular Proteomics | Year: 2010

Despite increasing importance of protein glycosylation, most of the large-scale glycoproteomics have been limited to profiling the sites of N-glycosylation. However, in-depth knowledge of protein glycosylation to uncover functions and their clinical applications requires quantitative glycoproteomics eliciting both peptide and glycan sequences concurrently. Here we describe a novel strategy for the multiplexed quantitative mouse serum glycoproteomics based on a specific chemical ligation, namely, reverse glycoblotting technique, focusing sialic acids and multiple reaction monitoring (MRM). LC-MS/MS analysis of de-glycosylated peptides identified 270 mouse serum peptides (95 glycoproteins) as sialylated glycopeptides, of which 67 glycopeptides were fully characterized by MS/MS analyses in a straightforward manner. We revealed the importance of a fragment ion containing innermost N-acetylglucosamine (GlcNAc) residue as MRM transitions regardless the sequence of the peptides. Versatility of the reverse glycoblotting-assisted MRM assays was demonstrated by quantitative comparison of 25 targeted glycopeptides from 16 proteins between mice with homo and hetero types of diabetes disease model. © 2010 by The American Society for Biochemistry and Molecular Biology, Inc.


Cancer-associated O-glycopeptide combination epitopes derived from the VNTR of MUC1 are disclosed. Autoantibodies present in human sera target the combination epitopes and are reduced or absent in cancer patients. The epitopes are useful as therapeutic and immunoprophylactic cancer vaccines. Monoclonal antibodies directed against the epitopes are also useful as immunotherapeutics for treatment and prevention of cancer. Diagnostic methods using the epitopes and antibodies are also disclosed.


Trademark
Ezose Sciences | Date: 2009-06-30

Diagnostic reagents for research, clinical, or medical laboratory use; diagnostic kits comprised of reagents and assays for research, scientific, and clinical purposes. Diagnostic kits comprised of reagents and assays for medical purposes. Wholesale distributorship services of pharmaceutical preparations, vaccines, and diagnostic and therapeutic applications. Research and development of vaccines.

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