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RISS 인기검색어
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- 저자 : Dimapasoc, Lauren M. (검색결과 5 건)
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Hua, S.,Williams, C.C.,Dimapasoc, L.M.,Ro, G.S.,Ozcan, S.,Miyamoto, S.,Lebrilla, C.B.,An, H.J.,Leiserowitz, G.S. Elsevier 2013 Journal of chromatography A Vol.1279 No.-
Aberrant glycosylation has been observed for decades in essentially all types of cancer, and is now well established as an indicator of carcinogenesis. Mining the glycome for biomarkers, however, requires analytical methods that can rapidly separate, identify, and quantify isomeric glycans. We have developed a rapid-throughput method for chromatographic glycan profiling using microfluidic chip-based nanoflow liquid chromatography (nano-LC)/mass spectrometry. To demonstrate the utility of this method, we analyzed and compared serum samples from epithelial ovarian cancer cases (n=46) and healthy control individuals (n=48). Over 250 N-linked glycan compound peaks with over 100 distinct N-linked glycan compositions were identified. Statistical testing identified 26 potential glycan biomarkers based on both compositional and structure-specific analyses. Using these results, an optimized model was created incorporating the combined abundances of seven potential glycan biomarkers. The receiver operating characteristic (ROC) curve of this optimized model had an area under the curve (AUC) of 0.96, indicating robust discrimination between cancer cases and healthy controls. Rapid-throughput chromatographic glycan profiling was found to be an effective platform for structure-specific biomarker discovery.
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Hua, Serenus,Jeong, Ha Neul,Dimapasoc, Lauren M.,Kang, Inae,Han, Chanyoung,Choi, Jong-Soon,Lebrilla, Carlito B.,An, Hyun Joo American Chemical Society 2013 ANALYTICAL CHEMISTRY - Vol.85 No.9
<P>Mice are the premier mammalian models for studies of human physiology and disease, bearing extensive biological similarity to humans with far fewer ethical, economic, or logistic complications. To facilitate glycomic studies based on the mouse model, we comprehensively profiled the mouse serum N-glycome using isomer-specific nano-LC/MS and -LC/MS/MS. N-Glycans were identified by accurate mass MS and structurally elucidated by MS/MS. Porous graphitized carbon nano-LC was able to separate out nearly 300 N-linked glycan compounds (including isomers) from just over 100 distinct N-linked glycan compositions. Additional MS/MS structural analysis was performed on a number of novel N-glycans, revealing the structural characteristics of modifications such as dehydration, O-acetylation, and lactylation. Experimental findings were combined with known glycobiology to generate a theoretical library of all biologically possible mouse serum N-glycan compositions. The library may be used for automated identification of complex mixtures of mouse N-glycans, with possible applications to a wide range of mouse-related research endeavors, including pharmaceutical drug development and biomarker discovery.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/ancham/2013/ancham.2013.85.issue-9/ac400195h/production/images/medium/ac-2013-00195h_0007.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/ac400195h'>ACS Electronic Supporting Info</A></P>
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Serenus Hua,Inae Kang,Lauren M. Dimapasoc,Hyun Joo An 한국당과학회 2012 한국당과학회 학술대회 Vol.2012 No.1
In vivo medical research relies primarily on the common laboratory mouse, who exhibits an inherent similarity to its fellow mammal, the human, yet is much more amenable to experimentation (for ethical, economic, and life cycle -related reasons). Numerous studies have elucidated the genome, proteome, and metabolome of the various mouse models available, but few if any have paid any attention to the mouse glycome. However, glycosylation is one of the most common eukaryotic post-translational modifications, and variations in glycosylation have been linked to cancer and other important human diseases by over fifty years of glycobiological research. Elucidation of the mouse glycome would aid glycomic and glycoproteomic biomarker studies based on the mouse model and advance our understanding of mice as models for humans. We have used retrosynthetic analysis to create a library of all possible mouse serum N-glycan compositions, based on our knowledge of the N-glycan biosynthesis pathway. Highly sensitive nano-LC/MS profiling of mouse serum N-glycans allowed us to annotate the theoretical library with experimental data, while isomer-specific nano-LC/MS/MS provided structural information. The annotated mouse serum N-glycan library was applied to automated data analysis of large sample sets for the purposes of biomarker discovery.
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Human Cell Surface Glycan Mapping using Mass Spectrometry
Hyun Joo An,Mary Saunders,Shuai Wu,Jaehan Kim,Lauren Dimapasoc,Kit S. Lam,Carlito B. Lebirlla 한국당과학회 2011 한국당과학회 학술대회 Vol.2011 No.1
Every cell in an organism synthesizes a heterogeneous array of glycans in the form of various structures. Cell surface glycosylation may play an important role in development and may provide important new sources of markers for differentiation. However, studies regarding the glycosylation of cell surfaces are limited due to the lack of sensitive analytical methods. A mass spectrometry-based method that enables specific detection and quantitation, and acquisition of structural information has been developed. We have mapped cell surface glycans from more than 30 human cell lines including embryonic stem cells, cancer cells, and somatic cell lines. The results represent that specific surface glycomic signatures might have functional implications as well as characteristic features of a specific cell type.
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Tissue O-glycan Profile Alter during Mouse Natural Aging
Bum Jin Kim,Hyoung Jin Jeong,Serenus Hua,Sureyya Ozcan,Lauren Dimapasoc,Ik-Soon Jang,Jong-Soon Choi,Hyun Joo An 한국당과학회 2013 한국당과학회 학술대회 Vol.2013 No.1
Age-related biochemical and physiological changes have been found in all of the body's cells, tissues, and organs, affecting the function of all body systems. Glycosylation also undergoes changes in the pathophysiological process of aging. Glycosylation, which is highly sensitive to the biochemical environment, is a common post-translational modification of proteins, with over 50% of all human proteins glycosylated. Unlike N-glycans, the research of O-glycan for aging and longevity biomarkers are more challenging owing to the absence of abroad-specificity glycosidase for the release of O-glycans from glycoproteins. In this study, O-glycans in mouse skin tissues were chemically released by reductive β-elimination and analyzed by nano-LC chip/Q-TOF mass spectrometry (Nano-LC/MS). O-glycan enrichment was dramatically improved by optimized lipid removal prior to glycan release. The 20 O-glycan compositions were found in mouse skin tissues by Nano-LC/MS, and O-glycan structures were elucidated by tandem MS. Isomer-specific glycan analysis was successfully performed by accurate mass Q-TOF MS coupled with chip-based liquid chromatography. The alteration of O-glycans during aging was monitored by quantitative analysis. Furthermore, we could identify the relative contribution of neutral, sialylated and fucosylated glycan types. Sialylation was found to be highly correlated with the aging process. Further studies with larger sample sets will help confirm the initial data and lead to more confident detection of aging biomarkers.
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