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- 저자 : Rudolf Grimm (검색결과 4 건)
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Seunghyup Jeong,Serenus Hua,Do-Young Choi,Pyong-Gon Moon,Rudolf Grimm,Kwang Pyo Kim,Moon Chang Baek,Hyun Joo An 한국당과학회 2013 한국당과학회 학술대회 Vol.2013 No.1
Exosomes (microvesicles, or micropaticles) are small membrane-enclosed vesicles and these are secreted by various cell types, including tumor cells. These vesicles play an important role as mediators in extracellular communication. They are composed of membrane, cellular proteins, DNA, and RNA derived from their origin cells. It is also known that exosomes are involved in tumor metastasis, angiogenesis, and antitumor immunity. These biological functions are probably due to the glycosylation on their membrane proteins. Thus, the study of glycosylation of exosomes will be another potential source of new biomarker. However, there is a little study about the glycosylation of exosomes. Here, we targeted and analyzed N-glycans of exosomes derived from five cancer cell lines (A549, PC9, PC9/ZD, MCF-7, and MDA-MB231) using nano-LC/MS. We also have compared glycans of exosomes with glycans on their origin cell membrane to examine glycosylation correlation between origin cells and exosomes on three lung cancer cell lines. Additionally, we have compared anticancer drug resistant cell line PC9/ZD (Gefitinib resistant) and untreated PC9 in terms of origin cells and exosomes glycan profiling via isomer separation. Exosomes and cell membranes were prepared from three lung cancer cell lines: A549, PC9, and PC9/ZD. And two breast cancer exosomes were prepared: MCF-7 and MDA-MB231. Glycans were released by PNGase F, then enriched by graphitized carbon solid phase extraction. Nano-LC/chip Q-TOF MS was used for overall glycan profiling and quantitation. We successfully release and profile N-glycans from exosomes. Origin cells and exosomes of lung cancer contain high-mannose glycans in abundance. Although, exosomes have less high-mannose glycans compared with origin cells. Both origin cells and exosomes, isomer separation of sialylated glycans are different between PC9 and PC9/ZD. On breast cancer exosomes, two different matastatic samples represent quite different profiling. This is the first study of comprehensive glycan profiling of exosomes using mass spectrometry.
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Identification and Accurate Quantitation of Biological Oligosaccharide Mixtures
Strum, John S.,Kim, Jaehan,Wu, Shuai,De Leoz, Maria Lorna A.,Peacock, Kyle,Grimm, Rudolf,German, J. Bruce,Mills, David A.,Lebrilla, Carlito B. American Chemical Society 2012 ANALYTICAL CHEMISTRY - Vol.84 No.18
<P>Structure-specific characterization and quantitation is often required for effective functional studies of oligosaccharides. Inside the gut, HMOs are preferentially bound and catabolized by the beneficial bacteria. HMO utility by these bacteria employs structure-specific catabolism based on a number of glycosidases. Determining the activity of these enzymes requires accurate quantitation of a large number of structures. In this study, we describe a method for the quantitation of human milk oligosaccharide (HMO) structures employing LC/MS and isotopically labeled internal standards. Data analysis was accomplished with a newly developed software tool, LC/MS Searcher, that employs a reference structure library to process LC/MS data yielding structural identification with accurate quantitation. The method was used to obtain a meta-enzyme analysis of bacteria, the simultaneous characterization of all glycosidases employed by bacteria for the catabolism of milk oligosaccharides. Analysis of consumed HMO structures confirmed the utility of a β-1,3-galactosidase in <I>Bifidobacterium longum subsp. infantis</I> ATCC 15697 (<I>B. infantis</I>). In comparison, <I>Bifidobacterium breve</I> ATCC 15700 showed significantly less HMO catabolic activity compared to <I>B. infantis</I>.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/ancham/2012/ancham.2012.84.issue-18/ac301128s/production/images/medium/ac-2012-01128s_0002.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/ac301128s'>ACS Electronic Supporting Info</A></P>
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Oh, Myung Jin,Hua, Serenus,Kim, Bum Jin,Jeong, Ha Neul,Jeong, Seung Hyup,Grimm, Rudolf,Yoo, Jong Shin,An, Hyun Joo Future Science 2013 Bioanalysis Vol.5 No.5
<P>Erythropoietin is a therapeutic glycoprotein that stimulates red blood cell production. The quality, safety and potency of recombinant erythropoietins are determined largely by their glycosylation. Small variations in cell culture conditions can significantly affect the glycosylation, and therefore the efficacy, of recombinant erythropoietins. Thus, detailed glycomic analyses are necessary to assess biotherapeutic quality. We have developed a platform for qualitative and quantitative glycomic analysis of recombinant erythropoietins.</P>
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