Day 3 :
Korea University, South Korea
Keynote: Glycosylated ribosomal protein S3, secreted from various cancer cells, is a possible cancer biomarker.
Time : 09:00-09:30
Prof. Joon Kim has completed his BS and MS from Seoul National University, PhD in Biochemistry from the University of California at Berkeley and postdoctoral study from Harvard Medical School. He is a Professor in the Division of Life Sciences, and Director of Radiation Safety and Management Center, Korea University, Seoul, Korea. He has published more than 160 papers in reputed journals
Ribosomal protein S3(rpS3) is a genuine component of the 40S ribosomal small subunit. However, it has been known as a versatile protein with multiple other extra-ribosomal functions in apoptosis, cell cycle control, DNA repair etc. It has a DNA repair endonuclease activity which is related with various cancers. Recently, we have discovered that this protein forms a dimer and is secreted after N- glycosylation. It is secreted only from various cancer cells but not in normal cells. We also have confirmed that rpS3 is secreted more into media when cancer cells are more invasive. The secretion pathway turned out to be a standard ER-Golgi dependent pathway. We are currently developing various antibodies against rpS3 which could be used as useful reagents for future cancer biomarkers.
Fig 1. Cell Migration Assay for Invasive Cancer Cells
- Track 9: Glycoprotein Technologies
Track 10: Glyco Bioinformatics
Track 11: Glyco Proteomics
Track 12: Glycans in Genetic Disorders
Location: Holiday Inn London - Brentford Lock
Korea University, South Korea
Nanyang Technological University, Singapore
Xue-Wei Liu, China Agricultural University (BSc & MSc 1996), University of Southern California (PhD 2000), Procter & Gamble (Research Scientist, 2000-2002), Chugai Pharma USA (Senior Research Scientist, 2002-2003), Caltech (Postdoc, 2003-2005). Currently Assoc/Professor at Nanyang Technological University, Singapore. Research field: carbohydrate chemistry, natural products, and glycoproteins in addressing problems of medicinal and biochemical significance.
Glycopeptides and glycoproteins play vital roles in a wide array of biological activities including cell-cell adhesion, cell differentiation, cell growth and tumour metastasis. In addition, a host of major illnesses such as autoimmune diseases, infectious diseases and cancer are caused by aberrant protein glycosylation. Consequently, the development of new glycopeptides-based vaccines, diagnostics and therapeutics has gained significant interests, stimulating the study of glycopeptide synthesis. Here, a practical approach towards N-glycopeptide synthesis using an auxiliary-mediated dual native chemical ligation (NCL) is presented. The first NCL connects an N-linked glycosyl auxiliary to the thioester side chain of an N-terminal aspartate oligopeptide. This intermediate undergoes a second NCL with a C-terminal thioester peptide. Mild deprotection provides the desired N-glycopeptide. The flexibility and systematic control of our method clearly have significant advantages over preceding ones and present a major step forward in glycoscience. Taking into consideration of the previous approaches, our method offers an attractive and practical procedure to N-glycopeptide that does not require cysteine residue, allowing for straightforward glycosylation and ligation at aspartic acid terminal. The auxiliary-linked glycosyl donor can be obtained from readily available glycosyl azide. Our method can leverage modern techniques such as intein-mediated ligation or recombinant expression to gain access to peptides of virtually any length and order. In addition, quick access to polymeric peptidoglycans will also be presented.
Ege University, Turkey
She received her BSC degree in Biochemistry, Faculty of Science from Ege University in 2006. She is currently doing her master thesis about “Glycan Analysis of Monoclonal Antibodies” and she will be graduated at 2017 summer. At the same time she is working as a scientific researcher at the Center for Drug Research & Development and Pharmacokinetic Applications (ARGEFAR) since 2008. Her professional experience includes usage of HPLC, LC MS, MALDI TOF MS techniques. Her research interest covers physicochemical characterization of biosimilar drugs and biopharmaceutics.
Monoclonal antibodies (MAbs) are increasingly being used for the treatment of cancer or other autoimmune diseases. Correct glycan structure of MAbs is essential for functional and biological activity of the related Mab such as identification of antigens triggered by immune system cells, regulation of the signaling activities and physicochemical properties of produced therapeutics etc. Therefore, rapid monitoring of glycan structure is very critical for therapeutic drug production, biosimilar drug production and their quality control processes.
The principal of this study is the characterization of glycan structure of MAbs. In our study, glycan structure of trastuzumab, used as a drug for the treatment of breast cancer, was characterized. N-glycans were enzymatically released from Trastuzumab protein structure by trypsin digestion and PNGase F (Peptide:N-Glycosidase F) cleavage. Moreover, special buffer exchange and Solid Phase extraction procedures were used for the clean-up purposes prior to MALDI-TOF-MS (Matrix Assisted Laser Desorption/Ionization-Time of Flight- Mass Spectrometry) detection.
After designing appropriate sample treatment and optimization, GO, GOF, G1, G1F, GOF-GN glycans were clearly detected by MALDI-Q-IT-TOF MS without any labelling or using any additional chromatographic separation methods.
The current talk deals with the theoretical and experimental aspects of MALDI-Q-IT-TOF MS for the study of glycans on monoclonal antibodies. Sample preparation procedures and tips for MALDI-TOF-MS measurements will be addressed and the original data obtained from MALDI-Q-IT-TOF MS will be presented.
Infinitus (China) Company Ltd., China
Minghua Hu is R&D Lead Engineer of Infinitus (China) Company Ltd that is engaged in Chinese herbal plantations,R&D, production, sales and service of TCM health products. She is also the principle members of Joint Laboratory for the Research of Chinese Herbal Polysaccharides-Chinese Academy of Science Shanghai Institute of Materia Medica and Infinitus. She has published more than 20 papers in reputed journals
Fungal polysaccharides have been shown broad spectrum of biological activities, including anti-inflammatory, ant-oxidative and improve immunity. However, oral administration of fungal polysaccharides for rendering the conventional vaccine against influenza virus has been reported rarely. Here, we investigated the potential of fungal polysaccharides enhancing the influenza vaccine efficacy in a mouse model. Mice were immunized with inactivated H1N1 (A/PR8/1934) influenza vaccine combined with oral polysaccharides lentinan, tremellan, pachymaran, and a mixture of the three. The results showed that mice in the polysaccharides/vaccine groups had reduced morbidity, improved viral clearance, and recovered faster than the mice receiving the conventional vaccine only after infection. This effect could be attributed to the increased levels of virus-specific serum antibody IgG and decreased levels of inflammatory cytokine IFN-γ in the lung tissue. Our finding suggests that taking fungal polysaccharides orally might be useful for improving the efficacy of conventional inactive influenza vaccines.