Researcher: Demir, Ramiz
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Demir, Ramiz
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Publication Metadata only In silico analysis of glycosylation pattern in 5 th -6 th repeat sequence of reelin glycoprotein(Taylor & Francis Inc, 2021) Deveci, Remziye; N/A; Demir, Ramiz; PhD Student; Koç University Research Center for Translational Medicine (KUTTAM) / Koç Üniversitesi Translasyonel Tıp Araştırma Merkezi (KUTTAM); Graduate School of Health Sciences; N/AReelin is an extracellular matrix glycoprotein that plays a key role in cortical development, maturation, synaptic plasticity, and memory formation in the adult mammalian brain. Glycosylation is a significant post- and co-translational modification of proteins. Although glycosylation contributes to the characteristic of proteins from their production to molecular interactions, the knowledge about the glycosylation pattern of reelin is very limited. In this study, we aimed to predict the potential glycosylation pattern of the 5(th)-6(th) repeat of central reelin fragment that responsible for their signaling, by using in silico methods. We found that the predicted glycosylation pattern of the 5(th)-6(th) repeat of human reelin was highly conserved between vertebrate species. However, this conservation was not observed in analyzed invertebrates. For the first time, we described the sites of glycosylation at a three-dimensional protein structure in human reelin. Because the sites were very closed to EGF-like repeats and receptor binding sites, they could contribute the interaction with a partner of reelin in addition to the effect of thermostability to protein. Many of the residues related glycosylation were also conserved in analyzed species. These findings may guide biochemical, genetic, and glycobiology base on further experiments about reelin glycosylation. The understanding of reelin glycosylation might change the point of view of treatment for many pathological conditions in neurodegenerative diseases such as Alzheimer's disease. Communicated by Ramaswamy H. SarmaPublication Metadata only Exploring the candidate terminal glycan profile in neural regeneration of the sea urchin paracentrotus lividus, using lectin blotting and mass spectrometry(Univ Chicago Press) Sahar, Umut; Deveci, Remziye; N/A; Demir, Ramiz; PHD. Student; Graduate School of Health Sciences; N/AGlycans are expressed as conjugates of glycoproteins, glycolipids, and proteoglycans. The huge diversity of glycans on glycoconjugates contributes to many biological processes, from glycan-based molecular recognition to developmental events, such as regeneration in the nervous system. Echinoderms, which have a close phylogenetic relationship with chordates, are an important group of marine invertebrates for body regeneration. Although many major roles of glycans on glycoconjugates are known, their role in the glycosylation profile of the nervous system in sea urchins is poorly understood. In this study, we aimed to determine the terminal glycan profile by lectin blotting and to quantify sialic acids by the capillary liquid chromatography electrospray ionization tandem mass spectrometry system in the nervous tissue of the sea urchin Paracentrotus lividus. We determined the N-acetyl-D-glucosamine, mannose, and sialic acids (mainly alpha 2,3 linked) by lectin blotting and five types of sialic acids (N-glycolylneuraminic acid, N-acetylneuraminic acid, 9-O-acetyl-N-alycolylneuraminic acid, 5-N-acetyl-9-O-acetyl-N-acetylneuraminic acid, and di-O-acetylated-N-alycolylneuraminic acid) by capillary liquid chromatography electrospray ionization tandem mass spectrometry. This potential first description of the terminal glycan profile in the nervous system of the sea urchin is expected to help us understand its role in nervous system development and regeneration.Publication Metadata only Determination of terminal glycan and total monosaccharide profiles of reelin glycoprotein in SH-SY5Y neuroblastoma cell line by lectin blotting and capillary liquid chromatography electrospray ionization-ion trap tandem mass spectrometry system(Elsevier, 2021) Sahar, Umut; Deveci, Remziye; N/A; Demir, Ramiz; PhD Student; Graduate School of Health Sciences; N/AReelin (400 kDa) is an extracellular matrix glycoprotein that is a key regulator of the many significant biological processes including the brain formation, cell aggregation, and dendrite formation. The glycosylation contributes to the nature of the protein through folding, localization and trafficking, solubility, antigenicity, biological activity, and half-life. Although reelin is to be known as a glycoprotein, the knowledge of its glycosylation is very limited. In this study, we aimed to characterize the terminal glycan profile of reelin by lectin blotting and monosaccharide analysis of glycan chains by capillary liquid chromatography electrospray ionization ion trap tandem mass spectrometry (CapLC-ESI-MS/MS) in SH-SY5Y neuroblastoma cell line. According to our results, reelin was detected in different protein fragments (310, 250, and 85 kDa) in addition to full-length form (400 kDa) in the cell line. The reelin glycoprotein was found to carry the p-N-Acetylglucosamine, a-Mannose, 13-Galactose, and a-2,3 and a2,6 linked sialic acids by lectin blotting. Nevertheless, these terminal monosaccharides were found in different intensity according to reelin fragments. Besides, we purified a reelin fragment (250 kDa), and we analyzed it for their monosaccharide by CapLC-ESI-MS/MS. We found that reelin contained five types of monosaccharides, which were consisted of N-Acetylgalactosamine, N-Acetylglucosamine, Galactose, Glucose, Mannose and Sialic acid, from high to low abundance respectively. The present results provide a valuable guide for biochemical, genetic, and glycobiology based further experiments about reelin glycosylation in cancer perspective.