دورية أكاديمية
N-glycosylation state of TRPM8 protein revealed by terahertz spectroscopy and molecular modelling.
| العنوان: | N-glycosylation state of TRPM8 protein revealed by terahertz spectroscopy and molecular modelling. |
|---|---|
| المؤلفون: | Mernea M; Department DAFAB, Faculty of Biology, University of Bucharest, Splaiul Independenței 91-95, Bucharest, Romania., Ulăreanu R; Department DAFAB, Faculty of Biology, University of Bucharest, Splaiul Independenței 91-95, Bucharest, Romania., Călboreanu O; Department DAFAB, Faculty of Biology, University of Bucharest, Splaiul Independenței 91-95, Bucharest, Romania., Chirițoiu G; Department of Molecular Cell Biology, Institute of Biochemistry, Romanian Academy, Splaiul Independenței 296, 060031 Bucharest, Romania., Cucu D; Department DAFAB, Faculty of Biology, University of Bucharest, Splaiul Independenței 91-95, Bucharest, Romania. Electronic address: dana.cucu@bio.unibuc.ro., Mihăilescu DF; Department DAFAB, Faculty of Biology, University of Bucharest, Splaiul Independenței 91-95, Bucharest, Romania. Electronic address: d.f.mihailescu@gmail.com. |
| المصدر: | Biochimica et biophysica acta. General subjects [Biochim Biophys Acta Gen Subj] 2020 Jul; Vol. 1864 (7), pp. 129580. Date of Electronic Publication: 2020 Feb 25. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Country of Publication: Netherlands NLM ID: 101731726 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1872-8006 (Electronic) Linking ISSN: 03044165 NLM ISO Abbreviation: Biochim Biophys Acta Gen Subj Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Amsterdam : Elsevier |
| مواضيع طبية MeSH: | Models, Molecular*, Glucans/*chemistry , Membrane Lipids/*chemistry , TRPM Cation Channels/*chemistry, Cell Line ; Cell Movement/genetics ; Cell Proliferation/genetics ; Glycosylation ; Humans ; Sugars/chemistry ; TRPM Cation Channels/ultrastructure ; Terahertz Spectroscopy |
| مستخلص: | TRPM8 member of the TRP superfamily of membrane proteins participates to various cellular processes ranging from Ca 2+ uptake and cold sensation to cellular proliferation and migration. TRPM8 is a large tetrameric protein with more than 70% of its residues located in the cytoplasm. TRPM8 is N-glycosylated, with a single site per subunit. This work focuses on the N-glycosylation of TRPM8 channel that was previously studied by our group in relation to proliferation and migration of tumoral cells. Here, experimental data performed with deglycosylating agents assess that the sole glycosylation site contains complex glycans with a molecular weight of 2.5 kDa. The glycosylation state of TRPM8 in cells untreated and treated with a deglycosylating agent was addressed with Terahertz (THz) spectroscopy. Results show a clear difference between cells comprising glycosylated and deglycosylated TRPM8, the first presenting an increased THz absorption. Human TRPM8 was modelled using as templates the available TRPM8 and other TRPM channels structures. Glycosylations were modelled by considering two glycan structures with molecular weight close to the experiment: shorter and branched at the first sugar unit (glc1) and longer and unbranched (glc2). Simulation of THz spectra based on the molecular dynamics of unglycosylated and the two glycosylated TRPM8 models in lipid membrane and solvation box showed that glycan structure strongly influences the THz spectrum of the channel and of other components from the simulation system. Only spectra of TRPM8 with glc1 glycans were in agreement with the experiment, leading to the validation of glc1 glycan structure. Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. (Copyright © 2020. Published by Elsevier B.V.) |
| فهرسة مساهمة: | Keywords: THz spectroscopy; TRPM8 N-glycosylation; TRPM8 structural model; TRPM8 structure |
| المشرفين على المادة: | 0 (Glucans) 0 (Membrane Lipids) 0 (Sugars) 0 (TRPM Cation Channels) 0 (TRPM8 protein, human) |
| تواريخ الأحداث: | Date Created: 20200229 Date Completed: 20201021 Latest Revision: 20201021 |
| رمز التحديث: | 20221213 |
| DOI: | 10.1016/j.bbagen.2020.129580 |
| PMID: | 32109505 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1872-8006 |
|---|---|
| DOI: | 10.1016/j.bbagen.2020.129580 |