Yıl: 2022 Cilt: 46 Sayı: 5 Sayfa Aralığı: 1524 - 1530 Metin Dili: İngilizce DOI: 10.55730/1300-0527.3457 İndeks Tarihi: 07-12-2022

Comparison of denaturing agent effects in enzymatic N-glycan release for human plasma N-glycan analysis

Öz:
Glycosylation is an essential posttranslational modification observed in the living proteome. Glycosylation profiles in glycoproteins can change in commonly observed diseases such as cancer. Identifying these changes is crucial in discovering new biomarkers for the early diagnosis of cancer. One of the main steps of N-glycan analysis is to release N-glycans from glycoproteins by specific enzymes. The study compares common denaturing agent combinations used in N-glycan release methods. In the study, human plasma was used to test the release methods of N-glycans containing different detergent combinations. The released N-glycans were labeled with the procainamide tag, purified using cellulose-containing solid-phase extraction cartridges, and analyzed by high-performance liquid chromatography-hydrophilic interaction liquid chromatography equipped with fluorescence detection (HPLC-HILIC-FLD). The results showed that the sodium dodecyl sulfate and sodium deoxycholate (SDS + SDC) detergent combination provided the highest average FLD signal areas and intensities in the N-glycan analysis. The protocol with SDS resulted in more reproducible average FLD signal areas and intensities. It was also found that the average signal FLD signal areas and intensities of the detected N-glycans were reduced when SDS and SDC were used with 1,4-dithiothreitol (DTT) reducing agents. In addition, deglycosylation of glycoproteins with various denaturing agents resulted in relatively minor variation in human plasma N-glycosylation profiles.
Anahtar Kelime: Glycomics glycan release denaturing agents procainamide labeling human plasma detergents

Belge Türü: Makale Makale Türü: Araştırma Makalesi Erişim Türü: Erişime Açık
  • 1. Čaval T, Heck AJR, Reiding KR. Meta-heterogeneity: Evaluating and describing the diversity in glycosylation between sites on the same glycoprotein. Molecular & Cellular Proteomics 2021; 20. doi: 10.1074/mcp.R120.002093
  • 2. Rodrigues JG, Duarte HO, Reis CA, Gomes J. Aberrant protein glycosylation in cancer: implications in targeted therapy. Biochemical Society Transactions 2021; 49 (2): 843-854. doi: 10.1042/bst20200763
  • 3. Kałuża A, Szczykutowicz J, Ferens-Sieczkowska M. Glycosylation: rising potential for prostate cancer evaluation. Cancers 2021; 13 (15): 3726.
  • 4. Drake PM, Cho W, Li B, Prakobphol A, Johansen E, Anderson NL et al. Sweetening the pot: adding glycosylation to the biomarker discovery equation. Clinical chemistry 2010; 56 (2): 223-236. doi: 10.1373/clinchem.2009.136333
  • 5. Lan Y, Hao C, Zeng X, He Y, Zeng P, Guo Z et al. Serum glycoprotein-derived N- and O-linked glycans as cancer biomarkers. American Journal of Cancer Research 2016; 6 (11): 2390-2415.
  • 6. Miyamoto S. Clinical applications of glycomic approaches for the detection of cancer and other diseases. Current Opinion in Molecular Therapeutics 2006; 8 (6): 507-513.
  • 7. Peng W, Zhao J, Dong X, Banazadeh A, Huang Y, Hussien A et al. Clinical application of quantitative glycomics. Expert Review of Proteomics 2018; 15 (12): 1007-1031. doi: 10.1080/14789450.2018.1543594
  • 8. Wang MM, Zhu JH, Lubman DM, Gao CF. Aberrant glycosylation and cancer biomarker discovery: a promising and thorny journey. Clinical Chemistry and Laboratory Medicine 2019; 57 (4): 407-416. doi: 10.1515/cclm-2018-0379
  • 9. Koçak ÖF, Kayili HM, Albayrak M, Yaman ME, Kadıoğlu Y, Salih B. N-glycan profiling of papillary thyroid carcinoma tissues by MALDI- TOF-MS. Analytical Biochemistry 2019; 584: 113389. doi: 10.1016/j.ab.2019.113389
  • 10. Yaman ME, Kayili HM, Albayrak M, Kadioglu Y, Salih B. Differential N-glycosylation profiling of formalin-fixed paraffin-embedded (FFPE) invasive ductal carcinoma tissues using MALDI-TOF-MS. Molecular Omics 2021; 17 (3): 394-404. doi: 10.1039/D0MO00150C
  • 11. Patabandige MW, Pfeifer LD, Nguyen HT, Desaire H. Quantitative clinical glycomics strategies: A guide for selecting the best analysis approach. Mass Spectrometry Reviews 2021; Feb 10:10.1002/mas.21688 doi: 10.1002/mas.21688
  • 12. Vilaj M, Lauc G, Trbojević-Akmačić I. Evaluation of different PNGase F enzymes in immunoglobulin G and total plasma N-glycans analysis. Glycobiology 2020; 31 (1): 2-7. doi: 10.1093/glycob/cwaa047
  • 13. Huang Y, Orlando R. Kinetics of N-Glycan Release from Human Immunoglobulin G (IgG) by PNGase F: All Glycans Are Not Created Equal. Journal of biomolecular techniques : JBT 2017; 28 (4): 150-157. doi: 10.7171/jbt.17-2804-002
  • 14. Kotsias M, Blanas A, van Vliet SJ, Pirro M, Spencer DIR, Kozak RP. Method comparison for N-glycan profiling: Towards the standardization of glycoanalytical technologies for cell line analysis. Plos One 2019; 14 (10): e0223270. doi: 10.1371/journal.pone.0223270
  • 15. Lageveen-Kammeijer GSM, Kuster B, Reusch D, Wuhrer M. High sensitivity glycomics in biomedicine. Mass Spectrometry Reviews 2021; Sep 7: e21730. doi: 10.1002/mas.21730
  • 16. Tanca A, Biosa G, Pagnozzi D, Addis MF, Uzzau S. Comparison of detergent-based sample preparation workflows for LTQ-Orbitrap analysis of the Escherichia coli proteome. Proteomics 2013; 13 (17): 2597-2607. doi: 10.1002/pmic.201200478
  • 17. Yu Y-Q, Gilar M, Lee PJ, Bouvier ESP, Gebler JC. Enzyme-friendly, mass spectrometry-compatible surfactant for in-solution enzymatic digestion of proteins. Analytical Chemistry 2003; 75 (21): 6023-6028. doi: 10.1021/ac0346196
  • 18. Kayili HM, Salih B. N-glycan profiling of glycoproteins by hydrophilic interaction liquid chromatography with fluorescence and mass spectrometric detection. Jove-Journal of Visualized Experiments 2021 (175). doi: 10.3791/62751
  • 19. Kayili HM. Identification of bisecting N-glycans in tandem mass spectra using a procainamide labeling approach for in-depth N-glycan profiling of biological samples. International Journal of Mass Spectrometry 2020; 457. doi: 10.1016/j.ijms.2020.116412
  • 20. Zhu R, Zhou S, Peng W, Huang Y, Mirzaei P, Donohoo K et al. Enhanced Quantitative LC-MS/MS Analysis of N-linked Glycans Derived from Glycoproteins Using Sodium Deoxycholate Detergent. Journal of Proteome Research 2018; 17 (8): 2668-2678. doi: 10.1021/acs. jproteome.8b00127
  • 21. Kinoshita M, Yamada K. Recent advances and trends in sample preparation and chemical modification for glycan analysis. Journal of Pharmaceutical and Biomedical Analysis 2022; 207: 114424. doi: 10.1016/j.jpba.2021.114424
  • 22. Chen C-C, Su W-C, Huang B-Y, Chen Y-J, Tai H-C, Obena RP. Interaction modes and approaches to glycopeptide and glycoprotein enrichment. Analyst 2014; 139 (4): 688-704. doi: 10.1039/C3AN01813J
  • 23. Donohoo KB, Wang J, Goli M, Yu A, Peng W, Hakim MA et al. Advances in mass spectrometry-based glycomics-An update covering the period 2017–2021. Electrophoresis 2022; 43 (1-2): 119-142. doi: 10.1002/elps.202100199
  • 24. Selman MHJ, Hemayatkar M, Deelder AM, Wuhrer M. Cotton HILIC SPE Microtips for Microscale Purification and Enrichment of Glycans and Glycopeptides. Analytical Chemistry 2011; 83 (7): 2492-2499. doi: 10.1021/ac1027116
APA KAYILI H, sakhta R, Salih B (2022). Comparison of denaturing agent effects in enzymatic N-glycan release for human plasma N-glycan analysis. , 1524 - 1530. 10.55730/1300-0527.3457
Chicago KAYILI HACI MEHMET,sakhta Rokia,Salih Bekir Comparison of denaturing agent effects in enzymatic N-glycan release for human plasma N-glycan analysis. (2022): 1524 - 1530. 10.55730/1300-0527.3457
MLA KAYILI HACI MEHMET,sakhta Rokia,Salih Bekir Comparison of denaturing agent effects in enzymatic N-glycan release for human plasma N-glycan analysis. , 2022, ss.1524 - 1530. 10.55730/1300-0527.3457
AMA KAYILI H,sakhta R,Salih B Comparison of denaturing agent effects in enzymatic N-glycan release for human plasma N-glycan analysis. . 2022; 1524 - 1530. 10.55730/1300-0527.3457
Vancouver KAYILI H,sakhta R,Salih B Comparison of denaturing agent effects in enzymatic N-glycan release for human plasma N-glycan analysis. . 2022; 1524 - 1530. 10.55730/1300-0527.3457
IEEE KAYILI H,sakhta R,Salih B "Comparison of denaturing agent effects in enzymatic N-glycan release for human plasma N-glycan analysis." , ss.1524 - 1530, 2022. 10.55730/1300-0527.3457
ISNAD KAYILI, HACI MEHMET vd. "Comparison of denaturing agent effects in enzymatic N-glycan release for human plasma N-glycan analysis". (2022), 1524-1530. https://doi.org/10.55730/1300-0527.3457
APA KAYILI H, sakhta R, Salih B (2022). Comparison of denaturing agent effects in enzymatic N-glycan release for human plasma N-glycan analysis. Turkish Journal of Chemistry, 46(5), 1524 - 1530. 10.55730/1300-0527.3457
Chicago KAYILI HACI MEHMET,sakhta Rokia,Salih Bekir Comparison of denaturing agent effects in enzymatic N-glycan release for human plasma N-glycan analysis. Turkish Journal of Chemistry 46, no.5 (2022): 1524 - 1530. 10.55730/1300-0527.3457
MLA KAYILI HACI MEHMET,sakhta Rokia,Salih Bekir Comparison of denaturing agent effects in enzymatic N-glycan release for human plasma N-glycan analysis. Turkish Journal of Chemistry, vol.46, no.5, 2022, ss.1524 - 1530. 10.55730/1300-0527.3457
AMA KAYILI H,sakhta R,Salih B Comparison of denaturing agent effects in enzymatic N-glycan release for human plasma N-glycan analysis. Turkish Journal of Chemistry. 2022; 46(5): 1524 - 1530. 10.55730/1300-0527.3457
Vancouver KAYILI H,sakhta R,Salih B Comparison of denaturing agent effects in enzymatic N-glycan release for human plasma N-glycan analysis. Turkish Journal of Chemistry. 2022; 46(5): 1524 - 1530. 10.55730/1300-0527.3457
IEEE KAYILI H,sakhta R,Salih B "Comparison of denaturing agent effects in enzymatic N-glycan release for human plasma N-glycan analysis." Turkish Journal of Chemistry, 46, ss.1524 - 1530, 2022. 10.55730/1300-0527.3457
ISNAD KAYILI, HACI MEHMET vd. "Comparison of denaturing agent effects in enzymatic N-glycan release for human plasma N-glycan analysis". Turkish Journal of Chemistry 46/5 (2022), 1524-1530. https://doi.org/10.55730/1300-0527.3457