Analysis of glycosaminoglycan-derived, precolumn, 2-aminoacridone–labeled disaccharides with LC-fluorescence and LC-MS detection

Nicola Volpi; Fabio Galeotti; Bo Yang; Robert J Linhardt

doi:10.1038/nprot.2014.026

journal article Feb 06, 2014

Analysis of glycosaminoglycan-derived, precolumn, 2-aminoacridone–labeled disaccharides with LC-fluorescence and LC-MS detection

Nicola Volpi

Fabio Galeotti Bo Yang

Robert J Linhardt

Nature Protocols Vol. 9 No. 3 pp. 541-558 · Springer Science and Business Media LLC

View at Publisher Save 10.1038/nprot.2014.026

Topics

No keywords indexed for this article. Browse by subject →

References

112

[1]

Gupta, G. & Surolia, A. Glycomics: an overview of the complex glycocode. Adv. Exp. Med. Biol. 749, 1–13 (2012). 10.1007/978-1-4614-3381-1_1

[2]

Raman, R. et al. Glycomics: an integrated systems approach to structure-function relationships of glycans. Nat. Methods 2, 817–824 (2005). 10.1038/nmeth807

[3]

Shriver, Z. et al. Glycomics: a pathway to a class of new and improved therapeutics. Nat. Rev. Drug Discov. 3, 863–873 (2004). 10.1038/nrd1521

[4]

Dennis, J.W. et al. Protein glycosylation in development and disease. Bioessays 21, 412–421 (1999). 10.1002/(sici)1521-1878(199905)21:5<412::aid-bies8>3.0.co;2-5

[5]

Feizi, T. & Mulloy, B. Carbohydrates and glycoconjugates. Glycomics: the new era of carbohydrate biology. Curr. Opin. Struct. Biol. 13, 602–604 (2003). 10.1016/j.sbi.2003.09.001

[6]

Ly, M. et al. Proteoglycanomics: recent progress and future challenges. OMICS 14, 389–399 (2010). 10.1089/omi.2009.0123

[7]

Gesslbauer, B. et al. Proteoglycanomics: tools to unravel the biological function of glycosaminoglycans. Proteomics 7, 2870–2880 (2007). 10.1002/pmic.200700176

[8]

Morgan, M.R. et al. Synergistic control of cell adhesion by integrins and syndecans. Nat. Rev. Mol. Cell Biol. 8, 957–969 (2007). 10.1038/nrm2289

[9]

Capila, I. & Linhardt, R.J. Heparin–protein interactions. Angew. Chem. Int. Ed. Engl. 41, 391–412 (2002). 10.1002/1521-3773(20020201)41:3<390::aid-anie390>3.0.co;2-b

[10]

Cattaruzza, S. & Perris, R. Approaching the proteoglycome: molecular interactions of proteoglycans and their functional output. Macromol. Biosci. 6, 667–680 (2006). 10.1002/mabi.200600100

[11]

Cattaruzza, S. et al. Proteoglycans in the control of tumor growth and metastasis formation. Connect. Tissue Res. 49, 225–229 (2008). 10.1080/03008200802143448

[12]

Gesslbauer, B. et al. New targets for glycosaminoglycans and glycosaminoglycans as novel targets. Exp. Rev. Proteomics 10, 77–95 (2013). 10.1586/epr.12.75

[13]

Zhao, X. et al. Sequence analysis and domain motifs in the porcine skin decorin glycosaminoglycan chain. J. Biol. Chem. 288, 9226–9237 (2013). 10.1074/jbc.m112.437236

[14]

Li, L. et al. Proteoglycan sequence. Mol. Biosyst. 8, 1613–1625 (2012). 10.1039/c2mb25021g

[15]

Jackson, R.L. et al. Glycosaminoglycans: molecular properties, protein interactions, and role in physiological processes. Physiol. Rev. 71, 481–539 (1991). 10.1152/physrev.1991.71.2.481

[16]

Gama, C.I. & Hsieh-Wilson, L.C. Chemical approaches to deciphering the glycosaminoglycan code. Curr. Opin. Chem. Biol. 9, 609–619 (2005). 10.1016/j.cbpa.2005.10.003

[17]

Hyaluronan: its nature, distribution, functions and turnover

J. R. E. Fraser, T. C. Laurent, U. B. G. Laurent

Journal of Internal Medicine 1997 10.1046/j.1365-2796.1997.00170.x

[18]

Volpi, N. Analytical aspects of pharmaceutical grade chondroitin sulfates. J. Pharm. Sci. 96, 3168–3180 (2007). 10.1002/jps.20997

[19]

Sugahara, K. et al. Recent advances in the structural biology of chondroitin sulfate and dermatan sulfate. Curr. Opin. Struct. Biol. 13, 612–620 (2003). 10.1016/j.sbi.2003.09.011

[20]

Yamada, S. & Sugahara, K. Potential therapeutic application of chondroitin sulfate/dermatan sulfate. Curr. Drug. Discov. Technol. 5, 289–301 (2008). 10.2174/157016308786733564

[21]

Sugahara, K. & Mikami, T. Chondroitin/dermatan sulfate in the central nervous system. Curr. Opin. Struct. Biol. 17, 536–545 (2007). 10.1016/j.sbi.2007.08.015

[22]

Volpi, N. Advances in chondroitin sulfate analysis: application in physiological and pathological states of connective tissue and during pharmacological treatment of osteoarthritis. Curr. Pharm. Des. 12, 639–658 (2006). 10.2174/138161206775474350

[23]

Linhardt, R.J. et al. New methodologies in heparin structure analysis and the generation of LMW heparins. Adv. Exp. Med. Biol. 313, 37–47 (1992). 10.1007/978-1-4899-2444-5_4

[24]

Rabenstein, D.L. Heparin and heparan sulfate: structure and function. Nat. Prod. Rep. 19, 312–331 (2002). 10.1039/b100916h

[25]

Casu, B. Structure of heparin and heparin fragments. Ann. N.Y. Acad. Sci. 556, 1–17 (1989). 10.1111/j.1749-6632.1989.tb22485.x

[26]

Casu, B. Structure and biological activity of heparin. Adv. Carbohydr. Chem. Biochem. 43, 51–134 (1985). 10.1016/s0065-2318(08)60067-0

[27]

Kamhi, E. et al. Glycosaminoglycans in infectious disease. Biol. Rev. Camb. Philos. Soc. 88, 928–943 (2013). 10.1111/brv.12034

[28]

Kogan, G. et al. Hyaluronic acid: a natural biopolymer with a broad range of biomedical and industrial applications. Biotechnol. Lett. 29, 17–25 (2007). 10.1007/s10529-006-9219-z

[29]

Volpi, N. et al. Role, metabolism, chemical modifications and applications of hyaluronan. Curr. Med. Chem. 16, 1718–1745 (2009). 10.2174/092986709788186138

[30]

Gray, E. et al. The anticoagulant and antithrombotic mechanisms of heparin. Handb. Exp. Pharmacol. 207, 43–61 (2012). 10.1007/978-3-642-23056-1_3

[31]

Hassan, Y. et al. Heparin-induced thrombocytopenia and recent advances in its therapy. J. Clin. Pharm. Ther. 32, 535–544 (2007). 10.1111/j.1365-2710.2007.00865.x

[32]

Masuko, S. & Linhardt, R.J. Chemoenzymatic synthesis of the next generation of ultralow MW heparin therapeutics. Future Med. Chem. 4, 289–296 (2012). 10.4155/fmc.11.185

[33]

Wang, Z et al. Control of the heparosan N-deacetylation leads to an improved bioengineered heparin. Appl. Microbiol. Biotechnol. 91, 91–99 (2011). 10.1007/s00253-011-3231-5

[34]

Zhou, H. et al. M402, a novel heparan sulfate mimetic, targets multiple pathways implicated in tumor progression and metastasis. PLoS ONE 6, e21106 (82011). 10.1371/journal.pone.0021106

[35]

Volpi, N. (Ed.) Chondroitin Sulfate: Structure, Role, and Pharmacological Activity (Academic Press, 2006).

[36]

Karst, N.A. & Linhardt, R.J. Recent chemical and enzymatic approaches to the synthesis of glycosaminoglycan oligosaccharides. Curr. Med. Chem. 10, 1993–2031 (2003). 10.2174/0929867033456891

[37]

Leymarie, N. & Zaia, J. Effective use of mass spectrometry for glycan and glycopeptide structural analysis. Anal. Chem. 84, 3040–3048 (2012). 10.1021/ac3000573

[38]

Volpi, N. et al. Electrophoresis for the analysis of heparin purity and quality. Electrophoresis 33, 1531–1537 (2012). 10.1002/elps.201100479

[39]

Yang, B. et al. Hyphenated techniques for the analysis of heparin and heparan sulfate. Anal. Bioanal. Chem. 399, 541–557 (2011). 10.1007/s00216-010-4117-6

[40]

Sisu, E. et al. Modern developments in mass spectrometry of chondroitin and dermatan sulfate glycosaminoglycans. Amino Acids 41, 235–256 (2011). 10.1007/s00726-010-0682-4

[41]

Beni, S. et al. Analysis and characterization of heparin impurities. Anal. Bioanal. Chem. 399, 527–239 (2011). 10.1007/s00216-010-4121-x

[42]

Zaia, J. Mass spectrometry and glycomics. OMICS 14, 401–418 (2010). 10.1089/omi.2009.0146

[43]

Zaia, J. On-line separations combined with MS for analysis of glycosaminoglycans. Mass. Spectrom. Rev. 28, 254–272 (2009). 10.1002/mas.20200

[44]

Volpi, N. et al. Capillary electrophoresis of complex natural polysaccharides. Electrophoresis 29, 3095–3106 (2008). 10.1002/elps.200800109

[45]

Amon, S. et al. Glycosylation analysis of glycoproteins and proteoglycans using capillary electrophoresis-mass spectrometry strategies. Electrophoresis 29, 2485–2507 (2008). 10.1002/elps.200800105

[46]

Volpi, N. & Linhardt, R.J. High-performance liquid chromatography-mass spectrometry for mapping and sequencing glycosaminoglycan-derived oligosaccharides. Nat. Protoc. 5, 993–1004 (2010). 10.1038/nprot.2010.48

[47]

Michaud, P. et al. Polysaccharide lyases: recent developments as biotechnological tools. Crit. Rev. Biotechnol. 23, 233–266 (2003). 10.1080/07388550390447043

[48]

Ernst, S. et al. Enzymatic degradation of glycosaminoglycans. Crit. Rev. Biochem. Mol. Biol. 30, 387–444 (1995). 10.3109/10409239509083490

[49]

Linhardt, R.J. et al. Polysaccharide lyases. Appl. Biochem. Biotechnol. 12, 135–176 (1986). 10.1007/bf02798420

[50]

Xia, B. et al. Versatile fluorescent derivatization of glycans for glycomic analysis. Nat. Methods 2, 845–850 (2005). 10.1038/nmeth808

Showing 50 of 112 references

Cited By

130

Arylsulfatase I is a novel lysosomal chondroitin endosulfatase regulating endochondral ossification

Rafaela Grecco-Machado, Satomi Nadanaka · 2026

Matrix Biology

The GAGOme: a cell-based library of displayed glycosaminoglycans

Yen-Hsi Chen, Yoshiki Narimatsu · 2018

Nature Methods

Metrics

130

Citations

112

References

Details

Published: Feb 06, 2014
Vol/Issue: 9(3)
Pages: 541-558
License: View

Authors

Kunming University of Science and Technology

R

Robert J Linhardt

Cite This Article

Nicola Volpi, Fabio Galeotti, Bo Yang, et al. (2014). Analysis of glycosaminoglycan-derived, precolumn, 2-aminoacridone–labeled disaccharides with LC-fluorescence and LC-MS detection. Nature Protocols, 9(3), 541-558. https://doi.org/10.1038/nprot.2014.026

Analysis of glycosaminoglycan-derived, precolumn, 2-aminoacridone–labeled disaccharides with LC-fluorescence and LC-MS detection

You May Also Like