A capillary zone electrophoresis method for detection of Apolipoprotein C-III glycoforms and other related artifactually modified species

Journal of Chromatography A

Volumn 1532, Issue , 2018, Pages 238-245

  Ruel, Coralie ^a,b   Morani, Marco ^a   Bruneel, Arnaud ^c,d   Junot, Christophe ^b   Taverna, Myriam ^a   Fenaille, François ^b   Tran, Nguyet Thuy ^a  

^a UNIV PARIS SUD   (France)

^b UNIVERSITÉ PARIS SACLAY   (France)

^c BICHAT HOSPITAL   (France)

^d Universite Paris Sud   (France)

Author keywords

ApolipoproteinC III; Capillary zone electrophoresis; Carbamylation; Glycoprotein

Indexed keywords

AMINES; CHEMICAL ANALYSIS; CHEMICAL MODIFICATION; DIAGNOSIS; ELECTROPHORESIS; GLYCOPROTEINS; GLYCOSYLATION; MASS SPECTROMETRY; NITROGEN COMPOUNDS; SEPARATION; SILICA; UREA;

APOLIPOPROTEINC-III; CAPILLARY ZONE ELECTROPHORESIS; CARBAMYLATION; CONGENITAL DISORDERS; HIGH-RESOLUTION SEPARATIONS; MALDI-TOF MASS SPECTROMETRY; RELATIVE QUANTIFICATION; RELIABLE METHODS;

CAPILLARY ELECTROPHORESIS;

APOLIPOPROTEIN C3; DIAMINE; POLYACRYLAMIDE; POLYVINYL ALCOHOL; SIALIDASE; TRYPSIN; UREA; AMINO ACID; BUFFER; GLYCOPROTEIN;

ARTICLE; CAPILLARY ELECTROPHORESIS; CAPILLARY ZONE ELECTROPHORESIS; CONGENITAL DISORDER OF GLYCOSYLATION; CONTROLLED STUDY; HUMAN; IONIC STRENGTH; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; PH; PRIORITY JOURNAL; ULTRAVIOLET RADIATION; ARTIFACT; CHEMISTRY; GLYCOSYLATION; MATRIX-ASSISTED LASER DESORPTION-IONIZATION MASS SPECTROMETRY; METABOLISM; PROCEDURES; REPRODUCIBILITY;

AMINO ACIDS; APOLIPOPROTEIN C-III; ARTIFACTS; BUFFERS; ELECTROPHORESIS, CAPILLARY; GLYCOPROTEINS; GLYCOSYLATION; HUMANS; NEURAMINIDASE; REPRODUCIBILITY OF RESULTS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; ULTRAVIOLET RAYS;

EID: 85038610507     PISSN: 00219673     EISSN: 18733778     Source Type: Journal    
DOI: 10.1016/j.chroma.2017.12.002     Document Type: Article

References (45)

1. Varki, A., Cummings, R., Esko, J., Freeze, H., Hart, G., Marth, J., Historical Background and Overview. 1999, Cold Spring Harbor Laboratory Press (Accessed 11 July 2017) https://www.ncbi.nlm.nih.gov/books/NBK20744/.
2. Freeze, H.H., Chong, J.X., Bamshad, M.J., Ng, B.G., Solving glycosylation disorders: fundamental approaches reveal complicated pathways. Am. J. Hum. Genet. 94 (2014), 161–175, 10.1016/j.ajhg.2013.10.024.
3. Jaeken, J., Congenital disorders of glycosylation. Chapter 179 M.L, Olivier Dulac, H.B.S., (eds.) Handb. Clin. Neurol., 2013, Elsevier, 1737–1743, 10.1016/B978-0-444-59565-2.00044-7.
4. Wopereis, S., Grünewald, S., Morava, É., Penzien, J.M., Briones, P., Garcı́a-Silva, M.T., Demacker, P.N.M., Huijben, K.M.L.C., Wevers, R.A., Apolipoprotein C-III isofocusing in the diagnosis of genetic defects in O-glycan biosynthesis. Clin. Chem. 49 (2003), 1839–1845, 10.1373/clinchem.2003.022541.
5. Wopereis, S., Grünewald, S., Huijben, K.M.L.C., Morava, É., Mollicone, R., van Engelen, B.G.M., Lefeber, D.J., Wevers, R.A., Transferrin and apolipoprotein C-III isofocusing are complementary in the diagnosis of N- and O-glycan biosynthesis defects. Clin. Chem. 53 (2007), 180–187, 10.1373/clinchem.2006.073940.
6. Wu, X., Steet, R.A., Bohorov, O., Bakker, J., Newell, J., Krieger, M., Spaapen, L., Kornfeld, S., Freeze, H.H., Mutation of the COG complex subunit gene COG7 causes a lethal congenital disorder. Nat. Med. 10 (2004), 518–523, 10.1038/nm1041.
7. Foulquier, F., COG defects, birth and rise!. Biochim. Biophys. Acta BBA – Mol. Basis Dis. 1792 (2009), 896–902, 10.1016/j.bbadis.2008.10.020.
8. Spaapen, L.J.M., Bakker, J.A., van der Meer, S.B., Sijstermans, H.J., Steet, R.A., Wevers, R.A., Jaeken, J., Clinical and biochemical presentation of siblings with COG-7 deficiency, a lethal multiple O- and N-glycosylation disorder. J. Inherit. Metab. Dis., 28, 2005, 707, 10.1007/s10545-005-0015-z.
9. Jong, M.C., Hofker, M.H., Havekes, L.M., Role of ApoCs in lipoprotein metabolism. Arterioscler. Thromb. Vasc. Biol. 19 (1999), 472–484, 10.1161/01.ATV.19.3.472.
10. Petibois, C., Cazorla, G., Cassaigne, A., Déléris, G., Plasma protein contents determined by fourier-transform infrared spectrometry. Clin. Chem. 47 (2001), 730–738.
11. Sakurabayashi, I., Saito, Y., Kita, T., Matsuzawa, Y., Goto, Y., Reference intervals for serum apolipoproteins A-I, A-II, B, C-II, C-III, and E in healthy Japanese determined with a commercial immunoturbidimetric assay and effects of sex, age, smoking, drinking, and Lp(a) level. Clin. Chim. Acta 312 (2001), 87–95, 10.1016/S0009-8981(01)00591-5.
12. Albers, J.J., Scanu, A.M., Isoelectric fractionation and characterization of polypeptides from human serum very low density lipoproteins. Biochim. Biophys. Acta BBA – Protein Struct. 236 (1971), 29–37, 10.1016/0005-2795(71)90145-0.
13. Shulman, R.S., Herbert, P.N., Fredrickson, D.S., Wehrly, K., Brewer, H.B., Isolation and alignment of the tryptic peptides of alanine apolipoprotein, an apolipoprotein from human plasma very low density lipoproteins. J. Biol. Chem. 249 (1974), 4969–4974.
14. Hospattankar, A.V., Bryan Brewer, H., Ronan, R., Fairwell, T., Amino acid sequence of human plasma apolipoprotein C-III from normalipidemic subjects. FEBS Lett. 197 (1986), 67–73, 10.1016/0014-5793(86)80300-3.
15. Balog, C.I.A., Mayboroda, O.A., Wuhrer, M., Hokke, C.H., Deelder, A.M., Hensbergen, P.J., Mass spectrometric identification of aberrantly glycosylated human apolipoprotein C-III peptides in urine from schistosoma mansoni-Infected individuals. Mol. Cell. Proteom. MCP 9 (2010), 667–681, 10.1074/mcp.M900537-MCP200.
16. Nicolardi, S., van der Burgt, Y.E.M., Wuhrer, M., Deelder, A.M., Mapping O-glycosylation of apolipoprotein C-III in MALDI-FT-ICR protein profiles. Proteomics 13 (2013), 992–1001, 10.1002/pmic.201200293.
17. Ondrušková, N., Honzík, T., Kytnarová, J., Matoulek, M., Zeman, J., Hansíková, H., Isoelectric focusing of serum apolipoprotein C-III as a sensitive screening method for the detection of O-glycosylation disturbances. Prague Med. Rep. 116 (2015), 73–86, 10.14712/23362936.2015.48.
18. Haase, R., Menke-Möllers, I., Oette, K., Analysis of human apolipoproteins C by isoelectric focusing in immobilized pH gradients. Electrophoresis 9 (1988), 569–575, 10.1002/elps.1150090917.
19. Bruneel, A., Morelle, W., Carre, Y., Habarou, F., Dupont, D., Hesbert, A., Durand, G., Michalski, J.C., Drouin-Garraud, V., Seta, N., Two dimensional gel electrophoresis of apolipoprotein C-III and MALDI-TOF MS are complementary techniques for the study of combined defects in N- and mucin type O-glycan biosynthesis. Proteom. – Clin. Appl. 2 (2008), 1670–1674, 10.1002/prca.200800089.
20. Sprecher, D.L., Taam, L., Brewer, H.B., Two-dimensional electrophoresis of human plasma apolipoproteins. Clin. Chem. 30 (1984), 2084–2092.
21. Yen-Nicolaÿ, S., Boursier, C., Rio, M., Lefeber, D.J., Pilon, A., Seta, N., Bruneel, A., MALDI-TOF MS applied to apoC-III glycoforms of patients with congenital disorders affecting O-glycosylation. Comparison with two-dimensional electrophoresis. Proteom. – Clin. Appl. 9 (2015), 787–793, 10.1002/prca.201400187.
22. Choukaife, A., Visvikis, S., Steinmetz, J., Galteau, M.M., Kabbaj, O., Férard, G., Métais, P., Siest, G., Two-dimensional electrophoresis of plasma proteins and high density lipoproteins during inflammation. Electrophoresis 10 (1989), 781–784, 10.1002/elps.1150101110.
23. Bruneel, A., Robert, T., Lefeber, D.J., Benard, G., Loncle, E., Djedour, A., Durand, G., Seta, N., Two-dimensional gel electrophoresis of apolipoprotein C-III and other serum glycoproteins for the combined screening of human congenital disorders of O- and N-glycosylation. Proteom. – Clin. Appl. 1 (2007), 321–324, 10.1002/prca.200600777.
24. Wada, Y., Mass spectrometry of transferrin and apolipoprotein C-III for diagnosis and screening of congenital disorder of glycosylation. Glycoconj. J. 33 (2016), 297–307, 10.1007/s10719-015-9636-0.
25. Harvey, S.B., Zhang, Y., Wilson-Grady, J., Monkkonen, T., Nelsestuen, G.L., Kasthuri, R.S., Verneris, M.R., Lund, T.C., Ely, E.W., Bernard, G.R., Zeisler, H., Homoncik, M., Jilma, B., Swan, T., Kellogg, T.A., O-Glycoside biomarker of apolipoprotein C3: responsiveness to obesity, bariatric surgery, and therapy with metformin, to chronic or severe liver disease and to mortality in severe Sepsis and Graft vs Host disease. J. Proteome Res. 8 (2009), 603–612, 10.1021/pr800751x.
26. Trenchevska, O., Schaab, M.R., Nelson, R.W., Nedelkov, D., Development of multiplex mass spectrometric immunoassay for detection and quantification of apolipoproteins C-I, C-II, C-III and their proteoforms. Methods San Diego Calif. 81 (2015), 86–92, 10.1016/j.ymeth.2015.02.020.
27. Wada, Y., Kadoya, M., Okamoto, N., Mass spectrometry of apolipoprotein C-III, a simple analytical method for mucin-type O-glycosylation and its application to an autosomal recessive cutis laxa type-2 (ARCL2) patient. Glycobiology 22 (2012), 1140–1144, 10.1093/glycob/cws086.
28. Jian, W., Edom, R.W., Wang, D., Weng, N., Zhang, S. (Weihua), Relative quantitation of glycoisoforms of intact apolipoprotein C3 in human plasma by liquid chromatography–high-resolution mass spectrometry. Anal. Chem. 85 (2013), 2867–2874, 10.1021/ac3034757.
29. Hoffstetter-Kuhn, S., Paulus, A., Gassmann, E., Widmer, H.M., Influence of borate complexation on the electrophoretic behavior of carbohydrates in capillary electrophoresis. Anal. Chem. 63 (1991), 1541–1547, 10.1021/ac00015a009.
30. Watson, E., Yao, F., Capillary electrophoretic separation of human recombinant erythropoietin (r-HuEPO) Glycoforms. Anal. Biochem. 210 (1993), 389–393, 10.1006/abio.1993.1212.
31. Alahmad, Y., Taverna, M., Mobdi, H., Duboeuf, J., Grégoire, A., Rancé, I., Tran, N.T., A validated capillary electrophoresis method to check for batch-to-batch consistency during recombinant human glycosylated interleukin-7 production campaigns. J. Pharm. Biomed. Anal. 51 (2010), 882–888, 10.1016/j.jpba.2009.09.013.
32. Cohen, N., Grushka, E., Controlling electroosmotic flow in capillary zone electrophoresis. J. Chromatogr. A 678 (1994), 167–175, 10.1016/0021-9673(94)87086-1.
33. European Pharmacopeia 9.0 European Directorate for the Quality of Medicines, vol. 1316, Council of Europe, Erythropoietin concentrated solution, Council of Europe, Strasbourg, in: 2008: pp. 2391–2395.
34. Stark, G.R., Stein, W.H., Moore, S., Reactions of the cyanate present in aqueous urea with amino acids and proteins. J. Biol. Chem. 235 (1960), 3177–3181.
35. Kollipara, L., Zahedi, R.P., Protein carbamylation: in vivo modification or in vitro artefact?. Proteomics 13 (2013), 941–944, 10.1002/pmic.201200452.
36. Herbert, P.N., Shulman, R.S., Levy, R.I., Fredrickson, D.S., Fractionation of the C-Apoproteins from human plasma very low density lipoproteins artifactual polymorphism from carbamylation in urea-containing solutions. J. Biol. Chem. 248 (1973), 4941–4946.
37. Lundqvist, M., Berggård, T., Hellstrand, E., Lynch, I., Dawson, K.A., Linse, S., Cedervall, T., Rapid and facile purification of apolipoprotein A-I from human plasma using thermoresponsive Nanoparticles. J. Biomater. Nanobiotechnol., 02, 2011, 258, 10.4236/jbnb.2011.23033.
38. Nicolardi, S., van der Burgt, Y.E.M., Dragan, I., Hensbergen, P.J., Deelder, A.M., Identification of new apolipoprotein-CIII Glycoforms with ultrahigh Resolution MALDI-FTICR mass spectrometry of human sera. J. Proteome Res. 12 (2013), 2260–2268, 10.1021/pr400136p.
39. Martinez-Val, A., Garcia, F., Ximénez-Embún, P., Martínez Teresa-Calleja, A., Ibarz, N., Ruppen, I., Munoz, J., Urea artifacts interfere with immuno-purification of lysine acetylation. J. Proteome Res. 16 (2017), 1061–1068, 10.1021/acs.jproteome.6b00463.
40. Park, Z.-Y., Sadygov, R., Clark, J.M., Clark, J.I., Yates, J.R., Assigning in vivo carbamylation and acetylation in human lens proteins using tandem mass spectrometry and database searching. Int. J. Mass Spectrom. 259 (2007), 161–173, 10.1016/j.ijms.2006.08.013.
41. McCarthy, J., Hopwood, F., Oxley, D., Laver, M., Castagna, A., Righetti, P.G., Williams, K., Herbert, B., Carbamylation of proteins in 2-D electrophoresis–myth or reality?. J. Proteome Res. 2 (2003), 239–242.
42. Palmigiano, A., Bua, R.O., Barone, R., Rymen, D., Régal, L., Deconinck, N., Dionisi-Vici, C., Fung, C.-W., Garozzo, D., Jaeken, J., Sturiale, L., MALDI-MS profiling of serum O-glycosylation and N-glycosylation in COG5-CDG. J. Mass Spectrom. 52 (2017), 372–377, 10.1002/jms.3936.
43. Bondarenko, P.V., Cockrill, S.L., Watkins, L.K., Cruzado, I.D., Macfarlane, R.D., Mass spectral study of polymorphism of the apolipoproteins of very low density lipoprotein. J. Lipid Res. 40 (1999), 543–555.
44. Liu, Z., Pawliszyn, J., Capillary isoelectric focusing with laser-induced fluorescence whole column imaging detection as a tool to monitor reactions of proteins. J. Proteome Res. 3 (2004), 567–571, 10.1021/pr034114w.
45. Delanghe, S., Moerman, A., Pletinck, A., Schepers, E., Glorieux, G., Van Biesen, W., Delanghe, J.R., Speeckaert, M.M., Quantification of carbamylated albumin in serum based on capillary electrophoresis. Electrophoresis 38 (2017), 2135–2140.