Modern proteomic methodologies for the characterization of lactosylation protein targets in milk

Proteomics

Volumn 10, Issue 19, 2010, Pages 3414-3434

  Arena, Simona ^a   Renzone, Giovanni ^a   Novi, Gianfranco ^a   Paffetti, Alessandro ^b   Bernardini, Giulia ^b   Santucci, Annalisa ^b   Scaloni, Andrea ^a  

^a CNR   (Italy)

^b UNIVERSITY OF SIENA   (Italy)

Author keywords

Animal proteomics; Combinatorial peptide ligand libraries; Electron transfer dissociation; Lactosylation; Milk proteins; Phenyl boronic acid

Indexed keywords

ALPHA LACTALBUMIN; BETA LACTOGLOBULIN; BORONIC ACID DERIVATIVE; LACTOSE; MARKER; MILK PROTEIN; PEPTIDE; PROTEIN;

AFFINITY CHROMATOGRAPHY; ARTICLE; CELL PROLIFERATION; COLLISIONALLY ACTIVATED DISSOCIATION; ELECTRON TRANSPORT; FOOD QUALITY; GLYCATION; HEAT TREATMENT; METHODOLOGY; MILK; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN MODIFICATION; PROTEIN TARGETING; PROTEOMICS;

AMINO ACID SEQUENCE; ANIMALS; BLOTTING, WESTERN; BORONIC ACIDS; INFANT FORMULA; LACTOSE; MILK; MILK PROTEINS; MOLECULAR SEQUENCE DATA; PEPTIDE LIBRARY; PEPTIDES; PROTEOMICS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

ANIMALIA;

EID: 77957192354     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201000321     Document Type: Article

References (67)

1. Casado, B., Affolter, M., Kussmann, M., OMICS-rooted studies of milk proteins, oligosaccharides and lipids. J. Proteomics 2009, 73, 196-208.
2. Wheeler, T. T., Hodgkinson, A. J., Prosser, C. G., Davis, S. R., Immune components of colostrum and milk - a historical perspective. J. Mammary Gland Biol. Neoplasia 2007, 12, 237-247.
3. Lönnerdal, B., Nutritional and physiologic significance of human milk proteins. Am. J. Clin. Nutr. 2003, 77, 1537S-1543S.
4. D'Alessandro, A., Scaloni, A., Zolla, L., Human milk proteins: an interactomics and updated functional overview. J. Proteome Res. 2010, in press.
5. Gauthier, S. F., Pouliot, Y., Maubois, J. L., Growth factors from bovine milk and colostrum: composition, extraction and biological activities. Lait 2006, 86, 99-125.
6. Jouan, P. N., Pouliot, Y., Gauthier, S. F., Laforest, J. P., Hormones in bovine milk and milk products: A survey. Int. Dairy J. 2006, 16, 1408-1414.
7. Castell, J. V., Friedrich, G., Kuhn, C. S., Poppe, G. E., Intestinal absorption of undegraded proteins in men: presence of bromelain in plasma after oral intake. Am. J. Physiol. 1997, 273, G139-G146.
8. Sorva, R., Mâkinen-Kiljunen, S., Juntunen-Backman, K., Beta-lactoglobulin secretion in human milk varies widely after cow's milk ingestion in mothers of infants with cow's milk allergy. J. Allergy Clin. Immunol. 1994, 93, 787-792.
9. Moreno, F. J., Rubio, L. A., Olano, A., Clemente, A., Uptake of 2S albumin allergens, Ber e 1 and Ses i 1, across human intestinal epithelial Caco-2 cell monolayers. J. Agric. Food Chem. 2006, 54, 8631-8639.
10. van Boekel, M. A. J. S., Effect of heating on Maillard reactions in milk. Food Chem. 1998, 62, 403-414.
11. Siciliano, R., Rega, B., Amoresano, A., Pucci, P., Modern mass spectrometric methodologies in monitoring milk quality. Anal. Chem. 2000, 72, 408-415.
12. Jones, A. D., Tier, C. M., Wilkins, J. P. G., Analysis of the Maillard reaction products of beta-lactoglobulin and lactose in skimmed milk powder by capillary electrophoresis and electrospray mass spectrometry. J. Chromatogr. A 1998, 822, 147-154.
13. Morgan, F., Leonil, J., Mollé, D., Bouhallab, S., Nonenzymic lactosylation of bovine beta-lactoglobulin under mild heat treatment leads to structural heterogeneity of the glycoforms. Biochem. Biophys. Res. Commun. 1997, 236, 413-417.
14. Czerwenka, C., Maier, I., Pittner, F., Lindner, W., Investigation of the lactosylation of whey proteins by liquid chromatography-mass spectrometry. J. Agric. Food Chem. 2006, 54, 8874-8882.
15. Losito, I., Carbonara, T., Monaci, L., Palmisano, F., Evaluation of the thermal history of bovine milk from the lactosylation of whey proteins: an investigation by liquid chromatography-electrospray ionization mass spectrometry. Anal. Bioanal. Chem. 2007, 389, 2065-2074.
16. Monaci, L., van Hengel, A. J., Effect of heat treatment on the detection of intact bovine beta-lactoglobulins by LC mass spectrometry. J. Agric. Food Chem. 2007, 55, 2985-2992.
17. Fenaille, F., Campos-Giménez, E., Guy, P. A., Schmitt, C., Morgan, F., Monitoring of beta-lactoglobulin dry-state glycation using various analytical techniques. Anal. Biochem. 2003, 320, 144-148.
18. Meltretter, J., Birlouez-Aragon, I., Becker, C. M., Pischetsrieder, M., Assessment of heat treatment of dairy products by MALDI-TOF-MS. Mol. Nutr. Food Res. 2009, 53, 1487-1495.
19. Fenaille, F., Morgan, F., Parisod, V., Tabet, J. C., Guy, P. A., Solid-state glycation of beta-lactoglobulin monitored by electrospray ionisation mass spectrometry and gel electrophoresis techniques. Rapid Commun. Mass Spectrom. 2003, 17, 1483-1492.
20. Lund, M. N., Olsen, K., Sørensen, J., Skibsted, L. H., Kinetics and mechanism of lactosylation of alpha-lactalbumin. J. Agric. Food Chem. 2005, 53, 2095-2102.
21. Scaloni, A., Perillo, V., Franco, P., Fedele, E. et al., Characterization of heat-induced lactosylation products in caseins by immunoenzymatic and mass spectrometric methodologies. Biochim. Biophys. Acta 2002, 1598, 30-39.
22. Leonil, J., Molle, D., Fauquant, J., Maubois, J. L. et al., Characterization by ionization mass spectrometry of lactosyl beta-lactoglobulin conjugates formed during heat treatment of milk and whey and identification of one lactose-binding site. J. Dairy Sci. 1997, 80, 2270-2281.
23. Fogliano, V., Monti, S. M., Visconti, A., Randazzo, G. et al., Identification of a b-lactoglobulin lactosylation site. Biochim. Biophys. Acta 1998, 1388, 295-304.
24. Meltretter, J., Becker, C. M., Pischetsrieder, M., Identification and site-specific relative quantification of beta-lactoglobulin modifications in heated milk and dairy products. J. Agric. Food Chem. 2008, 56, 5165-5171.
25. Fenaille, F., Morgan, F., Parisod, V., Tabet, J. C., Guy, P. A., Solid-state glycation of beta-lactoglobulin by lactose and galactose: localization of the modified amino acids using mass spectrometric techniques. J. Mass Spectrom. 2004, 39, 16-28.
26. Henle, T., Walter, H., Klostermeyer, H., Evaluation of the extent of the early Maillard-reaction in milk products by direct measurement of the Amadori-product lactulosyllysine. Z. Lebensm. Unters. Forsch. 1991, 193, 119-122.
27. Sebekova, K., Somoza, V., Dietary advanced glycation endproducts (AGEs) and their health effects. Mol. Nutr. Food Res. 2007, 51, 1079-1084.
28. Henle, T., Dietary advanced glycation end products-a risk to human health? A call for an interdisciplinary debate. Mol. Nutr. Food Res. 2007, 51, 1075-1078.
29. Rérat, A., Calmes, R., Vaissade, P., Finot, P. A., Nutritional and metabolic consequences of the early Maillard reaction of heat treated milk in the pig. Significance for man. Eur. J. Nutr. 2002, 41, 1-11.
30. Karamanova, L., Fukal, L., Kodicek, M., Rauch, P. et al., Immunoprobes for thermally-induced alteration in whey protein structure and their application to the analysis of thermally-treated milks. Food Agric. Immunol. 2003, 15, 77-91.
31. Gruber, P., Vieths, S., Wangorsch, A., Nerkamp, J., Hofmann, T., Maillard reaction and enzymatic browning affect the allergenicity of Pru av 1, the major allergen from cherry (Prunus avium). J. Agric. Food Chem. 2004, 52, 4002-4007.
32. Birlouez-Aragon, I., Pischetsrieder, M., Leclere, J., Morales, F. J. et al., Assessment of protein glycation markers in infant formulas. Food Chem. 2004, 87, 253-259.
33. Drusch, S., Faist, V., Erbersdobler, H. F., Determination of N(epsilon)-carboxymethyllysine in milk products by a modified reversed-phase HPLC method. Food Chem. 1999, 65, 547-553.
34. Henle, T., Schwarzenbolz, U., Klostermeyer, H., Detection and quantification of pentosidine in foods. Z. Lebensm. Unters. Forsch. 1997, 204, 95-98.
35. Pischetsrieder, M., Gross, U., Schoetter, C., Detection of Maillard products of lactose in heated or processed milk by HPLC/DAD. Z. Lebensm. Unters. Forsch. 1999, 208, 172-177.
36. Baxter, J. H., Lai, C. S., Phillips, R. R., Dowlati, L. et al., Direct determination of methionine sulfoxide in milk proteins by enzyme hydrolysis/high-performance liquid chromatography. J. Chromatogr. A 2007, 1157, 10-16.
37. Meltretter, J., Seeber, S., Humeny, A., Becker, C. M., Pischetsrieder, M., Site-specific formation of Maillard, oxidation, and condensation products from whey proteins during reaction with lactose. J. Agric. Food Chem. 2007, 55, 6096-6103.
38. Fenaille, F., Parisod, V., Vuichoud, J., Tabet, J. C., Guy, P. A., Quantitative determination of dityrosine in milk powders by liquid chromatography coupled to tandem mass spectrometry using isotope dilution. J. Chromatogr. A 2004, 1052, 77-84.
39. Fenaille, F., Parisod, V., Tabet, J. C., Guy, P. A., Carbonylation of milk powder proteins as a consequence of processing conditions. Proteomics 2005, 5, 3097-3104.
40. Wessel, D., Flügge, U. I., A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem. 1984, 138, 141-143.
41. Aschaffenburg, R., Drewry, J., New procedure for the routine determination of the various noncasein proteins of milk. XV. International Dairy Congress, Vol. 3, London, 1959, 1631-1637.
42. Braconi, D., Bernardini, G., Possenti, S., Laschi, M. et al., Proteomics and redox-proteomics of the effects of herbicides on a wild-type wine Saccharomyces cerevisiae strain. J. Proteome Res. 2009, 8, 256-267.
43. Salzano, A. M., Arena, S., Renzone, G., D'Ambrosio, C. et al., A widespread picture of the Streptococcus thermophilus proteome by cell lysate fractionation and gel-based/gel-free approaches. Proteomics 2007, 7, 1420-1433.
44. Righetti, P. G., Boschetti, E., The ProteoMiner and the FortyNiners: searching for gold nuggets in the proteomic arena. Mass Spectrom. Rev. 2008, 27, 596-608.
45. Boschetti, E., Righetti, P. G., The art of observing rare protein species in proteomes with peptide ligand libraries. Proteomics 2009, 9, 1492-1510.
46. D'Amato, A., Bachi, A., Fasoli, E., Boschetti, E. et al., In-depth exploration of cow's whey proteome via combinatorial peptide ligand libraries. J. Proteome Res. 2009, 8, 3925-3936.
47. Candiano, G., Dimuccio, V., Bruschi, M., Santucci, L. et al., Combinatorial peptide ligand libraries for urine proteome analysis: investigation of different elution systems. Electrophoresis 2009, 30, 2405-2411.
48. Scaloni, A., Ingallinella, P., Andolfo, A., Jones, W. et al., Structural investigations on human erythrocyte acylpeptide hydrolase by mass spectrometric procedures. J. Protein Chem. 1999, 18, 349-360.
49. D'Ambrosio, C., Arena, S., Fulcoli, G., Scheinfeld, M. H. et al., Hyperphosphorylation of JNK-interacting protein 1, a protein associated with Alzheimer disease. Mol. Cell. Proteomics 2006, 5, 97-113.
50. Scippa, G. S., Rocco, M., Ialicicco, M., Trupiano, D. et al., The proteome of lentil (Lens culinaris Medik.) seeds: discriminating between landraces. Electrophoresis 2010, 31, 497-506.
51. Lee, J. H., Kim, Y., Ha, M. Y., Lee, E. K., Choo, J., Immobilization of aminophenylboronic acid on magnetic beads for the direct determination of glycoproteins by matrix assisted laser desorption ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 2005, 16, 1456-1460.
52. Gontarev, S., Shmanai, V., Frey, S. K., Kvach, M., Schweigert, F. J., Application of phenylboronic acid modified hydrogel affinity chips for high-throughput mass spectrometric analysis of glycated proteins. Rapid Commun. Mass Spectrom. 2007, 21, 1-6.
53. Frolov, A., Hoffmann, R., Analysis of amadori peptides enriched by boronic acid affinity chromatography. Ann. N. Y. Acad. Sci. 2008, 1126, 253-256.
54. Zhang, Q., Tang, N., Brock, J. W., Mottaz, H. M. et al., Enrichment and analysis of nonenzymatically glycated peptides: boronate affinity chromatography coupled with electron-transfer dissociation mass spectrometry. J. Proteome Res. 2007, 6, 2323-2330.
55. Zhang, Q., Tang, N., Schepmoes, A. A., Phillips, L. S. et al., Proteomic profiling of nonenzymatically glycated proteins in human plasma and erythrocyte membranes. J. Proteome Res. 2008, 7, 2025-2032.
56. Zhang, Q., Schepmoes, A. A., Brock, J. W., Wu, S. et al., Improved methods for the enrichment and analysis of glycated peptides. Anal. Chem. 2008, 80, 9822-9829.
57. Syka, J. E., Coon, J. J., Schroeder, M. J., Shabanowitz, J., Hunt, D. F., Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc. Natl. Acad. Sci. USA 2004, 101, 9528-9533.
58. Zhang, Q., Frolov, A., Tang, N., Hoffmann, R. et al., Application of electron transfer dissociation mass spectrometry in analyses of non-enzymatically glycated peptides. Rapid Commun. Mass Spectrom. 2007, 21, 661-666.
59. Mollé, D., Morgan, F., Bouhallab, S., Léonil, J., Selective detection of lactolated peptides in hydrolysates by liquid chromatography/ electrospray tandem mass spectrometry. Anal. Biochem. 1998, 259, 152-161.
60. Marvin, L. F., Parisod, V., Fay, L. B., Guy, P. A., Characterization of lactosylated proteins of infant formula powders using two-dimensional gel electrophoresis and nanoelectrospray mass spectrometry. Electrophoresis 2002, 23, 2505-2512.
61. Boye, J. I., Alli, I., Thermal denaturation of mixtures of β-lactalbumin and a-lactoglobulin: a differential scanning calorimetric study. Food Res. Int. 2000, 33, 673-682.
62. de la Fuente, M. A., Singh, H. H. Y., Recent advances in the characterisation of heat induced aggregates and intermediates of whey proteins. Trends Food Sci. Technol. 2002, 13, 262-274.
63. Meisel, H., Biochemical properties of peptides encrypted in bovine milk proteins. Curr. Med. Chem. 2005, 12, 1915-1919.
64. Haque, E., Chand, R., Antihypertensive and antimicrobial bioactive peptides from milk proteins. Eur. Food Res. Technol. 2008, 227, 7-15.
65. Clare, D. A., Swaisgood, H. E., Bioactive milk peptides: a prospectus. J. Dairy Sci. 2000, 83, 1187-1195.
66. Astwood, J. D., Leach, J. N., Fuchs, R. L., Stability of food allergens to digestion in vitro. Nat. Biotechnol. 1996, 14, 1269-1273.
67. Wal, J. M., Structure and function of milk allergens. Allergy 2001, 56, 35-38.