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Analysis of γ-globulin mobility on routine clinical CE equipment: exploring its molecular basis and potential clinical utility

Dieter Vanderschaeghe (UGent) , Evi Debruyne (UGent) , Hans Van Vlierberghe (UGent) , Nico Callewaert (UGent) and Joris Delanghe (UGent)
(2009) ELECTROPHORESIS. 30(15). p.2617-2623
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Abstract
A study was conducted on the variability of gamma-globulin mobility in serum protein electrophoresis and its molecular basis. We found that the migration time of gamma-globulins can be reproducibly determined (CV = 1.1%) on clinical CE equipment. Moreover, we found a significant difference (p<0.001) in the migration of gamma-globulins between chronic liver disease patients (n = 98) and a healthy reference group (n = 47). Serum immunoglobulins were purified from these patients' sera using protein L-agarose and their glycosylation was studied using CE on a DNA sequencer. This glycomics approach revealed that several non-sialylated N-glycans show a moderate Pearson correlation coefficient (r = 0.2-0.4) with the migration time of gamma-globulins. Their sialylated structures correlate negatively (r = -0.2 to -0.3). Immunoglobulins are significantly more sialylated in the healthy reference group compared with the patients (p<0.001). We estimated that sialylation heterogeneity contributes about 36% to the molecular variance (carbohydrates and amino-acid composition) that affects the electrophoretic mobility of immunoglobulins. This is the first report on the migration time of gamma-globulins on a clinical CE instrument and its potential clinical value to the routinely analyzed serum protein CE profiles.
Keywords
ANTIINFLAMMATORY ACTIVITY, CAPILLARY-ELECTROPHORESIS, SERUM-PROTEIN GLYCOMICS, DNA-SEQUENCING EQUIPMENT, Serum protein electrophoresis, Liver fibrosis, Immunoglobulins, Glycomics, DSA-FACE, HUMAN-IGG, GLYCOSYLATION, FC

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MLA
Vanderschaeghe, Dieter et al. “Analysis of Γ-globulin Mobility on Routine Clinical CE Equipment: Exploring Its Molecular Basis and Potential Clinical Utility.” ELECTROPHORESIS 30.15 (2009): 2617–2623. Print.
APA
Vanderschaeghe, D., Debruyne, E., Van Vlierberghe, H., Callewaert, N., & Delanghe, J. (2009). Analysis of γ-globulin mobility on routine clinical CE equipment: exploring its molecular basis and potential clinical utility. ELECTROPHORESIS, 30(15), 2617–2623.
Chicago author-date
Vanderschaeghe, Dieter, Evi Debruyne, Hans Van Vlierberghe, Nico Callewaert, and Joris Delanghe. 2009. “Analysis of Γ-globulin Mobility on Routine Clinical CE Equipment: Exploring Its Molecular Basis and Potential Clinical Utility.” Electrophoresis 30 (15): 2617–2623.
Chicago author-date (all authors)
Vanderschaeghe, Dieter, Evi Debruyne, Hans Van Vlierberghe, Nico Callewaert, and Joris Delanghe. 2009. “Analysis of Γ-globulin Mobility on Routine Clinical CE Equipment: Exploring Its Molecular Basis and Potential Clinical Utility.” Electrophoresis 30 (15): 2617–2623.
Vancouver
1.
Vanderschaeghe D, Debruyne E, Van Vlierberghe H, Callewaert N, Delanghe J. Analysis of γ-globulin mobility on routine clinical CE equipment: exploring its molecular basis and potential clinical utility. ELECTROPHORESIS. 2009;30(15):2617–23.
IEEE
[1]
D. Vanderschaeghe, E. Debruyne, H. Van Vlierberghe, N. Callewaert, and J. Delanghe, “Analysis of γ-globulin mobility on routine clinical CE equipment: exploring its molecular basis and potential clinical utility,” ELECTROPHORESIS, vol. 30, no. 15, pp. 2617–2623, 2009.
@article{748928,
  abstract     = {A study was conducted on the variability of gamma-globulin mobility in serum protein electrophoresis and its molecular basis. We found that the migration time of gamma-globulins can be reproducibly determined (CV = 1.1%) on clinical CE equipment. Moreover, we found a significant difference (p<0.001) in the migration of gamma-globulins between chronic liver disease patients (n = 98) and a healthy reference group (n = 47). Serum immunoglobulins were purified from these patients' sera using protein L-agarose and their glycosylation was studied using CE on a DNA sequencer. This glycomics approach revealed that several non-sialylated N-glycans show a moderate Pearson correlation coefficient (r = 0.2-0.4) with the migration time of gamma-globulins. Their sialylated structures correlate negatively (r = -0.2 to -0.3). Immunoglobulins are significantly more sialylated in the healthy reference group compared with the patients (p<0.001). We estimated that sialylation heterogeneity contributes about 36% to the molecular variance (carbohydrates and amino-acid composition) that affects the electrophoretic mobility of immunoglobulins. This is the first report on the migration time of gamma-globulins on a clinical CE instrument and its potential clinical value to the routinely analyzed serum protein CE profiles.},
  author       = {Vanderschaeghe, Dieter and Debruyne, Evi and Van Vlierberghe, Hans and Callewaert, Nico and Delanghe, Joris},
  issn         = {0173-0835},
  journal      = {ELECTROPHORESIS},
  keywords     = {ANTIINFLAMMATORY ACTIVITY,CAPILLARY-ELECTROPHORESIS,SERUM-PROTEIN GLYCOMICS,DNA-SEQUENCING EQUIPMENT,Serum protein electrophoresis,Liver fibrosis,Immunoglobulins,Glycomics,DSA-FACE,HUMAN-IGG,GLYCOSYLATION,FC},
  language     = {eng},
  number       = {15},
  pages        = {2617--2623},
  title        = {Analysis of γ-globulin mobility on routine clinical CE equipment: exploring its molecular basis and potential clinical utility},
  url          = {http://dx.doi.org/10.1002/elps.200900054},
  volume       = {30},
  year         = {2009},
}

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