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A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples
Published on: October 2, 2009
Evaluation and clinical interest of mannan binding lectin function in human plasma
C Dumestre-Perard1, D Ponard, G J Arlaud
1Laboratoire d'Immunologie, Hôpital Sud, Université Joseph Fourier JE2236, Avenue de Kimberley, 38130 Echirolles, France. cdumestre-perard@chu-grenoble.fr
Molecular Immunology
|November 5, 2002
Summary
Mannan-binding lectin (MBL) activity is crucial for innate immunity. This study developed a method to measure MBL specific activity, finding higher oligomers are more effective at complement activation.
Area of Science:
- Immunology
- Biochemistry
Background:
- Mannan-binding lectin (MBL) is key in innate immunity, activating complement.
- The relationship between MBL gene polymorphism, oligomeric state, and activity is unclear.
- Assessing MBL function solely by protein levels or genotyping is insufficient.
Purpose of the Study:
- To develop a method for calculating specific activity of circulating MBL.
- To investigate the functional differences between MBL oligomeric forms.
Main Methods:
- Purification of MBL from human plasma using a three-step process.
- Development of a simplified MBL activity assay based on complement activation.
- Analysis of MBL oligomeric forms and their C4 cleavage efficiency.
Main Results:
- A highly purified MBL preparation was obtained, existing in two oligomeric forms.
- Higher MBL oligomeric forms demonstrated more efficient C4 cleavage than lower forms.
- A method for calculating MBL specific activity (MBLsa) was established.
Conclusions:
- The developed method allows for the assessment of MBL biological activity.
- Higher MBL oligomers exhibit superior complement-activating capacity.
- This assay has potential applications in studying diseases like chronic hepatitis C and investigating MBL genotype-phenotype correlations.
