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Related Experiment Videos

Molecular basis for the microheterogeneity of human complement factor B.

G Garnier1, C Davrinche, R Charlionet

  • 1Institut National de la Santé et de la Recherche Médicale, Unité 78, Bois-Guillaume, France.

Complement (Basel, Switzerland)
|January 1, 1988
PubMed
Summary

Human complement factor B heterogeneity stems from sialic acid levels on N-glycans. This finding clarifies posttranslational modifications impacting protein structure and function.

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Area of Science:

  • Biochemistry
  • Immunology
  • Glycobiology

Background:

  • Human complement factor B (fB) exhibits charge heterogeneity.
  • This microheterogeneity may arise from posttranslational modifications.

Purpose of the Study:

  • To investigate the role of sialic acids in human fB microheterogeneity.
  • To explore the relationship between heterogeneity and posttranslational events in cultured cells.

Main Methods:

  • Desialylation kinetics analysis.
  • Isoelectric focusing of fB.
  • Cultured hepatoma cells.
  • Tunicamycin treatment to inhibit N-glycosylation.

Main Results:

  • Desialylation revealed fB charge intermediates from complex native to homogeneous forms.

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  • Intracellular fB matched desialylated fB; secreted fB was heterogeneous.
  • Inhibition of N-glycosylation normalized both intracellular and secreted fB patterns.

    • Conclusions:

    • Human fB microheterogeneity is primarily due to variable sialylation of N-glycans.
    • Posttranslational sialylation, not N-glycosylation itself, drives fB charge heterogeneity.