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Recombinant and native zymogen forms of human complement factor D

Y Yamauchi1, J W Stevens, K J Macon

  • 1Department of Medicine, University of Alabama at Birmingham 35294.

Journal of Immunology (Baltimore, Md. : 1950)
|April 1, 1994
PubMed
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Researchers identified and characterized human factor D zymogen (profactor D) using recombinant expression and purification from patient urine. Trypsin efficiently activates profactor D, revealing its role in complement system regulation.

Area of Science:

  • Biochemistry
  • Immunology
  • Proteolysis

Background:

  • Human factor D is a serine protease crucial for the alternative complement pathway.
  • The inactive precursor, or zymogen, of human factor D has remained elusive.
  • Understanding factor D activation is key to regulating complement-mediated inflammation.

Purpose of the Study:

  • To express and characterize the full-length human factor D zymogen.
  • To investigate the activation mechanism and properties of recombinant and native profactor D.
  • To compare the activation of profactor D by different proteases.

Main Methods:

  • Expression of human factor D cDNA using a baculovirus system.
  • Purification and characterization of recombinant profactor D.

Related Experiment Videos

  • Amino acid sequencing and enzymatic activity assays.
  • Purification of native profactor D from patient urine.

    • Main Results:

    • Recombinant protein identified as profactor D with activation peptides AAPPRGR and APPRGR.
    • Trypsin efficiently converted profactor D to active factor D with similar properties to native factor D.
    • Other proteases like thrombin, kallikrein, and plasmin activated profactor D less efficiently.
    • Native profactor D purified from urine had a Gly-Arg activation peptide and was inhibited by DFP.

    Conclusions:

    • Human factor D exists as a zymogen (profactor D) that can be activated by trypsin.
    • Recombinant and native profactor D exhibit distinct activation pathways and properties.
    • Profactor D plays a role in complement regulation, with potential implications for inflammatory diseases.