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Related Experiment Videos

Identification of the second heparin-binding domain in human complement factor H

T K Blackmore1, J Hellwage, T A Sadlon

  • 1Department of Microbiology and Infectious Diseases, Flinders Medical Centre, Bedford Park, South Australia. tim.blackmore@flinders.edu.au

Journal of Immunology (Baltimore, Md. : 1950)
|April 8, 1998
PubMed
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Complement factor H has two heparin binding sites. These sites are located in SCR 7 and SCR 20, which are crucial for regulating complement activation on sialic acid-rich surfaces.

Area of Science:

  • Immunology
  • Biochemistry

Background:

  • Complement factor H (fH) regulates the alternative complement pathway.
  • fH prevents complement activation on sialic acid-rich surfaces.
  • Heparin binding serves as a model for fH's sialic acid-binding properties.

Purpose of the Study:

  • To identify all heparin-binding sites within complement factor H.
  • To investigate the role of specific Short Consensus Repeat (SCR) modules in heparin binding.

Main Methods:

  • Preparation of recombinant truncated and SCR deletion mutants of fH.
  • Heparin-agarose affinity chromatography to test heparin binding.
  • Analysis of fH-related proteins (FHR-3 and FHR-4) for heparin binding.

Main Results:

Related Experiment Videos

  • SCR 7 was previously identified as a heparin-binding site.
  • SCRs 16-20, specifically SCR 20, were found to contain another heparin binding site.
  • Deletion of both SCR 7 and SCR 20 abolished heparin binding.
  • FHR-3, containing an SCR homologous to fH's SCR 7, bound heparin, while FHR-4 did not.

Conclusions:

  • Complement factor H possesses two distinct heparin binding sites.
  • These sites are located in SCR 7 and SCR 20.
  • SCR 20 requires adjacent SCRs (18-19) for effective heparin binding.