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Related Experiment Videos

Function of the factor I modules (FIMS) of human complement component C6.

R G DiScipio1, S M Linton, N K Rushmere

  • 1La Jolla Institute for Experimental Medicine, La Jolla, California 92037, USA.

The Journal of Biological Chemistry
|November 5, 1999
PubMed
Summary
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The factor I modules (FIMs) in complement component C6 are crucial for efficient C5b-6 complex formation. Deleting FIMs reduces C6 activity, particularly in the Classical Pathway, highlighting their role in C6-C5 interaction.

Area of Science:

  • Immunology
  • Complement System Biology

Background:

  • The complement system is vital for innate and adaptive immunity.
  • Complement component C6 plays a role in the terminal pathway of complement activation.
  • Understanding C6 function is key to deciphering complement-mediated immune responses.

Purpose of the Study:

  • To elucidate the functional role of specific modules within complement component C6.
  • To investigate the contribution of Factor I Modules (FIMs) and Complement Control Protein (CCP) modules to C6 activity.
  • To compare the functional impact of FIMs and CCPs on C6 in both Classical and Alternative Complement Pathways.

Main Methods:

  • Recombinant expression of truncated C6 molecules, including C6 lacking FIMs (C6des-748-913) and C6 lacking both CCP and FIMs (C6des-611-913).

Related Experiment Videos

  • Assays for hemolytic activity of full-length and truncated C6 in both Classical and Alternative Complement Pathways.
  • Measurement of the stability and decay rates of metastable C5b* and (125)I-C5b in different complement pathways.
  • Investigation of the binding kinetics of C5 to C6 and its truncated variants.

    • Main Results:

    • C6 lacking FIMs (C6des-748-913) showed reduced hemolytic activity (60-70% in Alternative Pathway, 4-6% in Classical Pathway) compared to full-length C6.
    • The stability of metastable C5b* and the half-life of (125)I-C5b were significantly longer in the Alternative Pathway than in the Classical Pathway.
    • (125)I-C5 binding to C6 was ionic strength-dependent, weak to C6des-FIMs, and absent in C6des-CCP/FIMs.

    Conclusions:

    • Factor I Modules (FIMs) are important for efficient C6 interaction with C5, facilitating C5b-6 complex formation.
    • While not absolutely essential, FIMs significantly enhance C6 activity, particularly in the Classical Pathway.
    • Differences in C5b* stability between complement pathways contribute to the observed functional variations of truncated C6 molecules.