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Related Experiment Videos

C5L2, a nonsignaling C5A binding protein.

Shoji Okinaga1, Dubhfeasa Slattery, Alison Humbles

  • 1The Ina Sue Perlmutter Laboratory, Children's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.

Biochemistry
|August 6, 2003
PubMed
Summary
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The orphan receptor C5L2 binds C5a with high affinity but does not activate typical signaling pathways. C5L2 may modulate C5a

Area of Science:

  • Immunology
  • Molecular Biology
  • Cellular Signaling

Background:

  • C5a anaphylatoxin is a key inflammatory mediator acting via G protein-coupled receptors.
  • The complete in vivo effects of C5a are not fully explained by the known C5a receptor (C5aR).

Purpose of the Study:

  • To investigate the role of the orphan receptor C5L2 in C5a binding and signaling.
  • To characterize the functional properties of C5L2 in response to C5a.

Main Methods:

  • Transfection of C5L2 into cell lines.
  • C5a binding assays and assessment of downstream signaling (MAPK activation, calcium flux, chemotaxis).
  • Microarray analysis of gene transcription in C5a receptor-deficient mice expressing C5L2.

Main Results:

Related Experiment Videos

  • C5L2 exhibits high affinity binding to C5a but is uncoupled from G proteins due to a DRY sequence mutation.
  • C5L2 shows weak phosphorylation upon C5a binding but does not induce significant cellular activation.
  • C5a receptor-deficient mice expressing C5L2 do not exhibit C5a-induced gene transcription changes.
  • C5L2 demonstrates slow ligand kinetics, no internalization, and high affinity for C5a des Arg.

Conclusions:

  • C5L2 functions as a high-affinity C5a binding protein distinct from C5aR.
  • C5L2's inability to signal suggests a modulatory role in C5a's in vivo functions.
  • C5L2 does not interact with C3a or C4a anaphylatoxins.