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Related Experiment Video

Updated: Jan 4, 2026

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion
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Complement C1q subunit molecules from Xenopus laevis possess conserved function in C1q-immunoglobulin interaction.

Fangfang Yan1, Enxu Zhou1, Shuo Liu1

  • 1Institute of Modern Aquaculture Science and Engineering, School of Life Sciences, South China Normal University, Guangdong Provincial Key Laboratory for Healthy and Safe Aquaculture, Guangdong, 510631, PR China.

Developmental and Comparative Immunology
|November 4, 2019
PubMed
Summary

Researchers cloned and analyzed Xenopus laevis C1q (XlC1q) subunits, finding conserved immunoglobulin-binding functions and inhibitory effects on complement-dependent hemolysis, suggesting functional conservation across species.

Keywords:
C1q-Ig interactionComplement component 1q (C1q)HemolysisImmunoglobulin (Ig)Xenopus laevis

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Optimized Analysis of Proteins from Xenopus Oocytes and Embryos by Immunoblotting
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Area of Science:

  • Immunology
  • Molecular Biology
  • Xenopus laevis research

Background:

  • The classical complement pathway is initiated by the C1 complex, which includes complement component 1q (C1q).
  • C1q plays a crucial role in recognizing and binding immune complexes.

Purpose of the Study:

  • To clone and analyze the C1q subunit molecules (XlC1qA, XlC1qB, XlC1qC) from Xenopus laevis.
  • To investigate the functional conservation of XlC1q in binding immunoglobulins and its role in the complement pathway.

Main Methods:

  • Cloning and sequence analysis of XlC1qA, XlC1qB, and XlC1qC from Xenopus laevis.
  • Phylogenetic analysis to determine evolutionary relationships.
  • Expression analysis in various tissues.
  • Functional assays involving interactions with aggregated immunoglobulins and C1q-dependent hemolysis.

Main Results:

  • The deduced amino acid sequences of XlC1q subunits possess characteristic collagen-like regions and C1q family domains.
  • Phylogenetic analysis places XlC1qs within the amphibian clade.
  • XlC1qs are constitutively expressed in all examined tissues, with the highest levels in the liver.
  • XlC1q demonstrated binding to mouse IgG, mouse IgM, Xenopus IgM, and Nile tilapia IgM.
  • XlC1qs inhibited C1q-dependent hemolysis in a concentration-dependent manner.

Conclusions:

  • The cloned XlC1q subunits from Xenopus laevis share structural similarities with other species.
  • XlC1q exhibits conserved functional activity in binding immunoglobulins.
  • XlC1q plays a role in inhibiting the classical complement pathway, similar to mammals and teleosts.