Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Complement receptor type 1 (CR1, CD35) is a receptor for C1q

L B Klickstein1, S F Barbashov, T Liu

  • 1Department of Medicine, Harvard Medical School, Boston, Massachusetts 02215, USA.

Immunity
|November 5, 1997
PubMed
Summary

Complement component C1q binds to complement receptor 1 (CR1), also known as CD35. This finding identifies CR1 as a cellular C1q receptor recognizing C1q, C3b, and C4b.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

The survival of patients with high grade glioma from different ethnic groups in South East England.

Journal of neuro-oncology·2014
Same author

Under-filled blood collection tubes containing K2EDTA as anticoagulant are acceptable for automated complete blood counts, white blood cell differential, and reticulocyte count.

International journal of laboratory hematology·2010
Same author

Production of a subtracted cDNA library.

Current protocols in molecular biology·2008
Same author

Amplification of a bacteriophage library.

Current protocols in molecular biology·2008
Same author

Conversion of mRNA into double-stranded cDNA.

Current protocols in molecular biology·2008
Same author

Ligation of linkers or adapters to double-stranded cDNA.

Current protocols in molecular biology·2008

Area of Science:

  • Immunology
  • Complement System Biology

Background:

  • The cellular receptor for the collagen domain of complement component C1q remained undefined.
  • C1q plays a crucial role in initiating the classical complement pathway and immune complex clearance.

Purpose of the Study:

  • To identify the specific cellular receptor for the collagen domain of C1q.
  • To characterize the binding interaction between C1q and its cellular receptor.

Main Methods:

  • Surface plasmon resonance (SPR) was used to analyze the kinetics of C1q binding to immobilized recombinant soluble CR1 (rsCR1).
  • Binding assays were performed using transfected cells expressing CR1 and purified C1q.
  • Inhibition studies were conducted using unlabeled C1q, C1q collagen domain, and C3b dimers.

Related Experiment Videos

Main Results:

  • C1q specifically binds to human complement receptor 1 (CR1/CD35), a known receptor for C3b/C4b and opsonized immune complexes.
  • Binding of C1q to CR1 was confirmed on transfected cells and immobilized rsCR1.
  • SPR analysis revealed an apparent equilibrium dissociation constant (K[eq2]) of 3.9 nM for the C1q-CR1 interaction.
  • Binding was inhibited by unlabeled C1q and its collagen domain, and partially by C3b dimers.

Conclusions:

  • Complement receptor 1 (CR1/CD35) is identified as a cellular C1q receptor.
  • CR1 recognizes C1q, C3b, and C4b, acting as a key receptor for multiple complement opsonins.
  • This discovery advances the understanding of complement system regulation and immune complex processing.