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

Specific interactions between gC1qR and alpha1-adrenoceptor subtypes.

Andre S Pupo1, Kenneth P Minneman

  • 1Department of Pharmacology, Rollins Research Center, Emory University School of Medicine, Atlanta, Georgia 30322, USA.

Journal of Receptor and Signal Transduction Research
|November 25, 2003
PubMed
Summary

The complement component 1q binding protein (gC1qR) specifically interacts with alpha1B- and alpha1D-adrenoceptors (ARs), but not alpha1A-ARs. This interaction requires the C-terminal tail of the adrenoceptors.

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

Vascular Hyporesponsiveness in Sepsis Is Associated With Nitric Oxide-Dependent Activation of G-Protein Receptor Kinase.

Journal of cardiovascular pharmacology·2026
Same author

In Vitro Contraction of Isolated Cauda Epididymal Duct Smooth Muscle as a Complimentary Approach to Physiological, Pathological, Toxicological, and Pharmacological Studies on Epididymal Function.

Methods in molecular biology (Clifton, N.J.)·2021
Same author

The affinity and selectivity of α-adrenoceptor antagonists, antidepressants, and antipsychotics for the human α1A, α1B, and α1D-adrenoceptors.

Pharmacology research & perspectives·2020
Same author

Mirabegron elicits rat corpus cavernosum relaxation and increases in vivo erectile response.

European journal of pharmacology·2019
Same author

Updates in the function and regulation of α<sub>1</sub> -adrenoceptors.

British journal of pharmacology·2019
Same author

Contractile Effects of Serotonin (5-HT) in the Rat Cauda Epididymis: Expression and Functional Characterization of 5-HT Receptors.

The Journal of pharmacology and experimental therapeutics·2019

Area of Science:

  • Molecular biology
  • Cell biology
  • Biochemistry

Background:

  • The multi-functional protein gC1qR interacts with alpha1B-adrenoceptors (ARs) via an arginine-rich motif in its C-tail, influencing receptor expression and localization.
  • A similar motif exists in alpha1D-ARs, but not alpha1A-ARs, suggesting potential differences in gC1qR interaction specificity.

Purpose of the Study:

  • To investigate the specificity of the interaction between gC1qR and different human alpha1-AR subtypes (alpha1A, alpha1B, and alpha1D).
  • To confirm the role of the C-terminal arginine-rich motif in mediating the interaction between gC1qR and alpha1-ARs.

Main Methods:

  • Coexpression of Flag-tagged human alpha1-AR subtypes and HA-tagged gC1qR in HEK293 cells.
  • Immunoprecipitation assays to detect gC1qR and alpha1-AR interactions.

Related Experiment Videos

  • Analysis of interactions using truncated alpha1-ARs lacking the C-terminal tail.

    • Main Results:

    • Immunoprecipitation studies demonstrated that gC1qR specifically coimmunoprecipitated with alpha1B-ARs and alpha1D-ARs, but not with alpha1A-ARs.
    • Conversely, Flag-tagged alpha1B-ARs and alpha1D-ARs, but not alpha1A-ARs, coimmunoprecipitated HA-tagged gC1qR.
    • Truncation of the C-terminal tail of alpha1-ARs abolished the interaction with gC1qR, confirming the motif's importance.

    Conclusions:

    • gC1qR exhibits specific binding to alpha1B- and alpha1D-adrenoceptors.
    • The interaction is subtype-selective, excluding alpha1A-adrenoceptors.
    • An intact C-terminal tail containing the arginine-rich motif is essential for gC1qR binding to alpha1-ARs.