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

Substrate specificities of murine C1s

R T Ogata1, P J Low, B M Bradt

  • 1Medical Biology Institute, La Jolla, CA 92037.

Journal of Immunology (Baltimore, Md. : 1950)
|June 15, 1994
PubMed
Summary
This summary is machine-generated.

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

Moiré-Induced Optical Nonlinearities: Single- and Multiphoton Resonances.

Physical review letters·2022
Same author

Topological bands for ultracold atoms.

Reviews of modern physics·2020
Same author

P-Band Induced Self-Organization and Dynamics with Repulsively Driven Ultracold Atoms in an Optical Cavity.

Physical review letters·2019
Same author

Chromaticity separation and the alpha response.

Neuropsychologia·2017
Same author

Superradiance Induced Particle Flow via Dynamical Gauge Coupling.

Physical review letters·2016
Same author

Quantum Quenches in Chern Insulators.

Physical review letters·2015

Murine C1-s (mC1-s) does not cleave sex-limited protein (Slp), challenging its proposed role in complement pathways. Murine C1-s shows species-specific activity on C4, differing from human C1-s.

Area of Science:

  • Immunology
  • Biochemistry
  • Complement System

Background:

  • The classical complement pathway initiates via C4 cleavage by C1-s.
  • Sex-limited protein (Slp) is a murine C4 isotype previously thought to be unreactive with C1-s.
  • Recent hypotheses suggested Slp's role in a novel pathway, attributing prior non-reactivity to species incompatibility.

Purpose of the Study:

  • To investigate the substrate specificity of murine C1-s (mC1-s).
  • To determine if mC1-s cleaves murine Slp, and to compare mC1-s activity on human and murine C4.

Main Methods:

  • Proteolytic activity assays were performed using purified mC1-s.
  • Substrates included human C4, murine C4 (mC4), and murine Slp.
  • Enzyme concentrations were varied to assess cleavage efficiency.

Related Experiment Videos

Main Results:

  • Murine C1-s did not cleave murine Slp, even at high enzyme concentrations.
  • mC1-s showed a 10-fold higher activity on mC4 compared to human C1-s (hC1-s).
  • mC1-s cleaved human and murine C4 with equal efficiency, unlike hC1-s which prefers human C4.

Conclusions:

  • The findings do not support Slp's essential role in complement activation via mC1-s.
  • Murine C1-s exhibits species-specific activity on C4, but not the pronounced species preference seen with hC1-s.