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

Homotypic fibrillin-1 interactions in microfibril assembly.

Andrew Marson1, Matthew J Rock, Stuart A Cain

  • 1Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom.

The Journal of Biological Chemistry
|December 1, 2004
PubMed
Summary

Fibrillin-1 N- and C-terminal fragments show specific homotypic binding, revealing key interactions for microfibril assembly. These calcium-dependent interactions are regulated by specific sequences and associated proteins, impacting pericellular matrix formation.

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

Spontaneous spinal CSF leaks: a rare variant exome sequencing study and functional analysis.

The Lancet. Neurology·2026
Same author

Structural and biophysical analysis of the four CHRD domains of human chordin reveals a novel binding site for glycosaminoglycans.

The Journal of biological chemistry·2026
Same author

Human pluripotent stem cell model of multiple epiphyseal dysplasia with MATN3 mutation identifies altered matrix organisation and upregulation of the cholesterol biosynthesis pathway.

Osteoarthritis and cartilage·2026
Same author

New aspects of chronic beryllium disease.

Current opinion in allergy and clinical immunology·2026
Same author

An avidity-driven mechanism of extracellular BMP regulation by Twisted gastrulation.

Development (Cambridge, England)·2026
Same author

Investigating the effects of chelating agents, surfactants and magnesium cations on the size of LPS aggregates in formulations causing low endotoxin recovery in limulus amebocyte lysate assays.

European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V·2025

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Fibrillin-1 is a major component of extracellular microfibrils.
  • Understanding fibrillin-1 self-assembly is crucial for microfibril formation and function.
  • Previous studies have not fully elucidated the specific homotypic interactions governing fibrillin-1 assembly.

Purpose of the Study:

  • To define the homotypic interactions of fibrillin-1.
  • To gain new insights into the molecular mechanisms of microfibril assembly.
  • To identify regulatory factors influencing fibrillin-1 interactions.

Main Methods:

  • Investigated dose-dependent, saturable high-affinity binding between various fibrillin-1 fragments (N-terminal, C-terminal, post-furin cleavage).
  • Assessed the impact of calcium dependency, N-ethylmaleimide treatment, and microfibril-associated glycoprotein-1 on these interactions.

Related Experiment Videos

  • Utilized binding assays to characterize specific homotypic and heterotypic interactions.

    • Main Results:

    • Demonstrated high-affinity binding between N-terminal fragments, between furin-processed C-terminal fragments, and between N- and C-terminal fragments.
    • Identified interactions between the N terminus and downstream fragments, and post-furin cleavage sequences with N- and C-terminal fragments.
    • Found that some terminal interactions were inhibited by other sequences, were calcium-dependent, and could be modulated by N-ethylmaleimide and microfibril-associated glycoprotein-1.

    Conclusions:

    • Specific homotypic interactions between fibrillin-1 termini and internal fragments are critical for microfibril assembly.
    • These interactions are regulated by calcium ions, post-translational modifications (furin cleavage), and associated proteins like microfibril-associated glycoprotein-1.
    • The defined interactions provide a framework for understanding the regulation of pericellular fibrillin-1 microfibril assembly.