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

alpha 11beta 1 integrin recognizes the GFOGER sequence in interstitial collagens.

Wan-Ming Zhang1, Jarmo Kapyla, J Santeri Puranen

  • 1Department of Medical Biochemistry and Microbiology, Biomedical Center, Box 582, Uppsala University, Uppsala S-751 23, Sweden.

The Journal of Biological Chemistry
|December 24, 2002
PubMed
Summary

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

A living biobank of sarcoma patient-derived cell cultures reveals multi-omic and functional insights that capture disease heterogeneity.

Clinical and translational medicine·2026
Same author

P4HA3 is dispensable for prolyl 4-hydroxylation of type I collagen during mouse development.

The Journal of biological chemistry·2026
Same author

Jagged1 regulates extracellular matrix deposition and remodeling in triple-negative breast cancer.

Science advances·2026
Same author

PI3K and MAPK Signaling Nodes Serve as Divergent Drivers of Phenotypic Plasticity in Cancer-Associated Fibroblasts in Colorectal Cancer.

Cancer research·2026
Same author

C1s protects cutaneous squamous carcinoma cells from TRAIL-induced apoptosis.

Oncogenesis·2026
Same author

Embigin is involved in the regulation of early mouse kidney development.

Scientific reports·2026

Integrins alpha(11)beta(1) and alpha(2)beta(1) both recognize the GFOGER motif in fibrillar collagens, despite differing calcium sensitivities. This suggests overlapping functions for these collagen receptors.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Integrin Biology

Background:

  • Integrins are cell surface receptors involved in cell adhesion.
  • The collagen receptor subgroup includes integrins alpha(1)beta(1), alpha(2)beta(1), alpha(10)beta(1), and alpha(11)beta(1).
  • Integrins alpha(1)beta(1) and alpha(2)beta(1) recognize GFOGER motifs in collagen.

Purpose of the Study:

  • Investigate the collagen recognition mechanism of integrin alpha(11)beta(1).
  • Compare the ligand binding properties of alpha(11)beta(1) with alpha(2)beta(1).

Main Methods:

  • Utilized C2C12 cells transfected with alpha(11) cDNA.
  • Employed bacterially expressed recombinant alpha(11) I domain.
  • Assessed Mg(2+)-dependent binding to type I collagen, varying Ca(2+) concentrations.

Related Experiment Videos

  • Compared binding of alpha(11)beta(1) and alpha(2)beta(1) to fibrillar collagens, collagens IV, and VI.

    • Main Results:

    • Alpha(11)beta(1) binding to type I collagen was Mg(2+)-dependent, required micromolar Ca(2+), and was inhibited by millimolar Ca(2+).
    • Alpha(2)beta(1) binding was refractory to millimolar Ca(2+).
    • Both alpha(11)beta(1) and alpha(2)beta(1) recognized helical GFOGER sequences in fibrillar collagens.
    • Alpha(11)beta(1) and alpha(2)beta(1) showed similar preferences for fibrillar collagens over collagens IV and VI.

    Conclusions:

    • The GFOGER sequence is a common recognition motif for alpha(1)beta(1), alpha(2)beta(1), and alpha(11)beta(1) integrins in fibrillar collagens.
    • Despite sequence differences, alpha(2)beta(1) and alpha(11)beta(1) exhibit similar collagen specificities.
    • Further research is needed to determine if alpha(2)beta(1) and alpha(11)beta(1) share overlapping biological functions.