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

The cell adhesion domain in plasma vitronectin is cryptic

D Seiffert1, J W Smith

  • 1Department of Vascular Biology, The Scripps Research Institute, La Jolla, California 92037, USA. seiffeda@a1.lldmpc.umc.dupont.com

The Journal of Biological Chemistry
|May 23, 1997
PubMed
Summary

Native vitronectin (Vn) in plasma does not bind integrins. However, denatured Vn readily binds to integrin receptors like glycoprotein IIb/IIIa and alphavbeta3, suggesting conformational changes are key to Vn

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 rabbit model of cerebral microembolic signals for translational research: preclinical validation for aspirin and clopidogrel.

Journal of thrombosis and haemostasis : JTH·2016
Same author

Progress towards testing the amyloid hypothesis: inhibitors of APP processing.

Current opinion in drug discovery & development·2001
Same author

A method for defining binding sites involved in protein-protein interactions: analysis of the binding of plasminogen activator inhibitor 1 to the somatomedin domain of vitronectin.

Analytical biochemistry·2001
Same author

Rapid loss of microvascular integrin expression during focal brain ischemia reflects neuron injury.

Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism·2001
Same author

Positive-negative epitope-tagging of beta amyloid precursor protein to identify inhibitors of A beta processing.

Brain research. Molecular brain research·2000
Same author

Presenilin-1 and -2 are molecular targets for gamma-secretase inhibitors.

The Journal of biological chemistry·2000

Area of Science:

  • Biochemistry
  • Cell Biology
  • Hematology

Background:

  • Vitronectin (Vn) is a significant adhesive glycoprotein found in blood plasma.
  • The biological functions of Vn are modulated by its conformational state and multimerization.
  • Integrin adhesion receptors play a crucial role in cell-cell and cell-matrix interactions.

Purpose of the Study:

  • To compare the binding capabilities of native and denatured vitronectin to integrin adhesion receptors.
  • To investigate the role of Vn conformation in its adhesive properties.

Main Methods:

  • Utilized antibody binding assays to assess the accessibility of the cell adhesion domain in native Vn.
  • Performed dose-dependent binding studies of native and denatured Vn to glycoprotein IIb/IIIa and alphavbeta3 integrins.

Related Experiment Videos

  • Induced Vn denaturation through thermal treatment and complexation with plasminogen activator inhibitor-1 (PAI-1).

    • Main Results:

    • Native plasma Vn failed to bind to glycoprotein IIb/IIIa and alphavbeta3 integrins.
    • Denatured Vn exhibited dose-dependent binding to both glycoprotein IIb/IIIa and alphavbeta3.
    • Thermal denaturation or PAI-1 complexation exposed the cell adhesion domain of Vn.

    Conclusions:

    • Plasma vitronectin is not inherently adhesive due to its native conformation.
    • Conformational alterations expose the cell adhesion domain, enabling avid binding to integrins.
    • These conformational changes in Vn likely occur during tissue injury and thrombosis.