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

Factor VIIa-tissue factor interactions: an evaluation using factor VII-factor IX chimeras

J Y Chang1

  • 1Center for Thrombosis and Hemostasis, University of North Carolina at Chapel Hill 27599, USA.

Haemostasis
|January 1, 1996
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

Sprague Dawley rats from different vendors vary in the modulation of prepulse inhibition of startle (PPI) by dopamine, acetylcholine, and glutamate drugs.

Psychopharmacology·2023
Same author

Association of Left Vertebral Artery Hypoplasia with Posterior Circulation Stroke and the Functional Outcome of Patients with Atrial Fibrillation-Related Cardioembolic Stroke.

AJNR. American journal of neuroradiology·2022
Same author

Ultrasound-assisted desalination of crude oil: The influence of mixing extent, crude oil species, chemical demulsifier and operation variables.

Ultrasonics sonochemistry·2022
Same author

[Multidisciplinary classification of magnetic resonance imaging features of neuropsychiatric lupus].

Beijing da xue xue bao. Yi xue ban = Journal of Peking University. Health sciences·2018
Same author

Quantifying Rome symptoms for diagnosis of the irritable bowel syndrome.

Neurogastroenterology and motility·2018
Same author

[Clinical analysis on effect of retroperitoneoscopic nephrectomy in elderly donors for renal transplantation].

Zhonghua yi xue za zhi·2016
Same journal

Thrombosis and Haemostasis Issues in Cancer. International Conference. Bergamo, Italy, 2-4 November 2001. Lectures and abstracts.

Haemostasis·2002
Same journal

Biochemistry of cancer procoagulant.

Haemostasis·2002
Same journal

Management of thromboembolic disease in cancer patients.

Haemostasis·2002
Same journal

An overview of thromboprophylaxis in malignancy.

Haemostasis·2002
Same journal

Platelets cross-talk with tumor cells.

Haemostasis·2002
Same journal

Properties and function of heparanase in cancer metastasis and angiogenesis.

Haemostasis·2002
See all related articles

Researchers studied factor VIIa binding to tissue factor using chimeric molecules. Key interactions involve the EGF1 and catalytic domains, with Gla and EGF2 domains playing minor roles in binding.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein-protein interactions

Background:

  • Factor VIIa is a key enzyme in the extrinsic pathway of blood coagulation.
  • Tissue factor is the primary initiator of this pathway.
  • Understanding the interaction between factor VIIa and tissue factor is crucial for hemostasis research.

Purpose of the Study:

  • To elucidate the specific domains of factor VII involved in binding to tissue factor.
  • To characterize the molecular interactions between factor VIIa and tissue factor.

Main Methods:

  • Construction of factor VII-factor IX chimeric molecules.
  • Kinetic assays to measure binding.
  • Competition binding assays to assess domain contributions.

Related Experiment Videos

Main Results:

  • The primary binding interaction between factor VIIa and tissue factor involves the first epidermal growth factor-like (EGF1) domain and the catalytic domain.
  • The gamma-carboxyglutamic acid-containing (Gla) domain and the second epidermal growth factor-like (EGF2) domain contribute to binding in a minor capacity.
  • These minor contributions may relate to structural integrity or direct binding energy.

Conclusions:

  • The EGF1 and catalytic domains are essential for high-affinity binding of factor VIIa to tissue factor.
  • The Gla and EGF2 domains play a secondary role, potentially influencing overall molecular structure and binding affinity.
  • These findings enhance our understanding of the molecular basis of coagulation initiation.