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

[Epidermal growth factor and its receptor: the structure and function].

S Gamou1, N Shimizu

  • 1Department of Molecular Biology, Keio University School of Medicine.

Nihon Rinsho. Japanese Journal of Clinical Medicine
|August 1, 1992
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

Hepatocyte growth factor is linked by O-glycosylated oligosaccharide on the alpha chain.

Biochemical and biophysical research communications·1992
Same author

Overproduction of biologically-active human nerve growth factor in Escherichia coli.

Bioscience, biotechnology, and biochemistry·1992
Same author

Electrophysiological study of neurotropin-induced responses in guinea pig hypothalamic neurons.

Brain research bulletin·1992
Same author

[Burkitt's lymphoma diagnosed by molecular analysis of DNA from malignant cells in ascites].

[Rinsho ketsueki] The Japanese journal of clinical hematology·1992
Same author

[A case of periodic ataxia].

Rinsho shinkeigaku = Clinical neurology·1992
Same author

[A case of traumatic right diaphragmatic hernia diagnosed by pleurography].

Kyobu geka. The Japanese journal of thoracic surgery·1992

Structural changes in Epidermal Growth Factor (EGF) can alter its ability to bind its receptor, impacting cell signaling. Researchers used mutagenesis and mutant receptor studies to understand these EGF-receptor interactions.

Area of Science:

  • Molecular biology
  • Cell signaling
  • Biochemistry

Background:

  • Epidermal Growth Factor (EGF) initiates signal transduction upon binding to its membrane receptor.
  • This binding activates the receptor's intrinsic tyrosine kinase activity, a crucial step in cellular communication.
  • Understanding the structural basis of this interaction is key to deciphering cellular responses.

Purpose of the Study:

  • To investigate how structural modifications of EGF affect its receptor binding affinity.
  • To explore the functional consequences of altering EGF structure on signal transduction.
  • To analyze the role of EGF receptor structural characteristics in mediating EGF's effects.

Main Methods:

  • Site-directed mutagenesis was used to create altered EGF molecules.

Related Experiment Videos

  • Mutant EGF receptor constructs were expressed in transfected cells.
  • The binding ability and functional properties of modified EGF and receptors were assessed.
  • Main Results:

    • Structural alterations in EGF directly influence its binding to the EGF receptor.
    • Specific structural features of EGF are critical for maintaining receptor interaction.
    • Mutant receptor studies confirmed the importance of receptor structure in mediating EGF's biological effects.

    Conclusions:

    • The interaction between EGF and its receptor is highly structure-dependent.
    • Modifications in EGF structure can significantly impair or alter receptor binding and downstream signaling.
    • Further research into EGF-receptor dynamics can reveal therapeutic targets for diseases involving aberrant signaling.