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

Conformational changes in human red cell membrane proteins induced by sugar binding.

A Janoshazi1, G Kifor, A K Solomon

  • 1Biophysical Laboratory, Harvard Medical School, Boston, Massachusetts 02115.

The Journal of Membrane Biology
|September 1, 1991
PubMed
Summary

This study demonstrates bidirectional signaling between the human red cell glucose transport protein and band 3. Maltose binding induces oscillations in tryptophan fluorescence, modulated by DBDS, indicating conformational changes and communication in both directions.

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

Characterization of biological membranes by equivalent pores.

The Journal of general physiology·2009
Same author

Tracer diffusion and unidirectional fluxes.

Biophysical journal·2009
Same author

Abnormal erythrocyte anion exchange in Alzheimer disease.

Archives of pathology & laboratory medicine·2000
Same author

Reversible protein kinase C activation in PC12 cells: effect of NGF treatment.

The European journal of neuroscience·2000
Same author

Rapid in vitro conformational changes of the catalytic site of PKC alpha assessed by FIM-1 fluorescence.

Biochemistry·1999
Same author

Kinetics of chloride-bicarbonate exchange across the human red blood cell membrane.

The Journal of membrane biology·1997

Area of Science:

  • Biochemistry
  • Cell Biology
  • Membrane Transport

Background:

  • Previous work established unidirectional signaling from the glucose transport protein to band 3 in human red blood cells.
  • Band 3 is a crucial anion exchanger, and the glucose transporter facilitates sugar uptake.
  • Understanding inter-protein communication is vital for cellular function.

Purpose of the Study:

  • To investigate if signaling between the glucose transport protein and band 3 occurs in the reverse direction.
  • To characterize conformational changes in the glucose transport protein using tryptophan fluorescence.
  • To elucidate the role of specific disaccharides and inhibitors in this communication.

Main Methods:

  • Utilized tryptophan fluorescence to monitor conformational changes in the glucose transport protein.

Related Experiment Videos

  • Employed cytochalasin B (CB) displacement assays to validate fluorescence attribution.
  • Applied maltose and other disaccharides, along with the band 3 inhibitor DBDS, to probe protein interactions.
  • Analyzed temperature dependence of observed oscillations to determine activation energies.

    • Main Results:

    • Maltose binding induced time-dependent, biphasic enhancement of tryptophan fluorescence, modulated by DBDS.
    • These effects were dependent on disaccharide conformation, suggesting a conformation-sensitive binding site.
    • Long-term experiments revealed sustained damped oscillations in fluorescence upon maltose binding.
    • DBDS significantly increased the damping term activation energy, supporting conformational coupling.

    Conclusions:

    • Evidence strongly supports bidirectional signaling between the glucose transport protein and band 3.
    • Conformational changes in the glucose transport protein are influenced by band 3 interactions.
    • The observed oscillations and DBDS modulation provide a dynamic view of protein-protein communication.