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

Molecular organization of gap junctions.

J P Revel, B J Nicholson, S B Yancey

    Federation Proceedings
    |September 1, 1984
    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

    Site-directed mutagenesis reveals putative regions of protein interaction within the transmembrane domains of connexins.

    Cell communication & adhesion·2008
    Same author

    Connexin expression and cell coupling fail to reverse the v-src transformed growth characteristics of a Cx43-/- cell line.

    Cell communication & adhesion·2005
    Same author

    Aberrant gating, but a normal expression pattern, underlies the recessive phenotype of the deafness mutant Connexin26M34T.

    FASEB journal : official publication of the Federation of American Societies for Experimental Biology·2004
    Same author

    Mutagenic approaches to modifying gap junction phenotype.

    Current drug targets·2002
    Same author

    Identification of amino acid residues lining the pore of a gap junction channel.

    The Journal of cell biology·2002
    Same author

    Application of SCAM (substituted cysteine accessibility method) to gap junction intercellular channels.

    Cell communication & adhesion·2002

    Gap junction proteins from heart and liver share similarities, despite differences in other rat tissues. This research clarifies the structural relationships of gap junction proteins across species and organs.

    Area of Science:

    • Cellular Biology
    • Molecular Biology
    • Biochemistry

    Background:

    • Gap junctions are essential for intercellular communication.
    • The protein composition of gap junctions can vary between tissues and species.
    • Understanding gap junction protein structure is key to deciphering their function.

    Purpose of the Study:

    • To investigate the structural homology of gap junction proteins.
    • To compare gap junction proteins from different organs (heart, liver, lens) and species.
    • To identify conserved regions and variations in gap junction protein sequences.

    Main Methods:

    • Protein purification from heart and liver tissues.
    • Peptide mapping to assess protein homology.
    • Partial protein sequencing to analyze amino acid sequences.

    Related Experiment Videos

  • Comparison of proteins from different species and rat tissues.
  • Main Results:

    • Purified gap junction fractions from heart and liver revealed a single major protein (26,000-30,000 Da).
    • Hepatic gap junction proteins showed homology across different species via peptide mapping.
    • Peptide mapping detected no homology between different rat tissues.
    • Partial sequencing indicated related amino-terminal regions between liver and heart proteins.
    • No homology was found between lens and other junction proteins via sequencing.

    Conclusions:

    • Gap junction proteins exhibit species-specific conservation, particularly in the liver.
    • Significant structural divergence exists between gap junction proteins in different rat tissues.
    • The amino-terminal regions of liver and heart gap junction proteins share some homology.
    • Further research is needed to fully elucidate the relationships between lens and other gap junction proteins.