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Related Experiment Videos

Rat heart gap junctions as disulfide-bonded connexon multimers: their depolymerization and solubilization in

C K Manjunath, E Page

    The Journal of Membrane Biology
    |January 1, 1986
    PubMed
    Summary

    Rat heart gap junctions have disulfide bonds linking connexons, unlike liver junctions. This difference in quaternary organization affects their structural stability and detergent solubility.

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    Area of Science:

    • Biochemistry
    • Cell Biology
    • Structural Biology

    Background:

    • Gap junctions are protein channels crucial for intercellular communication.
    • Cardiac and liver gap junctions exhibit distinct structural and functional properties.
    • The role of disulfide bonds in gap junction quaternary structure is not fully understood.

    Purpose of the Study:

    • To investigate the presence and role of inter-subunit disulfide bonds in rat heart and liver gap junctions.
    • To compare the quaternary organization of cardiac and hepatic gap junctions.
    • To determine the impact of disulfide bonds on gap junction stability and detergent solubility.

    Main Methods:

    • Isolation of unproteolyzed and proteolyzed gap junctions from rat heart and liver.
    • Analysis using sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE).

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  • Assessment of detergent (deoxycholate) solubility before and after disulfide bond reduction (beta-mercaptoethanol treatment).

    • Main Results:

    • Rat cardiac gap junctions contain multiple inter-subunit disulfide bonds connecting Mr 47,000 connexon subunits.
    • Inter-subunit disulfide bonds are absent in rat liver gap junctions.
    • Disulfide bonds in cardiac gap junctions confer resistance to deoxycholate, which is lost upon reduction.
    • Proteolyzed cardiac junctions show disulfide bonding limited to Mr 29,500 subunits and remain insoluble in deoxycholate.

    Conclusions:

    • Heart and liver gap junctions exhibit significant differences in their quaternary organization due to the presence or absence of inter-subunit disulfide bonds.
    • Disulfide bonds play a critical role in stabilizing the quaternary structure of cardiac gap junctions, influencing their interaction with detergents.
    • These findings highlight distinct structural strategies employed by cardiac and hepatic gap junctions for their respective functions.