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Rat liver gap junction protein: properties and partial sequence.

B J Nicholson, M W Hunkapiller, L B Grim

    Proceedings of the National Academy of Sciences of the United States of America
    |December 1, 1981
    PubMed
    Summary
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    Researchers isolated rat liver gap junctions, revealing a primary Mr 28,000 protein. Sequencing identified its NH2-terminus, clarifying its structure and origin from proteolytic cleavage or aggregation.

    Area of Science:

    • Cell biology
    • Biochemistry
    • Molecular biology

    Background:

    • Gap junctions facilitate direct cell-to-cell communication.
    • Previous studies implicated gap junctions in cellular signaling.

    Purpose of the Study:

    • To isolate and characterize gap junction proteins from rat liver.
    • To determine the primary structure of the main gap junction polypeptide.

    Main Methods:

    • Isolation of gap junctions from rat liver.
    • Sodium dodecyl sulfate/polyacrylamide gel electrophoresis (SDS-PAGE).
    • Two-dimensional peptide mapping.
    • Amino acid sequencing of the NH2-terminus.

    Main Results:

    • High yield and purity of rat liver gap junctions were achieved.

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  • SDS-PAGE revealed multiple polypeptides, with a predominant Mr 28,000 protein.
  • Two-dimensional peptide mapping indicated most polypeptides derive from the Mr 28,000 protein.
  • The NH2-terminal sequence of 52 amino acids of the Mr 28,000 protein was determined.
  • A 10,000 Mr polypeptide in trypsin-treated preparations consists of two distinct peptides derived from the Mr 28,000 protein.

    • Conclusions:

    • The primary structural unit of rat liver gap junctions is a Mr 28,000 protein.
    • The NH2-terminal sequence provides insights into the protein's structure and function.
    • Understanding gap junction protein composition is crucial for cell communication research.