Comparative analysis of the gap junction protein from rat heart and liver: Is there a tissue specificity of gap junctions?

Daniel B. Gros, Bruce J. Nicholson, Jean Paul Revel

Research output: Contribution to journalArticlepeer-review

36 Scopus citations

Abstract

Gap junctions have been isolated from both rat heart and liver, tissues where junctions are typical in appearance and physiology. The purity of the fractions obtained was monitored by electron microscopy (thin-sectioning and negative staining) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The myocardial gap junctions are comprised of a single polypeptide of Mr 28,000, apparently derived from a protein of Mr 30,000. Hepatic gap junctions are also comprised of a single native protein of Mr 28,000 as previously reported. Exhaustive trypsin digestion of the isolated junctions cleaves both of these proteins similarly, while leaving their characteristic junctional lattice structures intact. However, comparison of heart and liver junctional proteins by two-dimensional peptide mapping of tryptic and α-chymotryptic fragments, followed by high pressure liquid chromatography, reveals no homology between these proteins.

Original languageEnglish (US)
Pages (from-to)539-549
Number of pages11
JournalCell
Volume35
Issue number2 PART 1
DOIs
StatePublished - Dec 1983
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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