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 journalArticle

36 Citations (Scopus)

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 - 1983
Externally publishedYes

Fingerprint

Organ Specificity
Connexins
Gap Junctions
Liver
Rats
Tissue
Proteins
Microtomy
High pressure liquid chromatography
Negative Staining
Peptides
Peptide Mapping
Physiology
Electrophoresis
Sodium Dodecyl Sulfate
Trypsin
Electron microscopy
Polyacrylamide Gel Electrophoresis
Digestion
Electron Microscopy

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Medicine(all)

Cite this

Comparative analysis of the gap junction protein from rat heart and liver : Is there a tissue specificity of gap junctions? / Gros, Daniel B.; Nicholson, Bruce J; Revel, Jean Paul.

In: Cell, Vol. 35, No. 2 PART 1, 1983, p. 539-549.

Research output: Contribution to journalArticle

@article{9a0a59a2b2a643f9ab1ff6c2471f4a90,
title = "Comparative analysis of the gap junction protein from rat heart and liver: Is there a tissue specificity of gap junctions?",
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.",
author = "Gros, {Daniel B.} and Nicholson, {Bruce J} and Revel, {Jean Paul}",
year = "1983",
doi = "10.1016/0092-8674(83)90188-5",
language = "English (US)",
volume = "35",
pages = "539--549",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "2 PART 1",

}

TY - JOUR

T1 - Comparative analysis of the gap junction protein from rat heart and liver

T2 - Is there a tissue specificity of gap junctions?

AU - Gros, Daniel B.

AU - Nicholson, Bruce J

AU - Revel, Jean Paul

PY - 1983

Y1 - 1983

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0021080021&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021080021&partnerID=8YFLogxK

U2 - 10.1016/0092-8674(83)90188-5

DO - 10.1016/0092-8674(83)90188-5

M3 - Article

C2 - 6317197

AN - SCOPUS:0021080021

VL - 35

SP - 539

EP - 549

JO - Cell

JF - Cell

SN - 0092-8674

IS - 2 PART 1

ER -