Skip to main content
NCBI home page
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1981 Aug 1;90(2):521–526. doi: 10.1083/jcb.90.2.521

Five-hour half-life of mouse liver gap-junction protein

PMCID: PMC2111874  PMID: 7287816

Abstract

The half-life of a gap-junction polypeptide band migrating at 21,000 Mr on SDS polyacrylamide gels isolated from mouse liver is measured to be 5 h. Two low-molecular wight bands, probably related to the 21,000 Mr material by proteolysis, have measured half-lives of 4.6 and 5.2 h. Gap junctions are labeled in vivo using the 14C-bicarbonate labeling procedure, followed by quantitative fluorography.

Full Text

The Full Text of this article is available as a PDF (744.5 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bonner W. M., Laskey R. A. A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem. 1974 Jul 1;46(1):83–88. doi: 10.1111/j.1432-1033.1974.tb03599.x. [DOI] [PubMed] [Google Scholar]
  2. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  3. Dwyer N., Blobel G. A modified procedure for the isolation of a pore complex-lamina fraction from rat liver nuclei. J Cell Biol. 1976 Sep;70(3):581–591. doi: 10.1083/jcb.70.3.581. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Elovson J. Biogenesis of plasma membrane glycoproteins. Tracer kinetic study of two rat liver plasma membrane glycoproteins in vivo. J Biol Chem. 1980 Jun 25;255(12):5816–5825. [PubMed] [Google Scholar]
  5. Epstein M. L., Sheridan J. D., Johnson R. G. Formation of low-resistance junctions in vitro in the absence of protein synthesis and ATP production. Exp Cell Res. 1977 Jan;104(1):25–30. doi: 10.1016/0014-4827(77)90064-7. [DOI] [PubMed] [Google Scholar]
  6. Evans W. H., Gurd J. W. Preparation and properties of nexuses and lipid-enriched vesicles from mouse liver plasma membranes. Biochem J. 1972 Jul;128(3):691–700. doi: 10.1042/bj1280691. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Fairbanks G., Steck T. L., Wallach D. F. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971 Jun 22;10(13):2606–2617. doi: 10.1021/bi00789a030. [DOI] [PubMed] [Google Scholar]
  8. Finbow M., Yancey S. B., Johnson R., Revel J. P. Independent lines of evidence suggesting a major gap junctional protein with a molecular weight of 26,000. Proc Natl Acad Sci U S A. 1980 Feb;77(2):970–974. doi: 10.1073/pnas.77.2.970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Flagg-Newton J., Loewenstein W. R. Experimental depression of junctional membrane permeability in mammalian cell culture. A study with tracer molecules in the 300 to 800 Dalton range. J Membr Biol. 1979 Oct 5;50(1):65–100. doi: 10.1007/BF01868788. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Garlick P. J., Waterlow J. C., Swick R. W. Measurement of protein turnover in rat liver. Analysis of the complex curve for decay of label in a mixture of proteins. Biochem J. 1976 Jun 15;156(3):657–663. doi: 10.1042/bj1560657. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Goldberg A. L., Dice J. F. Intracellular protein degradation in mammalian and bacterial cells. Annu Rev Biochem. 1974;43(0):835–869. doi: 10.1146/annurev.bi.43.070174.004155. [DOI] [PubMed] [Google Scholar]
  12. Goldberg A. L., St John A. C. Intracellular protein degradation in mammalian and bacterial cells: Part 2. Annu Rev Biochem. 1976;45:747–803. doi: 10.1146/annurev.bi.45.070176.003531. [DOI] [PubMed] [Google Scholar]
  13. Goodenough D. A. Bulk isolation of mouse hepatocyte gap junctions. Characterization of the principal protein, connexin. J Cell Biol. 1974 May;61(2):557–563. doi: 10.1083/jcb.61.2.557. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Goodenough D. A. Lens gap junctions: a structural hypothesis for nonregulated low-resistance intercellular pathways. Invest Ophthalmol Vis Sci. 1979 Nov;18(11):1104–1122. [PubMed] [Google Scholar]
  15. Goodenough D. A., Stoeckenius W. The isolation of mouse hepatocyte gap junctions. Preliminary chemical characterization and x-ray diffraction. J Cell Biol. 1972 Sep;54(3):646–656. doi: 10.1083/jcb.54.3.646. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Gurd J. W., Evans W. H. Relative rates of degradation of mouse-liver surface-membrane proteins. Eur J Biochem. 1973 Jul 2;36(1):273–279. doi: 10.1111/j.1432-1033.1973.tb02910.x. [DOI] [PubMed] [Google Scholar]
  17. Harms E., Reutter W. Half-life of N-acetylneuraminic acid in plasma membranes of rat liver and Morris hepatoma 7777. Cancer Res. 1974 Dec;34(12):3165–3172. [PubMed] [Google Scholar]
  18. Henderson D., Eibl H., Weber K. Structure and biochemistry of mouse hepatic gap junctions. J Mol Biol. 1979 Aug 5;132(2):193–218. doi: 10.1016/0022-2836(79)90391-7. [DOI] [PubMed] [Google Scholar]
  19. Hertzberg E. L., Gilula N. B. Isolation and characterization of gap junctions from rat liver. J Biol Chem. 1979 Mar 25;254(6):2138–2147. [PubMed] [Google Scholar]
  20. Ito S., Sato E., Loewenstein W. R. Studies on the formation of a permeable cell membrane junction. I. Coupling under various conditions of membrane contact. Effects of colchicine, cytochalasin B, dinitrophenol. J Membr Biol. 1974;19(4):305–337. doi: 10.1007/BF01869984. [DOI] [PubMed] [Google Scholar]
  21. Johnson R., Hammer M., Sheridan J., Revel J. P. Gap junction formation between reaggregated Novikoff hepatoma cells. Proc Natl Acad Sci U S A. 1974 Nov;71(11):4536–4540. doi: 10.1073/pnas.71.11.4536. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Kensler R. W., Goodenough D. A. Isolation of mouse myocardial gap junctions. J Cell Biol. 1980 Sep;86(3):755–764. doi: 10.1083/jcb.86.3.755. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Kreisel W., Volk B. A., Büchsel R., Reutter W. Different half-lives of the carbohydrate and protein moieties of a 110,000-dalton glycoprotein isolated from plasma membranes of rat liver. Proc Natl Acad Sci U S A. 1980 Apr;77(4):1828–1831. doi: 10.1073/pnas.77.4.1828. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  25. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  26. Laskey R. A., Mills A. D. Quantitative film detection of 3H and 14C in polyacrylamide gels by fluorography. Eur J Biochem. 1975 Aug 15;56(2):335–341. doi: 10.1111/j.1432-1033.1975.tb02238.x. [DOI] [PubMed] [Google Scholar]
  27. Loewenstein W. R., Kanno Y., Socolar S. J. Quantum jumps of conductance during formation of membrane channels at cell-cell junction. Nature. 1978 Jul 13;274(5667):133–136. doi: 10.1038/274133a0. [DOI] [PubMed] [Google Scholar]
  28. Makowski L., Caspar D. L., Phillips W. C., Goodenough D. A. Gap junction structures. II. Analysis of the x-ray diffraction data. J Cell Biol. 1977 Aug;74(2):629–645. doi: 10.1083/jcb.74.2.629. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. ORNSTEIN L. DISC ELECTROPHORESIS. I. BACKGROUND AND THEORY. Ann N Y Acad Sci. 1964 Dec 28;121:321–349. doi: 10.1111/j.1749-6632.1964.tb14207.x. [DOI] [PubMed] [Google Scholar]
  30. Rose B., Loewenstein W. R. Permeability of cell junction depends on local cytoplasmic calcium activity. Nature. 1975 Mar 20;254(5497):250–252. doi: 10.1038/254250a0. [DOI] [PubMed] [Google Scholar]
  31. Scornik O. A., Botbol V. Role of changes in protein degradation in the growth of regenerating livers. J Biol Chem. 1976 May 25;251(10):2891–2897. [PubMed] [Google Scholar]
  32. Swick R. W., Ip M. M. Measurement of protein turnover in rat liver with (14C)carbonate. Protein turnover during liver regeneration. J Biol Chem. 1974 Nov 10;249(21):6836–6841. [PubMed] [Google Scholar]
  33. Tanabe T., Pricer W. E., Jr, Ashwell G. Subcellular membrane topology and turnover of a rat hepatic binding protein specific for asialoglycoproteins. J Biol Chem. 1979 Feb 25;254(4):1038–1043. [PubMed] [Google Scholar]
  34. Turin L., Warner A. E. Intracellular pH in early Xenopus embryos: its effect on current flow between blastomeres. J Physiol. 1980 Mar;300:489–504. doi: 10.1113/jphysiol.1980.sp013174. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Turin L., Warner A. Carbon dioxide reversibly abolishes ionic communication between cells of early amphibian embryo. Nature. 1977 Nov 3;270(5632):56–57. doi: 10.1038/270056a0. [DOI] [PubMed] [Google Scholar]
  36. Unwin P. N., Zampighi G. Structure of the junction between communicating cells. Nature. 1980 Feb 7;283(5747):545–549. doi: 10.1038/283545a0. [DOI] [PubMed] [Google Scholar]
  37. Wong M. M., Robertson N. P., Horwitz J. Heat induced aggregation of the sodium dodecyl sulfate-solubilized main intrinsic polypeptide isolated from bovine lens plasma membrane. Biochem Biophys Res Commun. 1978 Sep 14;84(1):158–165. doi: 10.1016/0006-291x(78)90277-2. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES