A FINE STRUCTURAL ANALYSIS OF INTERCELLULAR JUNCTIONS IN THE MOUSE LIVER

doi:10.1083/jcb.45.2.272

Quantitative Colocalization Analysis Software

This Article

	Full Text (PDF, 2167K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JCB
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Goodenough, D. A.
	Articles by Revel, J. P.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Goodenough, D. A.
	Articles by Revel, J. P.


Social Bookmarking

	What's this?

ARTICLE

A FINE STRUCTURAL ANALYSIS OF INTERCELLULAR JUNCTIONS IN THE MOUSE LIVER

Daniel A. Goodenough ¹ and Jean Paul Revel ¹

¹ From the Department of Anatomy, Harvard Medical School, Boston, Massachusetts 02115

Zonulae occludentes and gap junctions were examined both inthe intact mouse liver and in a junction-rich membrane fractionfrom homogenized mouse liver. These preparations were visualizedwith the techniques of uranyl acetate staining en bloc, stainingwith colloidal lanthanum, negative staining with phosphotungstate,and freeze-cleaving. The zonula occludens is arranged as a meshworkof branching and anastomosing threadlike contacts sealing thelumen of the bile canaliculus from the liver intercellular space.The gap junction is characterized in section by a 20 A gap betweenthe apposed junctional membrane outer leaflets, and permeationof this space with lanthanum or phosphotungstate reveals a polygonallattice of subunits with a center-to-center spacing of 90–100A. Freeze-cleaved gap junctions show a similar lattice. Extractionof junction-rich fractions with 60% aqueous acetone resultsin a disappearance of the 20 A gap in sectioned pellets andan inability to demonstrate the polygonal lattice with eitherthe freeze-cleave or negative staining techniques. Extractionof the membranes with 50% acetone does not produce this effect.Thin-layer chromatography of the acetone extracts reveals agroup of phospholipids in the 60% extract that are not detectablein the 50% extract. Acetone does not cause any detectable changein the structure of the zonula occludens, but the occludingjunction becomes leaky to lanthanum following acetone treatment.The effects of other reagents on the junctions are reported.

Submitted on September 15, 1969
Revised on November 21, 1969

Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Hou, J., Renigunta, A., Gomes, A. S., Hou, M., Paul, D. L., Waldegger, S., Goodenough, D. A. (2009). Claudin-16 and claudin-19 interaction is required for their assembly into tight junctions and for renal reabsorption of magnesium. Proc. Natl. Acad. Sci. USA 106: 15350-15355 [Abstract] [Full Text]
Franke, W. W. (2009). Discovering the Molecular Components of Intercellular Junctions--A Historical View. Cold Spring Harb. Perspect. Biol. 1: a003061-a003061 [Abstract] [Full Text]
Falk, M. M., Baker, S. M., Gumpert, A. M., Segretain, D., Buckheit, R. W. III (2009). Gap Junction Turnover Is Achieved by the Internalization of Small Endocytic Double-Membrane Vesicles. Mol. Biol. Cell 20: 3342-3352 [Abstract] [Full Text]
Konopka, G., Tekiela, J., Iverson, M., Wells, C., Duncan, S. A. (2007). Junctional Adhesion Molecule-A Is Critical for the Formation of Pseudocanaliculi and Modulates E-cadherin Expression in Hepatic Cells. J. Biol. Chem. 282: 28137-28148 [Abstract] [Full Text]
Krysko, D. V., Mussche, S., Leybaert, L., D'Herde, K. (2004). Gap Junctional Communication and Connexin43 Expression in Relation to Apoptotic Cell Death and Survival of Granulosa Cells. J. Histochem. Cytochem. 52: 1199-1207 [Abstract] [Full Text]
Sasaki, H., Matsui, C., Furuse, K., Mimori-Kiyosue, Y., Furuse, M., Tsukita, S. (2003). Dynamic behavior of paired claudin strands within apposing plasma membranes. Proc. Natl. Acad. Sci. USA 100: 3971-3976 [Abstract] [Full Text]
Lauf, U., Giepmans, B. N. G., Lopez, P., Braconnot, S., Chen, S.-C., Falk, M. M. (2002). Dynamic trafficking and delivery of connexons to the plasma membrane and accretion to gap junctions in living cells. Proc. Natl. Acad. Sci. USA 99: 10446-10451 [Abstract] [Full Text]
Chen, Y.-h., Lu, Q., Schneeberger, E. E., Goodenough, D. A. (2000). Restoration of Tight Junction Structure and Barrier Function by Down-Regulation of the Mitogen-activated Protein Kinase Pathway in Ras-transformed Madin-Darby Canine Kidney Cells. Mol. Biol. Cell 11: 849-862 [Abstract] [Full Text]
Lacaz-Vieira, F. (1997). Calcium Site Specificity: Early Ca2+-related Tight Junction Events. JGP 110: 727-740 [Abstract] [Full Text]
Merzdorf, C., Goodenough, D. (1997). Localization of a novel 210 kDa protein in Xenopus tight junctions. J. Cell Sci. 110: 1005-1012 [Abstract]
Wang, Y, Rose, B (1997). An inhibition of gap-junctional communication by cadherins. J. Cell Sci. 110: 301-309 [Abstract]
Wang, Y., Mehta, P. P., Rose, , B. (1995). Inhibition of Glycosylation Induces Formation of Open Connexin-43 Cell-to-Cell Channels and Phosphorylation and Triton X-100 Insolubility of Connexin-43. J. Biol. Chem. 270: 26581-26585 [Abstract] [Full Text]
Citi, S, Volberg, T, Bershadsky, A., Denisenko, N, Geiger, B (1994). Cytoskeletal involvement in the modulation of cell-cell junctions by the protein kinase inhibitor H-7. J. Cell Sci. 107: 683-692 [Abstract]
Turner, D.F., Marfurt, C.F., Sattelberg, C. (1989). Demonstration of Physiological Barrier Between Pulpal Odontoblasts and its Perturbation Following Routine Restorative Procedures: A Horseradish Peroxidase Tracing Study in the Rat. JDR 68: 1262-1268 [Abstract]
Revel, J.-P., Nicholson, B. J., Yancey, S. B. (1982). Partial Sequence and Turnover of Rat Liver Gap Junction Protein. Cold Spring Harb Symp Quant Biol 46: 633-637 [Abstract]
Kachar, B, Pinto da Silva, P (1981). Rapid massive assembly of tight junction strands. Science 213: 541-544 [Abstract]
Flagg-Newton, J, Simpson, I, Loewenstein, W. (1979). Permeability of the cell-to-cell membrane channels in mammalian cell juncton. Science 205: 404-407 [Abstract]
Goodenough, D. A. (1976). The Structure and Permeability of Isolated Hepatocyte Gap Junctions. Cold Spring Harb Symp Quant Biol 40: 37-43 [Abstract]
Duguid, J. R., Revel, J. P. (1976). The Protein Components of the Gap Junction. Cold Spring Harb Symp Quant Biol 40: 45-47 [Abstract]
Loewenstein, W. R. (1976). Permeable Junctions. Cold Spring Harb Symp Quant Biol 40: 49-63 [Abstract]
Revel, J.-P., Brown, S. S. (1976). Cell Junctions in Development, with Particular Reference to the Neural Tube. Cold Spring Harb Symp Quant Biol 40: 443-455 [Abstract]
Fain, G. L., Gold, G. H., Dowling, J. E. (1976). Receptor Coupling in the Toad Retina. Cold Spring Harb Symp Quant Biol 40: 547-561 [Abstract]
Orci, L., Amherdt, M., Henquin, J. C., Lambert, A. E., Unger, R. H., Renold, A. E. (1973). Pronase Effect on Pancreatic Beta Cell Secretion and Morphology. Science 180: 647-649 [Abstract]
Johnson, R. G., Sheridan, J. D. (1971). Junctions between Cancer Cells in Culture: Ultrastructure and Permeability. Science 174: 717-719 [Abstract]
Bukauskas, F. F., Jordan, K., Bukauskiene, A., Bennett, M. V. L., Lampe, P. D., Laird, D. W., Verselis, V. K. (2000). Clustering of connexin 43-enhanced green fluorescent protein gap junction channels and functional coupling in living cells. Proc. Natl. Acad. Sci. USA 97: 2556-2561 [Abstract] [Full Text]