The structure and permeability of isolated hepatocyte gap junctions. 1976

D A Goodenough

The ultrastructure of the gap junction may be visualized in both in situ and isolated preparations by using a variety of electron microscope techniques. The junction is composed of a lattice of subunits, called connexons, which show variable degrees of packing into a hexagonal lattice depending on a variety of poorly understood conditions. In general, it appears that more uncoupled and "dead" the junction, the more regular and condensed the hexagonal lattice becomes. It is not yet known whether these are "postmortem" changes or physiologically active and reversible changes involved in regulation of junctional permeability. Using a variety of techniques, it can be seen that the connexon extends completely across the junctional membranes, from the cytoplasmic surface of one cell to the cytoplasmic surface of the other, spanning the 2-nm "gap" between the apposed junctional membranes. Thus it is possible to implicate the connexon as a permeability channel from cytoplasm to cytoplasm, although the hydrophilic pore through the center of the connexon has not yet been demonstrated to span the full junction thickness. X-ray diffraction experiments support these conclusions, and the excellent correlation between the electron microscope and X-ray diffraction data lends great confidence to the interpretations of gap junction structure presented thus far. These data are summarized in the drawing in Figure 17. This is a scale drawing of two connexons, each of which is imagined to be composed of a dimer of hexamers. It must be emphasized that as yet there is no direct evidence for a sixfold symmetry within the connexon. Of special interest now are the types of protein-protein interactions that hold the two halves of the connexon together across the 2-nm gap and the lateral interactions between the connexons at the level of the lipid bilayers.

UI MeSH Term Description Entries
D007365 Intercellular Junctions Direct contact of a cell with a neighboring cell. Most such junctions are too small to be resolved by light microscopy, but they can be visualized by conventional or freeze-fracture electron microscopy, both of which show that the interacting CELL MEMBRANE and often the underlying CYTOPLASM and the intervening EXTRACELLULAR SPACE are highly specialized in these regions. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p792) Cell Junctions,Cell Junction,Intercellular Junction,Junction, Cell,Junction, Intercellular,Junctions, Cell,Junctions, Intercellular
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D010539 Permeability Property of membranes and other structures to permit passage of light, heat, gases, liquids, metabolites, and mineral ions. Permeabilities
D002458 Cell Fractionation Techniques to partition various components of the cell into SUBCELLULAR FRACTIONS. Cell Fractionations,Fractionation, Cell,Fractionations, Cell
D003012 Microbial Collagenase A metalloproteinase which degrades helical regions of native collagen to small fragments. Preferred cleavage is -Gly in the sequence -Pro-Xaa-Gly-Pro-. Six forms (or 2 classes) have been isolated from Clostridium histolyticum that are immunologically cross-reactive but possess different sequences and different specificities. Other variants have been isolated from Bacillus cereus, Empedobacter collagenolyticum, Pseudomonas marinoglutinosa, and species of Vibrio and Streptomyces. EC 3.4.24.3. Clostridiopeptidase A,Clostridium histolyticum Collagenase,Collagenase, Microbial,Collagenase Clostridium histolyticum,Collagenase-Like Peptidase,Collalysine,Nucleolysin,Clostridium histolyticum, Collagenase,Collagenase Like Peptidase,Collagenase, Clostridium histolyticum,Peptidase, Collagenase-Like,histolyticum, Collagenase Clostridium
D006735 Horseradish Peroxidase An enzyme isolated from horseradish which is able to act as an antigen. It is frequently used as a histochemical tracer for light and electron microscopy. Its antigenicity has permitted its use as a combined antigen and marker in experimental immunology. Alpha-Peroxidase,Ferrihorseradish Peroxidase,Horseradish Peroxidase II,Horseradish Peroxidase III,Alpha Peroxidase,II, Horseradish Peroxidase,III, Horseradish Peroxidase,Peroxidase II, Horseradish,Peroxidase III, Horseradish,Peroxidase, Ferrihorseradish,Peroxidase, Horseradish
D006821 Hyaluronoglucosaminidase An enzyme that catalyzes the random hydrolysis of 1,4-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate. (From Enzyme Nomenclature, 1992) There has been use as ANTINEOPLASTIC AGENTS to limit NEOPLASM METASTASIS. Hyaluronidase,Duran-Reynals Permeability Factor,GL Enzyme,Hyaglosidase,Hyaluronate Hydrolase,Wydase,Duran Reynals Permeability Factor,Factor, Duran-Reynals Permeability,Hydrolase, Hyaluronate,Permeability Factor, Duran-Reynals
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D014357 Trypsin A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4. Tripcellim,Trypure,beta-Trypsin,beta Trypsin
D014961 X-Ray Diffraction The scattering of x-rays by matter, especially crystals, with accompanying variation in intensity due to interference effects. Analysis of the crystal structure of materials is performed by passing x-rays through them and registering the diffraction image of the rays (CRYSTALLOGRAPHY, X-RAY). (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Xray Diffraction,Diffraction, X-Ray,Diffraction, Xray,Diffractions, X-Ray,Diffractions, Xray,X Ray Diffraction,X-Ray Diffractions,Xray Diffractions

Related Publications

D A Goodenough
June 1981, European journal of cell biology,
D A Goodenough
June 1977, FEBS letters,
D A Goodenough
December 1979, Journal of molecular biology,
D A Goodenough
November 2007, The Journal of investigative dermatology,
D A Goodenough
January 2002, Molecular membrane biology,
D A Goodenough
January 1995, International review of cytology,
D A Goodenough
January 1988, BioEssays : news and reviews in molecular, cellular and developmental biology,
D A Goodenough
July 1980, Journal of ultrastructure research,
Copied contents to your clipboard!