Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Gap Junctions”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 19 recordsLinked to original sources
PubMed1976

Reflexive gap junctions. Gap junctions between processing arising from the same ovarian decidual cell.

Ajacent processes on ovarian decidual cells were shown by electron microscopy to form gap junctions with one another. Micrographs of tissues preserved with lanthanum included in the fixative confirm the hexagonal array and 2-4 nm gap which characterize gap junctions. It is suggested that these gap junctions may play a role in the process of merocrine secretion from the peduncular processes of ovarian decidual cells. The term reflexive gap junction is introduced to describe gap junctions between adjacent processes from the same cell.

Cytoplasmic Granules↗
PubMed1978

[Structural diversity of communicating intercellular junctions (gap junctions) in the posterior cecal epithelium of the crustacean Orchestis].

Two types of gap junction are described, they are different in the size, the spacing and the polarity of their intramembrane particles. The dense type shows two kinds of particles which rather remain joined to the P fracture face. The loose type shows larger and more spaced out particles which rather are held by the E fracture face. These observations demonstrate that one needs to shade the distinction between P-type gap (Vertebrate) and E-type gap (Arthropoda).

Animals↗
PubMed1995

Changes in gap junction permeability, gap junction number, and connexin43 expression in lindane-treated rat liver epithelial cells.

The pesticide lindane (gamma-hexachlorocyclohexane) is a mammalian neurotoxin and hepatocarcinogen. Lindane can inhibit gap junctional intercellular communication (GJIC) and this effect may contribute to its toxic properties. The mechanism of inhibition of GJIC by lindane in WB-F344 rat liver epithelial cells was studied to determine if altered gap junction permeability, gap junction number, and/or gap junction protein (connexin43) expression were involved. GJIC was monitored by fluorescent Lucifer Yellow CH dye microinjection (dye-coupling). Gap junction number was quantified visually after indirect immunostaining of gap junctions using an anti-connexin43 monoclonal antibody. Connexin43 mRNA and protein levels were determined by Northern and Western blotting, respectively. Short-term treatment (10-30 min) with lindane (50 microM) resulted in the rapid (within 10 min), nearly complete loss of dye-coupling but no changes in gap junction number of connexin43 mRNA or protein levels. Medium-term treatment (1-4 hr) resulted in the loss of dye-coupling, gap junctions, and phosphorylated connexin43 proteins. Long-term treatment (1-14 days) led to reductions in dye-coupling, total connexin43 protein, and connexin43 mRNA. Nuclear run-on assays indicated that transcription of the connexin43 gene was reduced nonspecifically by lindane. These data indicate that reductions in gap junction permeability, number, and expression may be involved in the inhibition of GJIC depending on pesticide treatment duration.

Animals↗
PubMed1987

Chemical synapses, particle arrays, pseudo-gap junctions and gap junctions of neurons and glia in the buccal ganglion of Helisoma.

The nervous system of the snail, Helisoma trivolvis, has been utilized for a wide range of studies of neuronal plasticity; however, the ultrastructural features of this tissue were previously unknown. The present study examined the nature of synaptic interactions of neurons and glia and considered several plasma membrane specializations of these cells. The symmetrical pair of buccal ganglia consisted of a ring of unipolar neurons surrounding a central neuropil. The neurons were separated by two morphologically distinct types of glia: type I were most numerous and possessed an electron-dense homogeneous cytoplasm, whereas type II glia were of lower electron density, possessed a heterogeneous cytoplasm, and appeared to be phagocytic. Gap junctions were abundant between glia and were occasionally found between neuronal processes, including those of neurons 19 injected with horseradish peroxidase (HRP). Comparison of neuron and glial gap junction widths (16.4 and 17.6 nm, respectively) in thin sections and their intramembrane particle diameters (13.1 and 13.7 nm, respectively) by freeze fracture, did not elucidate significant differences. A heterogeneous population of putative chemical synapses, similar to those reported in other molluscs, was also observed between axonal collaterals in the neuropil. Additionally, examination of freeze-fractured neuropil revealed rhombic arrays of particles localized on neuronal membranes; these arrays do not appear to form intercellular junctions but may represent postsynaptic receptor sites. Freeze fracture also revealed small, square arrays consisting of 7-9 nm diameter particles on glial membranes which may correspond to pentalaminar membrane contacts (pseudo-gap junctions) seen in thin sections between glia situated around dilated extracellular spaces (lacunae).

Animals↗
PubMed1985

Structural and functional studies of myometrial gap junctions.

Gap junctions are believed to be sites of metabolic and electrical coupling between cells. These contacts are present between myometrial cells immediately prior to and during parturition. We report the results of studies to investigate the control and the function of myometrial gap junctions. Injection of estradiol (500 micrograms/day) with or without progesterone into immature and ovariectomized mature rats demonstrated that estradiol stimulated whereas progesterone suppressed gap junction formation. Indomethacin treatment was also shown to potentiate the action of estradiol. Also, pregnant rats treated with oestradiol developed numerous myometrial gap junctions and aborted their fetuses. These results suggest that the steroid hormones and prostaglandins may control myometrial gap junction development. Diffusion studies of 3H-2-deoxyglucose in longitudinal myometrial strips revealed a significant increase in the diffusion coefficient in delivering versus ante-partum rat tissues. This indicates that there is increased metabolic transfer during parturition when gap junctions are present. The results of these studies show that steroid hormones and prostaglandins may regulate myometrial gap junctions and that metabolic, as well as electrical coupling, of uterine smooth muscle cells increase at parturition concomitant with the development of gap junctions.

Animals↗
PubMed1995

Functional analysis of amino acid sequences in connexin43 involved in intercellular communication through gap junctions.

Gap junctions allow direct communication between cells without recourse to the extracellular space and have been widely implicated as important mediators of cell-cell signalling. They are constructed from the connexin proteins, which form a large family, and individual connexins show complex spatial and temporal variations in their expression patterns. Understanding how this variation contributes to the control of intercellular signalling, both in the adult and during embryonic development, is an important problem that would be aided by reagents that interfere with gap junctional communication through specific connexins. We have begun to address this issue by raising antibodies to peptides derived from connexin43 and connexin32. Connexin43 peptides were located in the amino terminus, cytoplasmic loop and carboxytail. Connexin32 peptides came from the cytoplasmic loop and the first extracellular loop. Immunoblotting and immunostaining properties of purified IgGs were characterized on mouse heart, liver and the 8- to 16-cell mouse embryo. Effects on transfer through gap junctions were assessed in the fully compacted 8-cell mouse embryo by co-injection with Lucifer Yellow or Cascade Blue. Embryos were maintained in culture to assess the developmental consequences of injection. Peptide competition was used to confirm the specificity of immunostaining and inhibition of dye transfer. All connexin specific antibodies recognized their parent connexin on immunoblots and showed no 43/32 cross-reactivity. The connexin32 extracellular loop antibody recognized both connexin 32 and 43 on immunoblots, as predicted by the amino acid sequence homology in this region, but did not immunostain intact gap junctions. Connexin specific antibodies that immuno-stained showed the predicted connexin specificity. Antibodies to either connexin43 amino acids (AA) 1-16 (amino terminus) or AA 101-112 (cytoplasmic loop) neither immunostained nor prevented functional communication through 8-cell embryo gap junctions. Antibodies to AA 123-136 and AA 131-142 in the cytoplasmic loop immunostained heart and 8-cell embryo gap junctions and blocked transfer through them with high efficiency. Fab' fragments were equally effective. Peptide competition showed that both antibodies contained epitopes within AA 131-136 of connexin43. Antibodies against AA 313-324 in the carboxytail immunostained heart and the 8-cell embryo and, as IgGs, prevented dye transfer. Fab' fragments were ineffective. All connexin43 antibodies that blocked gap junctional communication between cells of the 8-cell mouse embryo induced non-communicating cells subsequently to withdraw from compaction.(ABSTRACT TRUNCATED AT 400 WORDS)

Amino Acid Sequence↗
PubMed1995

Structure--function relationships in gap junctions.

Gap junctions are metabolic and electrotonic pathways between cells and provide direct cooperation within and between cellular nets. They are among the cellular structures most frequently investigated. This chapter primarily addresses aspects of the assembly of the gap junction channel, considering the insertion of the protein into the membrane, the importance of phosphorylation of the gap junction proteins for coupling modulation, and the formation of whole channels from two hemichannels. Interactions of gap junctions with the subplasmalemmal cytoplasm on the one side and with tight junctions on the other side are closely considered. Furthermore, reviewing the significance and alterations of gap junctions during development and oncogenesis, respectively, including the role of adhesion molecules, takes up a major part of the chapter. Finally, the literature on gap junctions in the central nervous system, especially between astrocytes in the brain cortex and horizontal cells in the retina, is summarized and new aspects on their structure-function relationship included.

Animals↗
PubMed1982

Comparative analysis of the major polypeptides from liver gap junctions and lens fiber junctions.

Gap junctions from rat liver and fiber junctions from bovine lens have similar septilaminar profiles when examined by thin-section electron microscopy and differ only slightly with respect to the packing of intramembrane particles in freeze-fracture images. These similarities have often led to lens fiber junctions being referred to as gap junctions. Junctions from both sources were isolated as enriched subcellular fractions and their major polypeptide components compared biochemically and immunochemically. The major liver gap junction polypeptide has an apparent molecular weight of 27,000, while a 25,000-dalton polypeptide is the major component of lens fiber junctions. The two polypeptides are not homologous when compared by partial peptide mapping in SDS. In addition, there is not detectable antigenic similarity between the two polypeptides by immunochemical criteria using antibodies to the 25,000-dalton lens fiber junction polypeptide. Thus, in spite of the ultrastructural similarities, the gap junction and the lens fiber junction are comprised of distinctly different polypeptides, suggesting that the lens fiber junction contains a unique gene product and potentially different physiological properties.

Animals↗
PubMed1987

Topological analysis of the major protein in isolated intact rat liver gap junctions and gap junction-derived single membrane structures.

The topological organization of the major rat liver gap junction protein has been examined in intact gap junctions and gap junction-derived single membrane structures. Two methods, low pH and urea at alkaline pH, were used to "transform" or "split" double membrane gap junctions into single membrane structures. Low pH treatment "transforms" rat liver gap junctions into small single membrane vesicles which have an altered sodium dodecyl sulfate-polyacrylamide gel electrophoresis profile after digestion with L-1-to-sylamido-2-phenylethylchloromethyl ketone-trypsin. Alkaline pH treatment in the presence of 8 M urea can split isolated rat liver gap junctions into single membrane sheets which have no detectable structural alteration or altered sodium dodecyl sulfate-polyacrylamide gel electrophoresis profile after proteolytic digestion, suggesting that these single membrane sheets may be useful for topological studies of the gap junction protein. Proteolytic digestion studies have been used to localize the carboxyl terminus of the molecule on the cytoplasmic surface of the intact gap junction. However, the amino terminus does not appear to be accessible to proteases or to interaction with an antibody that is specific for the amino-terminal region of the molecule in intact or split gap junctions. Binding of antibodies, that block junctional channel conductance, can be eliminated by proteolytic digestion of intact gap junctions, suggesting that all antigenic sites for these antibodies are located on the cytoplasmic surface of the intact gap junction. In addition, calmodulin gel overlays indicate that at least two calmodulin binding sites exist on the cytoplasmic surface of the junctional protein. The information generated from these studies has been used to develop a low resolution two-dimensional model for the organization of the major rat liver gap junctional protein in the junctional membrane.

Amino Acid Sequence↗
PubMed1991

In vitro assembly of gap junctions.

Gap junction structures were assembled in vitro from octyl-beta-D-glucopyranoside-solubilized components of lens fiber cell membranes. Individual pore structures (connexons), short double-membrane structures, and other amorphous material were evident in the solubilized mixture. Following the removal of the detergent by dialysis, these connexons associated to form single- and double-layered, two-dimensional hexagonal arrays (unit cell size a = b = 8.5 nm). The formation of larger arrays was dependent on the lipid-to-protein ratio and the presence of Mg2+ ions. Crystallographic analysis of electron micrographs revealed that lens junctional connexons consisted of six subunits surrounding a stain-filled channel. Upon further detergent treatment, in vitro assembled gap junctions were insoluble and formed three-dimensional stacks while other components were solubilized. SDS-PAGE and mass data from scanning transmission electron microscopy strongly suggest that a 38-kDa polypeptide, which is a processed form of the lens specific gap junction protein MP70, is a major component of the arrays. The in vitro assembly of gap junctions opens new avenues for the structural analysis of gap junctions and for the study of the intermolecular interactions of connexons during junctional assembly.

Animals↗
PubMed1984

Phorbol ester tumor promoter affects the mouse epidermal gap junctions.

Gap junctions are known to mediate cell to cell coupling. This study shows that the potent tumor promoter, 12-O-tetradecanoyl-phorbol-13-acetate (TPA), drastically affects the presence of gap junctions between mouse interfollicular epidermal (IFE) cells. In a time course ultrastructural study after a single application of 1 microgram of TPA the gap junctions between the IFE basal cells begin to decrease by 10 h post-exposure, are totally absent between 18 h and 30 h, and start reappearing at 30 h after TPA application. The potent hyperplasiogen , but very weak tumor promoter, mezerein, produces comparable hyperplasia and wide intercellular spaces but the population of gap junctions remains unchanged.

Animals↗
PubMedDate not supplied

Two homologous protein components of hepatic gap junctions.

Gap junctions consist of closely packed pairs of transmembrane channels, the connexons, through which materials of low relative molecular mass diffuse from the cell to neighbouring cells. In liver, connexons consist of six protein subunits which, until now, were believed to be identical. However, besides the major polypeptide of relative molecular mass (Mr) 28,000 (and see refs 4 and 6), a component of Mr 21,000 (21K) has been repeatedly observed in liver. The amino-terminal sequence (18 residues) of this less abundant protein shows that it is related to, but distinct from, the Mr 28K protein. Immuno-staining and immuno-precipitation show both proteins to be in the same gap junctional plaques. Thus, it seems that hepatic gap junction channels (and by extension possibly others) are composed of two (or more) homologous proteins.

Amino Acid Sequence↗
PubMed1988

Tissue and species conservation of the vertebrate and arthropod forms of the low molecular weight (16-18000) proteins of gap junctions.

Gap junctions have been isolated from four murine tissues, from rat and Xenopus laevis liver, and from Nephrops norvegicus (Norway lobster) hepatopancreas. The preparations of gap junctions from each vertebrate tissue contain a single major protein, Mr 16,000, and those from Nephrops hepatopancreas a protein, Mr 18,000. Immunocytochemical studies using affinity-purified antibodies raised against gap junctions from Nephrops show the junctional origin of the 18k protein. Immunological studies using Western blotting and biochemical studies using tryptic peptide mapping show no significant differences between the 16k junctional proteins of mouse and hence provide no evidence of tissue variation. These studies also suggest that the mouse, rat, and Xenopus 16k proteins and the Nephrops 18k protein share some common structural features.

Animals↗
PubMed1993

Identification of a proline residue as a transduction element involved in voltage gating of gap junctions.

Gap junction channels are structurally distinct from other ion channels in that they comprise two hemichannels which interact head-to-head to form an aqueous channel between cells. Intercellular voltage differences together with increased intracellular concentrations of H+ and Ca2+ cause closure of these normally patent channels. The relative sensitivity to voltage varies with the subunit (connexin) composition of the channels. The third of four transmembrane-spanning regions (M3) in connexins has been proposed to form the channel lining, and a global 'tilting' of the hemichannel subunits has been correlated with channel closure. But specific components involved in transduction of channel gating events have not been identified in either gap junctions or other ion channel classes (however, see model in ref. 5). We have examined a strictly conserved proline centrally located in M2 of connexin proteins. Mutation of this proline (Pro 87) in connexin 26 causes a reversal in the voltage-gating response when the mutant hemichannel is paired with wild-type connexin 26 in the Xenopus oocyte system. This suggests that the unique properties associated with this residue are critical to the transduction of voltage gating in these channels.

Amino Acid Sequence↗
PubMed1988

Organization of connexons in isolated rat liver gap junctions.

Gap junction plaques from rat liver plasma membranes have been subjected to a range of detergent treatments in order to evaluate systematically the influence of different isolation procedures on their structure. The separation of the connexons was found to vary depending on the conditions used. In the absence of detergent the center-to-center separation of the connexons is, on average, approximately 90 A, and they are arranged on a hexagonal lattice so that the symmetry of the double-layered structure approximates to p6m in projection (or p622 in three-dimensions). Exposure to increasing concentration of detergent reduces the connexon separation to values below 80 A. More severe detergent treatment leads to disintegration of the gap junction plaques. Specimens with center-to-center separations smaller than 86 A show progressively larger deviation from p6m symmetry, seen as apparent rotations of the connexon assemblies within the crystal lattice. This reorganization occurs with both ice-embedded and negatively-stained specimens, using ionic or nonionic detergents, and therefore is probably a packing readjustment caused by depletion of intervening lipid molecules.

Animals↗
PubMed1989

Cardiac gap junctions and gap junction-associated vesicles: ultrastructural comparison of in situ negative staining with conventional positive staining.

By comparing in situ negative staining of mammalian heart muscle using La(NO3)3 with conventional positive staining by uranium and lead salts, we showed that 1) the membrane area of rat cardiac gap junctions (GJs) at the intercalated disks is threefold to fourfold greater than previously thought; 2) connexon arrays of cardiac GJ are subdivided into microdomains by connexon-free aisles; 3) profiles of GJ-associated vesicles (GJAVs) of plasmalemmal origin (which are present extracellularly and sharply localized at three extracellular sites) are paired to form GJs with each other and with myocyte plasmalemma; 4) some GJAVs contain arrays of assembled connexons; and 5) myocytes contain intracytoplasmic complexes lying within cylindrical or cigar-shaped membranes and consisting of GJs and multiple vesicles apparently dissociating from these GJs.

Animals↗
PubMed1992

Biophysics of gap junctions.

Gap junction channels, now known to be formed of connexins, connect the interiors of apposed cells. These channels can be opened and closed by various physiological stimuli and experimental treatments. They are permeable to ions and neutral molecules up to a size of about 1 kDa or 1.5 nm diameter, including second messengers and metabolites. The processes of gating and of permeation are the subject of this review. Voltage is a readily applied stimulus, and transjunctional voltages, or those between cytoplasm and exterior, affect most junctions. Single channel transitions between open and closed states are rapid and presumably involve a charge movement as occurs with channels of electrically excitable channels of nerve and muscle. Identification of gating domains and charges by domain replacement and site-directed mutagenesis is being pursued. Raising cytoplasmic H+ or Ca2+ concentrations rapidly reduces junctional conductance, and this action is generally reversible, at least in part. A number of lipophilic alcohols, fatty acids and volatile anesthetics have similar actions. Phosphorylation also modulates junctional conductance, and in several cases, sites of phosphorylation are known. These gating processes appear similar to those induced by voltage. Permeability measurement indicates that the channel is aqueous and that permeation is by diffusion with only minor interactions with the channel wall. Differences among junctions are known, but further characterization of connexin and cell specificity is required.

Animals↗
PubMed1992

Acid phosphatase localization in endocytosed horizontal cell gap junctions.

Gap junction (GJ) endocytosis appears to be part of a cycle of GJ renewal in horizontal cells of the teleost fish retina. At least three stages of GJ endocytosis in these neurons have been identified using conventional electron microscopy (EM): invagination of GJ membranes (GJ blebs); free GJ vesicles; and GJ vesicle fusion with mature lysosomes (Vaughan & Lasater, 1990a). In the present study, EM-level acid phosphatase (AP) histochemistry of white bass retina was used to determine at what stage enzymatic degradation of endocytosed GJs begins. Electron-dense AP reaction product was observed within the trans face of the Golgi apparatus, mature lysosomes, and occasional, internal GJ vesicles. In contrast, GJ blebs, peripheral GJ vesicles, and most internal GJ vesicles lacked AP reaction product. These results support the idea that at least some of the GJ vesicles observed within these retinal neurons arise from endocytosis, are on a degradative pathway, and can be termed GJ "endosomes." Furthermore, GJ vesicles appear to be initially free of AP, but some later acquire it (presumably from transport vesicles bearing degradative enzymes). It is still unclear whether our previous report of GJ vesicle fusion with mature lysosomes is a subsequent step in GJ degradation or part of a different degradative pathway altogether.

Acid Phosphatase↗