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1

Boitano, Scott, Zeenat Safdar, Donald G. Welsh, Jahar Bhattacharya, and Michael Koval. "Cell-cell interactions in regulating lung function." American Journal of Physiology-Lung Cellular and Molecular Physiology 287, no. 3 (2004): L455—L459. http://dx.doi.org/10.1152/ajplung.00172.2004.

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Tight junction barrier formation and gap junctional communication are two functions directly attributable to cell-cell contact sites. Epithelial and endothelial tight junctions are critical elements of the permeability barrier required to maintain discrete compartments in the lung. On the other hand, gap junctions enable a tissue to act as a cohesive unit by permitting metabolic coupling and enabling the direct transmission of small cytosolic signaling molecules from one cell to another. These components do not act in isolation since other junctional elements, such as adherens junctions, help
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2

Churchill, D., S. Coodin, R. R. Shivers, and S. Caveney. "Rapid de novo formation of gap junctions between insect hemocytes in vitro: a freeze-fracture, dye- transfer and patch-clamp study." Journal of Cell Science 104, no. 3 (1993): 763–72. http://dx.doi.org/10.1242/jcs.104.3.763.

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Gap junctions form between insect hemocytes (blood cells) when they encapsulate foreign objects in the hemocoel (body cavity). In this study we show that hemocytes from cockroach (Periplaneta americana) form gap-junctions rapidly in vitro. Freeze-fracture replicas of hemocyte aggregates fixed 5 minutes after bleeding contain gap-junctional plaques. Dye passage was detected between carboxyfluorescein diacetate- labelled and unlabelled hemocytes within 3 minutes of bleeding, when the cells made contact as they flattened rapidly onto coverslips. When double whole-cell voltage-clamp was used to me
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3

Scemes, Eliana, Sylvia O. Suadicani, Gerhard Dahl, and David C. Spray. "Connexin and pannexin mediated cell–cell communication." Neuron Glia Biology 3, no. 3 (2007): 199–208. http://dx.doi.org/10.1017/s1740925x08000069.

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AbstractIn this review, we briefly summarize what is known about the properties of the three families of gap junction proteins, connexins, innexins and pannexins, emphasizing their importance as intercellular channels that provide ionic and metabolic coupling and as non-junctional channels that can function as a paracrine signaling pathway. We discuss that two distinct groups of proteins form gap junctions in deuterostomes (connexins) and protostomes (innexins), and that channels formed of the deuterostome homologues of innexins (pannexins) differ from connexin channels in terms of important s
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4

Fujimoto, K., A. Nagafuchi, S. Tsukita, A. Kuraoka, A. Ohokuma, and Y. Shibata. "Dynamics of connexins, E-cadherin and alpha-catenin on cell membranes during gap junction formation." Journal of Cell Science 110, no. 3 (1997): 311–22. http://dx.doi.org/10.1242/jcs.110.3.311.

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We examined the dynamics of connexins, E-cadherin and alpha-catenin during gap-junction disassembly and assembly in regeneration hepatocytes by immunofluorescence microscopy, and immunogold-electron microscopy using SDS-digested freeze-replicas. The present findings suggest that during the disappearance of gap junctions most of the gap junction plaques are broken up into smaller aggregates, and then the gap junction proteins may be removed from the cell membrane, but some of the connexons or connexins remain dispersed in the plane of membrane as pure morphologically indistinguishable intramemb
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5

Lo, W. K., and T. S. Reese. "Multiple structural types of gap junctions in mouse lens." Journal of Cell Science 106, no. 1 (1993): 227–35. http://dx.doi.org/10.1242/jcs.106.1.227.

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Gap junctions in the epithelium and superficial fiber cells from young mice were examined in lenses prepared by rapid-freezing, and processed for freeze-substitution and freeze-fracture electron microscopy. There appeared to be three structural types of gap junction: one type between epithelial cells and two types between fiber cells. Epithelial gap junctions seen by freeze-substitution were approximately 20 nm thick and consistently associated with layers of dense material lying along both cytoplasmic surfaces. Fiber gap junctions, in contrast, were 15–16 nm (type 1) or 17–18 nm thick (type 2
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6

Musil, L. S., B. A. Cunningham, G. M. Edelman, and D. A. Goodenough. "Differential phosphorylation of the gap junction protein connexin43 in junctional communication-competent and -deficient cell lines." Journal of Cell Biology 111, no. 5 (1990): 2077–88. http://dx.doi.org/10.1083/jcb.111.5.2077.

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Connexin43 is a member of the highly homologous connexin family of gap junction proteins. We have studied how connexin monomers are assembled into functional gap junction plaques by examining the biosynthesis of connexin43 in cell types that differ greatly in their ability to form functional gap junctions. Using a combination of metabolic radiolabeling and immunoprecipitation, we have shown that connexin43 is synthesized in gap junctional communication-competent cells as a 42-kD protein that is efficiently converted to a approximately 46-kD species (connexin43-P2) by the posttranslational addi
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7

Ek-Vitorín, Jose F., and Janis M. Burt. "Quantification of gap junction selectivity." American Journal of Physiology-Cell Physiology 289, no. 6 (2005): C1535—C1546. http://dx.doi.org/10.1152/ajpcell.00182.2005.

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Gap junctions, which are essential for functional coordination and homeostasis within tissues, permit the direct intercellular exchange of small molecules. The abundance and diversity of this exchange depends on the number and selectivity of the comprising channels and on the transjunctional gradient for and chemical character of the permeant molecules. Limited knowledge of functionally significant permeants and poor detectability of those few that are known have made it difficult to define channel selectivity. Presented herein is a multifaceted approach to the quantification of gap junction s
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8

Rook, M. B., A. C. van Ginneken, B. de Jonge, A. el Aoumari, D. Gros, and H. J. Jongsma. "Differences in gap junction channels between cardiac myocytes, fibroblasts, and heterologous pairs." American Journal of Physiology-Cell Physiology 263, no. 5 (1992): C959—C977. http://dx.doi.org/10.1152/ajpcell.1992.263.5.c959.

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Cultures of neonatal rat heart cells contain predominantly myocytes and fibroblastic cells. Most abundant are groups of synchronously contracting myocytes, which are electrically well coupled through large gap junctions. Cardiac fibroblasts may be electrically coupled to each other and to adjacent myocytes, be it with low intercellular conductances. Nevertheless, synchronously beating myocytes interconnected via a fibroblast were present, demonstrating that nonexcitable cardiac cells are capable of passive impulse conduction. In fibroblast pairs as well as in myocyte-fibroblast cell pairs, no
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9

Koval, Michael. "Sharing signals: connecting lung epithelial cells with gap junction channels." American Journal of Physiology-Lung Cellular and Molecular Physiology 283, no. 5 (2002): L875—L893. http://dx.doi.org/10.1152/ajplung.00078.2002.

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Gap junction channels enable the direct flow of signaling molecules and metabolites between cells. Alveolar epithelial cells show great variability in the expression of gap junction proteins (connexins) as a function of cell phenotype and cell state. Differential connexin expression and control by alveolar epithelial cells have the potential to enable these cells to regulate the extent of intercellular coupling in response to cell stress and to regulate surfactant secretion. However, defining the precise signals transmitted through gap junction channels and the cross talk between gap junctions
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10

Zampighi, G., M. Kreman, F. Ramón, A. L. Moreno, and S. A. Simon. "Structural characteristics of gap junctions. I. Channel number in coupled and uncoupled conditions." Journal of Cell Biology 106, no. 5 (1988): 1667–78. http://dx.doi.org/10.1083/jcb.106.5.1667.

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Gap junctions between crayfish lateral axons were studied by combining anatomical and electrophysiological measurements to determine structural changes associated during uncoupling by axoplasmic acidification. In basal conditions, the junctional resistance, Rj, was approximately 60-80 k omega and the synapses appeared as two adhering membranes; 18-20-nm overall thickness, containing transverse densities (channels) spanning both membranes and the narrow extracellular gap (4-6 nm). In freeze-fracture replicas, the synapses contained greater than 3 X 10(3) gap junction plaques having a total of a
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11

Becker, David L., Catherine Leclerc-David, and Anne Warner. "The relationship of gap junctions and compaction in the preimplantation mouse embryo." Development 116, Supplement (1992): 113–18. http://dx.doi.org/10.1242/dev.116.supplement.113.

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In the mouse embryo, gap junctions first appear at the 8-cell stage as compaction is about to take place. Compaction of the embryo is important for the differentiation of the first two cell types; the inner cell mass and the trophectoderm. Our studies examine the contribution of gap junctional communication at this stage of development We have characterised the normal sequence of appearance of gap junction protein and its distribution. The extent of communication as shown by the passage of dye between cells has been recorded in both normal embryos and embryos treated with drugs that influence
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12

Jordan, K., R. Chodock, A. R. Hand, and D. W. Laird. "The origin of annular junctions: a mechanism of gap junction internalization." Journal of Cell Science 114, no. 4 (2001): 763–73. http://dx.doi.org/10.1242/jcs.114.4.763.

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Gap junctional intercellular communication is established when connexin proteins oligomerize into connexon hemichannels, which then pair at the cell surface with connexons from neighboring cells to form functional gap junction channels. Gap junction channels routinely cluster into gap junction plaques, which can exhibit dynamic characteristics while under the frequent processes of formation and removal from the cell surface. We have three lines of evidence to suggest that one mechanism of gap junction removal occurs when one of two contacting cells internalizes the gap junction contribution fr
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13

Postma, Friso R., Trudi Hengeveld, Jacqueline Alblas, et al. "Acute loss of Cell–Cell Communication Caused by G Protein–coupled Receptors: A Critical Role for c-Src." Journal of Cell Biology 140, no. 5 (1998): 1199–209. http://dx.doi.org/10.1083/jcb.140.5.1199.

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Gap junctions mediate cell–cell communication in almost all tissues, but little is known about their regulation by physiological stimuli. Using a novel single-electrode technique, together with dye coupling studies, we show that in cells expressing gap junction protein connexin43, cell–cell communication is rapidly disrupted by G protein–coupled receptor agonists, notably lysophosphatidic acid, thrombin, and neuropeptides. In the continuous presence of agonist, junctional communication fully recovers within 1–2 h of receptor stimulation. In contrast, a desensitization-defective G protein–coupl
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14

Cao, D., G. Lin, E. M. Westphale, E. C. Beyer, and T. H. Steinberg. "Mechanisms for the coordination of intercellular calcium signaling in insulin-secreting cells." Journal of Cell Science 110, no. 4 (1997): 497–504. http://dx.doi.org/10.1242/jcs.110.4.497.

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Insulin-mediated increases in cytosolic calcium are synchronized among the cells in a pancreatic islet, and result in pulsatile secretion of insulin. Pancreatic beta cells express the gap junction protein connexin43 and are functionally coupled, making gap junctional communication a likely mechanism for the synchronization of calcium transients among islet cells. To define the mechanism by which pancreatic islet cells coordinate calcium responses, we studied mechanically-induced intercellular calcium waves in the communication-deficient rat insulinoma cell line RINm5f, and in RINm5f cells tran
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15

Ko, Kevin, Pamela Arora, Wilson Lee, and Christopher McCulloch. "Biochemical and functional characterization of intercellular adhesion and gap junctions in fibroblasts." American Journal of Physiology-Cell Physiology 279, no. 1 (2000): C147—C157. http://dx.doi.org/10.1152/ajpcell.2000.279.1.c147.

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Despite their significance in wound healing, little is known about the molecular determinants of cell-to-cell adhesion and gap junctional communication in fibroblasts. We characterized intercellular adherens junctions and gap junctions in human gingival fibroblasts (HGFs) using a novel model. Calcein-labeled donor cells in suspension were added onto an established, Texas red dextran (10 kDa)-labeled acceptor cell monolayer. Cell-to-cell adhesion required Ca2+ and was >30-fold stronger than cell-to-fibronectin adhesion at 15 min. Electron micrographs showed rapid formation of adherens juncti
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16

Meyer, R. A., D. W. Laird, J. P. Revel, and R. G. Johnson. "Inhibition of gap junction and adherens junction assembly by connexin and A-CAM antibodies." Journal of Cell Biology 119, no. 1 (1992): 179–89. http://dx.doi.org/10.1083/jcb.119.1.179.

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We examined the roles of the extracellular domains of a gap junction protein and a cell adhesion molecule in gap junction and adherens junction formation by altering cell interactions with antibody Fab fragments. Using immunoblotting and immunocytochemistry we demonstrated that Novikoff cells contained the gap junction protein, connexin43 (Cx43), and the cell adhesion molecule, A-CAM (N-cadherin). Cells were dissociated in EDTA, allowed to recover, and reaggregated for 60 min in media containing Fab fragments prepared from a number of antibodies. We observed no cell-cell dye transfer 4 min aft
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17

Beyer, E. C., J. Kistler, D. L. Paul, and D. A. Goodenough. "Antisera directed against connexin43 peptides react with a 43-kD protein localized to gap junctions in myocardium and other tissues." Journal of Cell Biology 108, no. 2 (1989): 595–605. http://dx.doi.org/10.1083/jcb.108.2.595.

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Rat heart and other organs contain mRNA coding for connexin43, a polypeptide homologous to a gap junction protein from liver (connexin32). To provide direct evidence that connexin43 is a cardiac gap junction protein, we raised rabbit antisera directed against synthetic oligopeptides corresponding to two unique regions of its sequence, amino acids 119-142 and 252-271. Both antisera stained the intercalated disc in myocardium by immunofluorescence but did not react with frozen sections of liver. Immunocytochemistry showed anti-connexin43 staining of the cytoplasmic surface of gap junctions in is
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18

Breznau, Elaina B., Ansley C. Semack, Tomohito Higashi, and Ann L. Miller. "MgcRacGAP restricts active RhoA at the cytokinetic furrow and both RhoA and Rac1 at cell–cell junctions in epithelial cells." Molecular Biology of the Cell 26, no. 13 (2015): 2439–55. http://dx.doi.org/10.1091/mbc.e14-11-1553.

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Localized activation of Rho GTPases is essential for multiple cellular functions, including cytokinesis and formation and maintenance of cell–cell junctions. Although MgcRacGAP (Mgc) is required for spatially confined RhoA-GTP at the equatorial cortex of dividing cells, both the target specificity of Mgc's GAP activity and the involvement of phosphorylation of Mgc at Ser-386 are controversial. In addition, Mgc's function at cell–cell junctions remains unclear. Here, using gastrula-stage Xenopus laevis embryos as a model system, we examine Mgc's role in regulating localized RhoA-GTP and Rac1-GT
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19

Le, Anh-Chi N., and Linda S. Musil. "A novel role for FGF and extracellular signal–regulated kinase in gap junction–mediated intercellular communication in the lens." Journal of Cell Biology 154, no. 1 (2001): 197–216. http://dx.doi.org/10.1083/jcb.200101057.

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Gap junction–mediated intercellular coupling is higher in the equatorial region of the lens than at either pole, a property believed to be essential for lens transparency. We show that fibroblast growth factor (FGF) upregulates gap junctional intercellular dye transfer in primary cultures of embryonic chick lens cells without detectably increasing either gap junction protein (connexin) synthesis or assembly. Insulin and insulin-like growth factor 1, as potent as FGF in inducing lens cell differentiation, had no effect on gap junctions. FGF induced sustained activation of extracellular signal–r
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20

Lee, Y. C., C. E. Yellowley, Z. Li, H. J. Donahue, and D. E. Rannels. "Expression of functional gap junctions in cultured pulmonary alveolar epithelial cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 272, no. 6 (1997): L1105—L1114. http://dx.doi.org/10.1152/ajplung.1997.272.6.l1105.

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Recent observations suggest that cell-cell interactions may modulate the response of the alveolar epithelium to injury. Expression and function of gap junctions were thus evaluated in isolated alveolar type II cells. Freshly isolated (day 0) type II cells expressed mRNAs for gap junctional connexins 26, 32, and 43. Whereas connexin 26 mRNA declined approximately 40% in cultured cells, connexin 32 message decreased rapidly and was not detectable on day 1. In contrast, connexin 43 expression increased 10-fold by day 3 compared with day 0. Western blot confirmed a 30-fold elevation in connexin 43
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21

Imanaga, I., M. Kameyama, and H. Irisawa. "Cell-to-cell diffusion of fluorescent dyes in paired ventricular cells." American Journal of Physiology-Heart and Circulatory Physiology 252, no. 1 (1987): H223—H232. http://dx.doi.org/10.1152/ajpheart.1987.252.1.h223.

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The intracellular and cell-to-cell diffusion of fluorescent dyes of various molecular sizes were studied in enzymatically isolated paired ventricular cells of the guinea pig heart. Fluorescein sodium (mol wt 332), 6-carboxyfluorescein (mol wt 376), Lucifer yellow CH (mol wt 457), lissamine rhodamine B-200 (mol wt 559), and tetraglycine-conjugated lissamine rhodamine B-200 (mol wt 859) were all diffused into the single ventricular cell through the patch-clamp pipette. All these dyes were able to diffuse through the gap junction of the paired cells. The diffusion coefficient of 6-carboxyfluoresc
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22

Jørgensen, Niklas R., Steven T. Geist, Roberto Civitelli, and Thomas H. Steinberg. "ATP- and Gap Junction–dependent Intercellular Calcium Signaling in Osteoblastic Cells." Journal of Cell Biology 139, no. 2 (1997): 497–506. http://dx.doi.org/10.1083/jcb.139.2.497.

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Many cells coordinate their activities by transmitting rises in intracellular calcium from cell to cell. In nonexcitable cells, there are currently two models for intercellular calcium wave propagation, both of which involve release of inositol trisphosphate (IP3)- sensitive intracellular calcium stores. In one model, IP3 traverses gap junctions and initiates the release of intracellular calcium stores in neighboring cells. Alternatively, calcium waves may be mediated not by gap junctional communication, but rather by autocrine activity of secreted ATP on P2 purinergic receptors. We studied me
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23

Dhein, Stefan, and Aida Salameh. "Remodeling of Cardiac Gap Junctional Cell–Cell Coupling." Cells 10, no. 9 (2021): 2422. http://dx.doi.org/10.3390/cells10092422.

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The heart works as a functional syncytium, which is realized via cell-cell coupling maintained by gap junction channels. These channels connect two adjacent cells, so that action potentials can be transferred. Each cell contributes a hexameric hemichannel (=connexon), formed by protein subuntis named connexins. These hemichannels dock to each other and form the gap junction channel. This channel works as a low ohmic resistor also allowing the passage of small molecules up to 1000 Dalton. Connexins are a protein family comprising of 21 isoforms in humans. In the heart, the main isoforms are Cx4
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24

Reed, Anamika M., Thomas Kolodecik, Sohail Z. Husain, and Fred S. Gorelick. "Low pH enhances connexin32 degradation in the pancreatic acinar cell." American Journal of Physiology-Gastrointestinal and Liver Physiology 307, no. 1 (2014): G24—G32. http://dx.doi.org/10.1152/ajpgi.00010.2014.

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Decreased extracellular pH is observed in a number of clinical conditions and can sensitize to the development and worsen the severity of acute pancreatitis. Because intercellular communication through gap junctions is pH-sensitive and modulates pancreatitis responses, we evaluated the effects of low pH on gap junctions in the rat pancreatic acinar cell. Decreasing extracellular pH from 7.4 to 7.0 significantly inhibited gap junctional intracellular communication. Acidic pH also significantly reduced levels of connexin32, the predominant gap junction protein in acinar cells, and altered its lo
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25

Sosinsky, Gina E. "Diversity in gap junction structures." Proceedings, annual meeting, Electron Microscopy Society of America 50, no. 1 (1992): 442–43. http://dx.doi.org/10.1017/s0424820100122617.

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Gap junctions are the specialized regions between two adjoining cells responsible for regulated communication. The morphological unit of the gap junction is composed of 12 copies of the connexin molecule. Six connexins form a hexamer in each cell membrane called a connexon and two connexons pair across the two cell membranes of coupled cells to form gated channels. Although other proteins are found in enriched gap junction preparations, it is generally accepted that the gap junction structures are formed from a family of connexin proteins. The connexins are named according to their DNA deduced
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26

Spray, D. C., M. Chanson, A. P. Moreno, R. Dermietzel, and P. Meda. "Distinctive gap junction channel types connect WB cells, a clonal cell line derived from rat liver." American Journal of Physiology-Cell Physiology 260, no. 3 (1991): C513—C527. http://dx.doi.org/10.1152/ajpcell.1991.260.3.c513.

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Gap junctions, dye coupling, and junctional conductance were studied in a cell line (WB) that is derived from rat liver and displays a phenotype similar to “oval” cells. In freeze-fracture replicas, two distinctive particle sizes were detected in gap junctional plaques. Immunocytochemical studies indicated punctate staining at membrane appositions using antibodies to connexin 43 and to a brain gap junction-associated antigen (34 kDa). No staining was observed using antibodies prepared against rat liver gap junction proteins (connexins 32 and 26). Pairs of WB cells were electrically and dye cou
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27

Zhou, Cheng-Jie, Sha-Na Wu, Jiang-Peng Shen, et al. "The beneficial effects of cumulus cells and oocyte-cumulus cell gap junctions depends on oocyte maturation and fertilization methods in mice." PeerJ 4 (March 3, 2016): e1761. http://dx.doi.org/10.7717/peerj.1761.

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Cumulus cells are a group of closely associated granulosa cells that surround and nourish oocytes. Previous studies have shown that cumulus cells contribute to oocyte maturation and fertilization through gap junction communication. However, it is not known how this gap junction signaling affectsin vivoversusin vitromaturation of oocytes, and their subsequent fertilization and embryonic development following insemination. Therefore, in our study, we performed mouse oocyte maturation and insemination usingin vivo- orin vitro-matured oocyte-cumulus complexes (OCCs, which retain gap junctions betw
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28

Lampe, P. D. "Analyzing phorbol ester effects on gap junctional communication: a dramatic inhibition of assembly." Journal of Cell Biology 127, no. 6 (1994): 1895–905. http://dx.doi.org/10.1083/jcb.127.6.1895.

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The effect of 12-O-tetradeconylphorbol-13-acetate (TPA) on gap junction assembly between Novikoff hepatoma cells was examined. Cells were dissociated with EDTA to single cells and then reaggregated to form new junctions. When TPA (25 nM) was added to the cells at the onset of the 60-min reaggregation, dye transfer was detected at only 0.6% of the cell-cell interfaces compared to 72% for the untreated control and 74% for 4-alpha TPA, an inactive isomer of TPA. Freeze-fracture electron microscopy of reaggregated control cells showed interfaces containing an average of more than 600 aggregated in
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29

Mazet, F., I. Dunia, G. Vassort, and J. L. Mazet. "Ultrastructural changes in gap junctions associated with CO2 uncoupling in frog atrial fibres." Journal of Cell Science 74, no. 1 (1985): 51–63. http://dx.doi.org/10.1242/jcs.74.1.51.

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The correlation between gap junction morphology and the state of electrical coupling was investigated in the frog auricle, which presents an atypical gap-junction organization. Electrical uncoupling of the tissue was achieved by perfusion with CO2-saturated Ringer medium. The tissue was fixed with glutaraldehyde and freeze-fractured before and during the application of CO2-saturated Ringer medium and after returning to the initial medium. The electrical tissue coupling was assayed by microelectrode recording just before fixation. At least 97% uncoupling was induced by CO2-saturated Ringer medi
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30

PITTS, J. D., and M. E. FINBOW. "The Gap Junction." Journal of Cell Science 1986, Supplement 4 (1986): 239–66. http://dx.doi.org/10.1242/jcs.1986.supplement_4.15.

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31

Warner, A. "The gap junction." Journal of Cell Science 89, no. 1 (1988): 1–7. http://dx.doi.org/10.1242/jcs.89.1.1.

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32

Moore, L. K., E. C. Beyer, and J. M. Burt. "Characterization of gap junction channels in A7r5 vascular smooth muscle cells." American Journal of Physiology-Cell Physiology 260, no. 5 (1991): C975—C981. http://dx.doi.org/10.1152/ajpcell.1991.260.5.c975.

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Recent evidence suggest that coordination of blood flow in the microcirculation involves cell-to-cell coupling via gap junctions. In this study, using A7r5 cells as a model of vascular smooth muscle, we have characterized the gap junctions in terms of the unitary conductances of the observed channels, the responses to second messengers, and subunit protein composition. The cells were typically well coupled several hours after plating, with junctional conductances on the order 20-40 nS. Channels with mean conductances of 36 and 89 pS were observed in low-conductance cell pairs and in cell pairs
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33

Kurjiaka, David T., Timothy D. Steele, Mary V. Olsen, and Janis M. Burt. "Gap junction permeability is diminished in proliferating vascular smooth muscle cells." American Journal of Physiology-Cell Physiology 275, no. 6 (1998): C1674—C1682. http://dx.doi.org/10.1152/ajpcell.1998.275.6.c1674.

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In atherosclerosis and hypertension, vascular smooth muscle cells (SMCs) are stimulated to proliferate and exhibit enhanced gap junction protein expression. Our goal was to determine whether gap junction function differs in proliferating vs. growth-arrested SMCs. A7r5 cells (embryonic rat aortic SMCs) did not proliferate in media with reduced serum (∼90% of cells in G0/G1phase after 48–96 h in 1% fetal bovine serum). Dye coupling was less but electrical coupling was comparable in proliferating vs. growth-arrested A7r5 cells, suggesting differences in junctional permselectivity. In growth-arres
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34

Miller, T. M., and D. A. Goodenough. "Gap junction structures after experimental alteration of junctional channel conductance." Journal of Cell Biology 101, no. 5 (1985): 1741–48. http://dx.doi.org/10.1083/jcb.101.5.1741.

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Gap junctions are known to present a variety of different morphologies in electron micrographs and x-ray diffraction patterns. This variation in structure is not only seen between gap junctions in different tissues and organisms, but also within a given tissue. In an attempt to understand the physiological meaning of some aspects of this variability, gap junction structure was studied following experimental manipulation of junctional channel conductance. Both physiological and morphological experiments were performed on gap junctions joining stage 20-23 chick embryo lens epithelial cells. Chan
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35

de Rivero Vaccari, Juan Carlos, Roderick A. Corriveau, and Andrei B. Belousov. "Gap Junctions Are Required for NMDA Receptor–Dependent Cell Death in Developing Neurons." Journal of Neurophysiology 98, no. 5 (2007): 2878–86. http://dx.doi.org/10.1152/jn.00362.2007.

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A number of studies have indicated an important role for N-methyl-d-aspartate (NMDA) receptors in cell survival versus cell death decisions during neuronal development, trauma, and ischemia. Coupling of neurons by electrical synapses (gap junctions) is high or increases in neuronal networks during all three of these conditions. However, whether neuronal gap junctions contribute to NMDA receptor–regulated cell death is not known. Here we address the role of neuronal gap junction coupling in NMDA receptor–regulated cell death in developing neurons. We report that inactivation or hyperactivation
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36

Stains, Joseph P., and Roberto Civitelli. "Gap Junctions Regulate Extracellular Signal-regulated Kinase Signaling to Affect Gene Transcription." Molecular Biology of the Cell 16, no. 1 (2005): 64–72. http://dx.doi.org/10.1091/mbc.e04-04-0339.

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Osteoblasts are highly coupled by gap junctions formed by connexin43. Overexpression of connexin45 in osteoblasts results in decreased chemical and electrical coupling and reduces gene transcription from connexin response elements (CxREs) in the osteocalcin and collagen Iα1 promoters. Here, we demonstrate that transcription from the gap junction-dependent osteocalcin CxRE is regulated by extracellular signal-regulated protein kinase (ERK) and phosphatidylinositol 3-kinase (PI3K) cascades. Overexpression of a constitutively active mitogen-activated protein kinase kinase (MEK), Raf, or Ras can i
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37

ZAHS, KATHLEEN R., and PAUL W. CEELEN. "Gap junctional coupling and connexin immunoreactivity in rabbit retinal glia." Visual Neuroscience 23, no. 1 (2006): 1–10. http://dx.doi.org/10.1017/s0952523806231018.

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Gap junctions provide a pathway for the direct intercellular exchange of ions and small signaling molecules. Gap junctional coupling between retinal astrocytes and between astrocytes and Müller cells, the principal glia of vertebrate retinas, has been previously demonstrated by the intercellular transfer of gap-junction permeant tracers. However, functional gap junctions have yet to be demonstrated between mammalian Müller cells. In the present study, when the gap-junction permeant tracers Neurobiotin and Lucifer yellow were injected into a Müller cellviaa patch pipette, the tracers transferre
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38

Jeong, S.-H., M.-H. Cho, and J.-H. Cho. "Effects of cadmium on gap junctional intercellular communication in WB-F344 rat liver epithelial cells." Human & Experimental Toxicology 20, no. 11 (2001): 577–83. http://dx.doi.org/10.1191/096032701718620855.

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Cadmium has been associated with a number of tumors but its role in tumor promotion has not been elucidated clearly or the results obtained from various studies have been conflicting. This study was designed to investigate the effects of cadmium on the gap junctional intercellular communication (GJIC), number of gap junctions per cell, and cell proliferation in WB-F344 rat liver epithelial cells from the viewpoint of tumor promotion. GJIC was monitored by counting the cells stained with Lucifer yellow CH dye, using the scrape-loading and dye-transfer method. The numbers of gap junctions per ce
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39

Wolf, Klaus V. "Light and Electron Microscopic Studies Regarding Cell Contractility and Cell Coupling in Light Sensitive Smooth Muscle Cells from the Isolated Frog Iris Sphincter." Zeitschrift für Naturforschung C 42, no. 7-8 (1987): 977–85. http://dx.doi.org/10.1515/znc-1987-7-842.

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(1) In light microscopical studies of living isolated frog irises, it was found that the maximal areas of experimentally light induced contractions in the m. sphincter pupillae were located beneath small illuminated regions. There were no visible contractions of muscle cells outside the illuminated areas. It was shown that exposure to light could directly cause contractions of isolated single sphincter muscle cells. (2) Junctional structures of the iris sphincter cells were studied by means of thin sections and freeze fracture electron microscopy. Intermediate junctions, a few focal tight junc
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40

Solan, Joell L., and Paul D. Lampe. "Connexin43 phosphorylation: structural changes and biological effects." Biochemical Journal 419, no. 2 (2009): 261–72. http://dx.doi.org/10.1042/bj20082319.

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Vertebrate gap junctions, composed of proteins from the connexin gene family, play critical roles in embryonic development, co-ordinated contraction of excitable cells, tissue homoeostasis, normal cell growth and differentiation. Phosphorylation of connexin43, the most abundant and ubiquitously expressed connexin, has been implicated in the regulation of gap junctional communication at several stages of the connexin ‘life cycle’, including hemichannel oligomerization, export of the protein to the plasma membrane, hemichannel activity, gap junction assembly, gap junction channel gating and conn
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41

Harfst, E., N. J. Severs, and C. R. Green. "Cardiac myocyte gap junctions: evidence for a major connexon protein with an apparent relative molecular mass of 70,000." Journal of Cell Science 96, no. 4 (1990): 591–604. http://dx.doi.org/10.1242/jcs.96.4.591.

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It is widely accepted that there is a family of gap junction connexon proteins, their distribution appearing to vary with tissue type and species. In cardiac tissues the major junctional channel component identified is a 43K (K = 10(3) Mr) polypeptide. Using a gap junction isolation protocol in which low temperatures are maintained, and which is detergent-free, we have identified a second gap junction-related protein in cardiac tissues with an apparent relative molecular mass of 70,000. Antibodies raised to three synthetic peptides matching portions of the 43K gap junction protein cDNA sequenc
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42

Kumar, N. M., D. S. Friend, and N. B. Gilula. "Synthesis and assembly of human beta 1 gap junctions in BHK cells by DNA transfection with the human beta 1 cDNA." Journal of Cell Science 108, no. 12 (1995): 3725–34. http://dx.doi.org/10.1242/jcs.108.12.3725.

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Gap junctional communication is important in many physiological processes, including growth control, patterning, and the synchronization of cell-to-cell activities. It has been difficult to study the synthesis and assembly of gap junctions due to their low abundance. To overcome this limitation, baby hamster kidney cells (BHK) have been transfected with a human beta 1 (Cx32) connexin cDNA construct. Expression was placed under the control of the mouse metallothionein promoter that can be induced by heavy metals. The transfected cells were characterized by DNA, RNA and protein analysis, as well
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43

Sosinsky, Gina, Maryann Martone, Galen Handel, Linda Musil, and Mark Ellisman. "Correlative Confocal and Electron Microscopy of the Connexin43 Gap Junction Protein in NRK Cells: Balancing Fixation Conditions, Cell Permeabilization, Antigen-Antibody Interaction and Cell Ultrastructure." Microscopy and Microanalysis 4, S2 (1998): 450–51. http://dx.doi.org/10.1017/s1431927600022376.

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Synthesis and assembly of gap junction proteins into intercellular channels is an important biological problem with direct bearing on embryonic development. In particular, transgenic mice Cx43 gap junction protein knock-outs 1 and mutations in Cx43 sequence in human Viscera Hyper Taxia patients result in severely deformed hearts.NRK cells are one of the best studied systems for gap junction synthesis, transport and assembly. Gap junctions contain numerous cell-cell channels which are composed of two paired oligomers (called a connexon or hemichannel) each contributed from the plasma membrane o
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Zervos, A. S., J. Hope, and W. H. Evans. "Preparation of a gap junction fraction from uteri of pregnant rats: the 28-kD polypeptides of uterus, liver, and heart gap junctions are homologous." Journal of Cell Biology 101, no. 4 (1985): 1363–70. http://dx.doi.org/10.1083/jcb.101.4.1363.

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A procedure for the preparation of a gap junction fraction from the uteri of pregnant rats is described. The uterine gap junctions, when examined by electron microscopy of thin sections and in negatively stained preparations, were similar to gap junctions isolated from heart and liver. Major proteins of similar apparent molecular weight (Mr 28,000) were found in gap junction fractions isolated from the uterus, heart, and liver, and were shown to have highly homologous structures by two-dimensional mapping of their tryptic peptides. An Mr 10,000 polypeptide, previously deduced to be a proteolyt
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Valdimarsson, G., and G. M. Kidder. "Temporal control of gap junction assembly in preimplantation mouse embryos." Journal of Cell Science 108, no. 4 (1995): 1715–22. http://dx.doi.org/10.1242/jcs.108.4.1715.

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The de novo assembly of gap junctions during compaction in the 8-cell stage of mouse development is a temporally regulated event. We have performed experiments designed to explore the relationship between this event and DNA replication in the second, third, and fourth cell cycles after fertilization. Inhibition of DNA synthesis by continuous treatment with the DNA synthesis inhibitor, aphidicolin, during the third and fourth cell cycles had no effect on the establishment of gap junctional coupling during compaction. However, a delay of 10 hours in DNA synthesis during the second cell cycle cau
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46

Bell, Cheryl, Teresa Shakespeare, Amber Smith, and Sandra Murray. "Visualization of Annular Gap Junction Vesicle Processing: The Interplay Between Annular Gap Junctions and Mitochondria." International Journal of Molecular Sciences 20, no. 1 (2018): 44. http://dx.doi.org/10.3390/ijms20010044.

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It is becoming clear that in addition to gap junctions playing a role in cell–cell communication, gap junction proteins (connexins) located in cytoplasmic compartments may have other important functions. Mitochondrial connexin 43 (Cx43) is increased after ischemic preconditioning and has been suggested to play a protective role in the heart. How Cx43 traffics to the mitochondria and the interactions of mitochondria with other Cx43-containing structures are unclear. In this study, immunocytochemical, super-resolution, and transmission electron microscopy were used to detect cytoplasmic Cx43-con
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Mitra, Shalini, Lakshmanan Annamalai, Souvik Chakraborty, et al. "Androgen-regulated Formation and Degradation of Gap Junctions in Androgen-responsive Human Prostate Cancer Cells." Molecular Biology of the Cell 17, no. 12 (2006): 5400–5416. http://dx.doi.org/10.1091/mbc.e06-04-0280.

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The constituent proteins of gap junctions, called connexins (Cxs), have a short half-life. Despite this, the physiological stimuli that control the assembly of Cxs into gap junctions and their degradation have remained poorly understood. We show here that in androgen-responsive human prostate cancer cells, androgens control the expression level of Cx32—and hence the extent of gap junction formation—post-translationally. In the absence of androgens, a major fraction of Cx32 is degraded presumably by endoplasmic reticulum–associated degradation, whereas in their presence, this fraction is rescue
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48

Shah, US, and SA Murray. "Bimodal inhibition of connexin 43 gap junctions decreases ACTH-induced steroidogenesis and increases bovine adrenal cell population growth." Journal of Endocrinology 171, no. 1 (2001): 199–208. http://dx.doi.org/10.1677/joe.0.1710199.

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In order to elucidate the role of gap junctions in adrenal cell responses, we measured the effect of inhibiting gap junctions with 18-alpha glycerrhetinic acid (GA; a potent inhibitor of cell-cell communication) and connexin antisense transfection on cell proliferation and adrenocorticotropin (ACTH)-stimulated steroidogenesis. In these experiments we utilized a bovine adrenocortical cell (SBAC) population, which responds to ACTH treatment with a dose-dependent increase in steroid production, an increase in connexin 43 (alpha(1)-Cx43) gap junction protein concentrations, and a decrease in cell
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49

VanSlyke, Judy K., and Linda S. Musil. "Cytosolic Stress Reduces Degradation of Connexin43 Internalized from the Cell Surface and Enhances Gap Junction Formation and Function." Molecular Biology of the Cell 16, no. 11 (2005): 5247–57. http://dx.doi.org/10.1091/mbc.e05-05-0415.

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The protein constituents of gap junctions, connexins, have a rapid basal rate of degradation even after transport to the cell surface. We have used cell surface biotinylation to label gap junction-unassembled plasma membrane pools of connexin43 (Cx43) and show that their degradation is inhibited by mild hyperthermia, oxidative stress, and proteasome inhibitors. Cytosolic stress does not perturb endocytosis of biotinylated Cx43, but instead it seems to interfere with its targeting and/or transport to the lysosome, possibly by increasing the level of unfolded protein in the cytosol. This allows
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50

Banerjee, Debarshi. "Connexin’s Connection in Breast Cancer Growth and Progression." International Journal of Cell Biology 2016 (2016): 1–11. http://dx.doi.org/10.1155/2016/9025905.

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Gap junctions are cell-to-cell junctions that are located in the basolateral surface of two adjoining cells. A gap junction channel is composed of a family of proteins called connexins. Gap junction channels maintain intercellular communication between two cells through the exchange of ions, small metabolites, and electrical signals. Gap junction channels or connexins are widespread in terms of their expression and function in maintaining the development, differentiation, and homeostasis of vertebrate tissues. Gap junction connexins play a major role in maintaining intercellular communication
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