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Journal articles on the topic 'Connexin-36'

Author: Grafiati

Published: 4 June 2021

Last updated: 13 February 2022

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1

SITARAMAYYA, ARI, JOHN W. CRABB, DIANE F. MATESIC, ALEXANDER MARGULIS, VINITA SINGH, SADHONA PULUKURI, and LOAN DANG. "Connexin 36 in bovine retina: Lack of phosphorylation but evidence for association with phosphorylated proteins." Visual Neuroscience 20, no. 4 (July 2003): 385–95. http://dx.doi.org/10.1017/s0952523803204041.

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In vertebrate retina interneuronal communication through gap junctions is involved in light adaptation and in the transfer of visual information from the rod pathway to the cone pathway. Reports over the last two decades have indicated that these gap junctions are regulated by cyclic nucleotide-dependent protein kinases suggesting that the gap junction proteins, connexins, are phosphorylated. Though all the connexins involved in light adaptation and information transfer from rod to cone pathway are not yet known, connexin 36 has been shown to be definitively involved in the latter process. We have therefore attempted to investigate the cyclic nucleotide-dependent phosphorylation of this connexin in bovine retina. We found several soluble and membrane proteins in bovine retina whose phosphorylation was regulated by cyclic nucleotides. However, no protein of about 36 kDa with cyclic nucleotide-regulated phosphorylation was found in gap junction-enriched membrane preparations. A 36-kDa phosphorylated protein was found in gap junction-enriched membranes phosphorylated in the presence of calcium. However, this protein was not immunoprecipitated by anti-connexin 36 antibodies indicating that it was not connexin 36 in spite of its similarity in molecular weight. Immunoprecipitation did reveal phosphorylated proteins coimmunoprecipitated with connexin 36. Two of these proteins were identified as beta and alpha tubulin subunits. Though cyclic GMP and calcium did not greatly influence the association of these proteins with connexin 36, the results suggest the possibility of connexin 36 associating with other proteins. Together, these observations indicate that interneuronal communication at gap junctions made by connexin 36 may not be regulated by direct phosphorylation of connexin 36, but possibly by phosphorylation of associated proteins.

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2

Alonso, Angelika, Eileen Reinz, Jürgen W. Jenne, Marc Fatar, Hannah Schmidt-Glenewinkel, Michael G. Hennerici, and Stephen Meairs. "Reorganization of Gap Junctions after Focused Ultrasound Blood–Brain Barrier Opening in the Rat Brain." Journal of Cerebral Blood Flow & Metabolism 30, no. 7 (March 24, 2010): 1394–402. http://dx.doi.org/10.1038/jcbfm.2010.41.

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Ultrasound-induced opening of the blood–brain barrier (BBB) is an emerging technique for targeted drug delivery to the central nervous system. Gap junctions allow transfer of information between adjacent cells and are responsible for tissue homeostasis. We examined the effect of ultrasound-induced BBB opening on the structure of gap junctions in cortical neurons, expressing Connexin 36, and astrocytes, expressing Connexin 43, after focused 1-MHz ultrasound exposure at 1.25 MPa of one hemisphere together with intravenous microbubble (Optison, Oslo, Norway) application. Quantification of immunofluorescence signals revealed that, compared with noninsonicated hemispheres, small-sized Connexin 43 and 36 gap-junctional plaques were markedly reduced in areas with BBB breakdown after 3 to 6 hours (34.02±6.04% versus 66.49±2.16%, P=0.02 for Connexin 43; 33.80±1.24% versus 36.77±3.43%, P=0.07 for Connexin 36). Complementing this finding, we found significant increases in large-sized gap-junctional plaques (5.76±0.96% versus 1.02±0.84%, P=0.05 for Connexin 43; 5.62±0.22% versus 4.65±0.80%, P=0.02 for Connexin 36). This effect was reversible at 24 hours after ultrasound exposure. Western blot analyses did not show any change in the total connexin amount. These results indicate that ultrasound-induced BBB opening leads to a reorganization of gap-junctional plaques in both neurons and astrocytes. The plaque-size increase may be a cellular response to imbalances in extracellular homeostasis after BBB leakage.

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3

Song, Ji-Hoon, Yongfu Wang, Joseph D. Fontes, and Andrei B. Belousov. "Regulation of connexin 36 expression during development." Neuroscience Letters 513, no. 1 (March 2012): 17–19. http://dx.doi.org/10.1016/j.neulet.2012.01.075.

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4

Gonzalez-Nieto, D., J. M. Gomez-Hernandez, B. Larrosa, C. Gutierrez, M. D. Munoz, I. Fasciani, J. O'Brien, A. Zappala, F. Cicirata, and L. C. Barrio. "Regulation of neuronal connexin-36 channels by pH." Proceedings of the National Academy of Sciences 105, no. 44 (October 28, 2008): 17169–74. http://dx.doi.org/10.1073/pnas.0804189105.

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5

Barrio, Luis C., Daniel González-Nieto, Juan Gómez-Hernández, Bélen Larrosa, Cristina Gutièrrez, Ilaria Fasciani, María D. Muñoz, John O'Brien, Agata Zappala, and Federico Cicirata. "Regulation Of Neuronal Connexin-36 Channels by pH." Biophysical Journal 96, no. 3 (February 2009): 285a. http://dx.doi.org/10.1016/j.bpj.2008.12.1412.

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6

Nevin, Remington L. "Mefloquine Blockade of Connexin 36 and Connexin 43 Gap Junctions and Risk of Suicide." Biological Psychiatry 71, no. 1 (January 2012): e1-e2. http://dx.doi.org/10.1016/j.biopsych.2011.07.026.

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7

Mills, Stephen L., Jennifer J. O'Brien, Wei Li, John O'Brien, and Stephen C. Massey. "Rod pathways in the mammalian retina use connexin 36." Journal of Comparative Neurology 436, no. 3 (2001): 336–50. http://dx.doi.org/10.1002/cne.1071.

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8

Bargiotas, Panagiotis, Sajjad Muhammad, Mahbubur Rahman, Nurith Jakob, Raimund Trabold, Elke Fuchs, Lothar Schilling, Nikolaus Plesnila, Hannah Monyer, and Markus Schwaninger. "Connexin 36 promotes cortical spreading depolarization and ischemic brain damage." Brain Research 1479 (October 2012): 80–85. http://dx.doi.org/10.1016/j.brainres.2012.08.046.

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9

Le Gurun, Sabine, David Martin, Andrea Formenton, Pierre Maechler, Dorothée Caille, Gérard Waeber, Paolo Meda, and Jacques-Antoine Haefliger. "Connexin-36 Contributes to Control Function of Insulin-producing Cells." Journal of Biological Chemistry 278, no. 39 (May 22, 2003): 37690–97. http://dx.doi.org/10.1074/jbc.m212382200.

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10

Hartfield, Elizabeth M., Federica Rinaldi, Colin P. Glover, Liang-Fong Wong, Maeve A. Caldwell, and James B. Uney. "Connexin 36 Expression Regulates Neuronal Differentiation from Neural Progenitor Cells." PLoS ONE 6, no. 3 (March 9, 2011): e14746. http://dx.doi.org/10.1371/journal.pone.0014746.

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11

Pérez-Armendariz, E. Martha. "Connexin 36, a key element in pancreatic beta cell function." Neuropharmacology 75 (December 2013): 557–66. http://dx.doi.org/10.1016/j.neuropharm.2013.08.015.

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12

Short, Kurt W., W. Steve Head, and David W. Piston. "Connexin 36 mediates blood cell flow in mouse pancreatic islets." American Journal of Physiology-Endocrinology and Metabolism 306, no. 3 (February 1, 2014): E324—E331. http://dx.doi.org/10.1152/ajpendo.00523.2013.

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The insulin-secreting β-cells are contained within islets of Langerhans, which are highly vascularized. Blood cell flow rates through islets are glucose-dependent, even though there are no changes in blood cell flow within in the surrounding exocrine pancreas. This suggests a specific mechanism of glucose-regulated blood flow in the islet. Pancreatic islets respond to elevated glucose with synchronous pulses of electrical activity and insulin secretion across all β-cells in the islet. Connexin 36 (Cx36) gap junctions between islet β-cells mediate this synchronization, which is lost in Cx36 knockout mice (Cx36−/−). This leads to glucose intolerance in these mice, despite normal plasma insulin levels and insulin sensitivity. Thus, we sought to investigate whether the glucose-dependent changes in intraislet blood cell flow are also dependent on coordinated pulsatile electrical activity. We visualized and quantified blood cell flow using high-speed in vivo fluorescence imaging of labeled red blood cells and plasma. With the use of a live animal glucose clamp, blood cell flow was measured during either hypoglycemia (∼50 mg/dl) or hyperglycemia (∼300 mg/dl). In contrast to the large glucose-dependent islet blood velocity changes observed in wild-type mice, only minimal differences are observed in both Cx36+/− and Cx36−/− mice. This observation supports a novel model where intraislet blood cell flow is regulated by the coordinated electrical activity in the islet β-cells. Because Cx36 expression and function is reduced in type 2 diabetes, the resulting defect in intraislet blood cell flow regulation may also play a significant role in diabetic pathology.

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13

Li, Qian, Tian-Le Ma, You-Qi Qiu, Wen-Qiang Cui, Teng Chen, Wen-Wen Zhang, Jing Wang, et al. "Connexin 36 Mediates Orofacial Pain Hypersensitivity Through GluK2 and TRPA1." Neuroscience Bulletin 36, no. 12 (October 16, 2020): 1484–99. http://dx.doi.org/10.1007/s12264-020-00594-4.

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14

Frank, M., B. Eiberger, U. Janssen-Bienhold, L. P. de Sevilla Muller, A. Tjarks, J. S. Kim, S. Maschke, et al. "Neuronal connexin-36 can functionally replace connexin-45 in mouse retina but not in the developing heart." Journal of Cell Science 123, no. 20 (October 7, 2010): 3605–15. http://dx.doi.org/10.1242/jcs.068668.

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15

Rash, J. E., W. A. Staines, T. Yasumura, D. Patel, C. S. Furman, G. L. Stelmack, and J. I. Nagy. "Immunogold evidence that neuronal gap junctions in adult rat brain and spinal cord contain connexin-36 but not connexin-32 or connexin-43." Proceedings of the National Academy of Sciences 97, no. 13 (June 20, 2000): 7573–78. http://dx.doi.org/10.1073/pnas.97.13.7573.

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16

KOTHMANN, W. WADE, XIAOFAN LI, GARY S. BURR, and JOHN O'BRIEN. "Connexin 35/36 is phosphorylated at regulatory sites in the retina." Visual Neuroscience 24, no. 3 (May 2007): 363–75. http://dx.doi.org/10.1017/s095252380707037x.

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Connexin 35/36 is the most widespread neuronal gap junction protein in the retina and central nervous system. Electrical and/or tracer coupling in a number of neuronal circuits that express this connexin are regulated by light adaptation. In many cases, the regulation of coupling depends on signaling pathways that activate protein kinases such as PKA, and Cx35 has been shown to be regulated by PKA phosphorylation in cell culture systems. To examine whether phosphorylation might regulate Cx35/36 in the retina we developed phospho-specific polyclonal antibodies against the two regulatory phosphorylation sites of Cx35 and examined the phosphorylation state of this connexin in the retina. Western blot analysis with hybrid bass retinal membrane preparations showed Cx35 to be phosphorylated at both the Ser110 and Ser276 sites, and this labeling was eliminated by alkaline phosphatase digestion. The homologous sites of mouse and rabbit Cx36 were also phosphorylated in retinal membrane preparations. Quantitative confocal immunofluorescence analysis showed gap junctions identified with a monoclonal anti-Cx35 antibody to have variable levels of phosphorylation at both the Ser110 and Ser276 sites. Unusual gap junctions that could be identified by their large size (up to 32 μm2) and location in the IPL showed a prominent shift in phosphorylation state from heavily phosphorylated in nighttime, dark-adapted retina to weakly phosphorylated in daytime, light-adapted retina. Both Ser110 and Ser276 sites showed significant changes in this manner. Under both lighting conditions, other gap junctions varied from non-phosphorylated to heavily phosphorylated. We predict that changes in the phosphorylation states of these sites correlate with changes in the degree of coupling through Cx35/36 gap junctions. This leads to the conclusion that connexin phosphorylation mediates changes in coupling in some retinal networks. However, these changes are not global and likely occur in a cell type-specific or possibly a gap junction-specific manner.

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17

Butovas, Sergejus, Sheriar G. Hormuzdi, Hannah Monyer, and Cornelius Schwarz. "Effects of Electrically Coupled Inhibitory Networks on Local Neuronal Responses to Intracortical Microstimulation." Journal of Neurophysiology 96, no. 3 (September 2006): 1227–36. http://dx.doi.org/10.1152/jn.01170.2005.

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Using in vivo multielectrode electrophysiology in mice, we investigated the underpinnings of a local, long-lasting firing rate suppression evoked by intracortical microstimulation. Synaptic inhibition contributes to this suppression as it was reduced by pharmacological blockade of γ-aminobutyric acid type B (GABAB) receptors. Blockade of GABAB receptors also abolished the known sublinear addition of inhibitory response duration after repetitive electrical stimulation. Furthermore, evoked inhibition was weaker and longer in connexin 36 knockout (KO) mice that feature decoupled cortical inhibitory networks. In supragranular layers of KO mice even an unusually long excitatory response (≤50 ms) appeared that was never observed in wild-type (WT) mice. Furthermore, the spread and duration of very fast oscillations (>200 Hz) evoked by microstimulation at a short latency were strongly enhanced in KO mice. In the spatial domain, lack of connexin 36 unmasked a strong anisotropy of inhibitory spread. Although its reach along layers was almost the same as that in WT mice, the spread across cortical depth was severely hampered. In summary, the present data suggest that connexin 36–coupled networks significantly shape the electrically evoked cortical inhibitory response. Electrical coupling renders evoked cortical inhibition more precise and strong and ensures a uniform spread along the two cardinal axes of neocortical geometry.

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18

Kotova, Anna, Ksenia Timonina, and Georg R. Zoidl. "Endocytosis of Connexin 36 is Mediated by Interaction with Caveolin-1." International Journal of Molecular Sciences 21, no. 15 (July 29, 2020): 5401. http://dx.doi.org/10.3390/ijms21155401.

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The gap junctional protein connexin 36 (Cx36) has been co-purified with the lipid raft protein caveolin-1 (Cav-1). The relevance of an interaction between the two proteins is unknown. In this study, we explored the significance of Cav-1 interaction in the context of intracellular and membrane transport of Cx36. Coimmunoprecipitation assays and Förster resonance energy transfer analysis (FRET) were used to confirm the interaction between the two proteins in the Neuro 2a cell line. We found that the Cx36 and Cav-1 interaction was dependent on the intracellular calcium levels. By employing different microscopy techniques, we demonstrated that Cav-1 enhances the vesicular transport of Cx36. Pharmacological interventions coupled with cell surface biotinylation assays and FRET analysis revealed that Cav-1 regulates membrane localization of Cx36. Our data indicate that the interaction between Cx36 and Cav-1 plays a role in the internalization of Cx36 by a caveolin-dependent pathway.

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19

Wang, Yongfu, and Andrei B. Belousov. "Deletion of neuronal gap junction protein connexin 36 impairs hippocampal LTP." Neuroscience Letters 502, no. 1 (September 2011): 30–32. http://dx.doi.org/10.1016/j.neulet.2011.07.018.

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20

Kothmann, W. W., S. C. Massey, and J. O'Brien. "Dopamine-Stimulated Dephosphorylation of Connexin 36 Mediates AII Amacrine Cell Uncoupling." Journal of Neuroscience 29, no. 47 (November 25, 2009): 14903–11. http://dx.doi.org/10.1523/jneurosci.3436-09.2009.

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21

Telkes, Ildikó, Péter Kóbor, József Orbán, Tamás Kovács-Öller, Béla Völgyi, and Péter Buzás. "Connexin-36 distribution and layer-specific topography in the cat retina." Brain Structure and Function 224, no. 6 (June 6, 2019): 2183–97. http://dx.doi.org/10.1007/s00429-019-01876-y.

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22

Leite, A. R., C. P. F. Carvalho, A. G. Furtado, H. C. L. Barbosa, A. C. Boschero, and C. B. Collares-Buzato. "Co-expression and regulation of connexins 36 and 43 in cultured neonatal rat pancreatic islets." Canadian Journal of Physiology and Pharmacology 83, no. 2 (February 1, 2005): 142–51. http://dx.doi.org/10.1139/y04-133.

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Fetal and neonatal pancreatic islets present a lower insulin secretory response as compared with adult islets. Prolonged culturing leads to an improvement of the glucose-induced insulin secretion response in neonatal pancreatic islets that may involve regulation of gap junction mediated cell communication. In this study, we investigated the effect of culturing neonatal islet cells for varying periods of time and with different glucose medium concentrations on the cellular expression of the endocrine pancreatic gap junction associated connexin (Cx) 36 and Cx43. We report here that the 7-d culture induced upregulation of the expression of these junctional proteins in neonatal islets in a time-dependent manner. A correlation was observed between the increased mRNA and protein expression of Cx36 and Cx43 and the increased insulin secretion following islet culturing. In addition, increasing glucose concentration within the culture medium induced a concentration-dependent enhancement of Cx36 islet expression, but not of Cx43 expression in cultured neonatal islets. In conclusion, we suggest that the regulation of gap junctional proteins by culture medium containing factors and glucose may be an important event for the maturation process of β cells observed at in vitro conditions.Key words: connexin 36, connexin 43, gap junctions, insulin secretion, in vitro maturation, neonatal pancreatic islets.

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23

Placantonakis, Dimitris, Federico Cicirata, and John P. Welsh. "A dominant negative mutation of neuronal connexin 36 that blocks intercellular permeability." Molecular Brain Research 98, no. 1-2 (January 2002): 15–28. http://dx.doi.org/10.1016/s0169-328x(01)00306-0.

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24

Hormuzdi, Sheriar G., Isabel Pais, Fiona E. N. LeBeau, Stephen K. Towers, Andrei Rozov, Eberhard H. Buhl, Miles A. Whittington, and Hannah Monyer. "Impaired Electrical Signaling Disrupts Gamma Frequency Oscillations in Connexin 36-Deficient Mice." Neuron 31, no. 3 (August 2001): 487–95. http://dx.doi.org/10.1016/s0896-6273(01)00387-7.

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25

Wang, H. Y., Y. P. Lin, C. K. Mitchell, S. Ram, and J. O'Brien. "Two-color fluorescent analysis of connexin 36 turnover: relationship to functional plasticity." Journal of Cell Science 128, no. 21 (September 10, 2015): 3888–97. http://dx.doi.org/10.1242/jcs.162586.

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26

Melamed, Lisa, Christine Lee, Hiroaki Nagashima, Julie Miller, Hiroaki Wakimoto, and Daniel Cahill. "TAMI-36. CONNEXIN 43 BLOCKADE INHIBITS PROLIFERATION IN IDH1-MUTANT GLIOMA CELLS." Neuro-Oncology 22, Supplement_2 (November 2020): ii220—ii221. http://dx.doi.org/10.1093/neuonc/noaa215.924.

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Abstract IDH1-mutant gliomas are characteristically sensitive to NAD+ depletion. It is known that NAD+ can move between cells through gap junctions, which provides an opportunity for treatments that prevent NAD+ sharing across tumor cells, effectively decreasing available NAD+. Previous studies have also shown the role of connexin 43 (Cx43) in mediating communication in glioma cell networks and have identified Cx43 as a potential mediator of temozolomide resistance in glioma. We hypothesized that blocking Cx43 would prevent intercellular NAD+ sharing in IDH-mutant gliomas, causing tumor cells to be more vulnerable to metabolic NAD+ depletion via nicotinamide phosphoribosyltransferase (NAMPT) inhibitors and temozolomide (TMZ) treatment. Here, we show that blockade of Cx43 with α-connexin carboxyl-terminal (ACT1) is able to inhibit growth of patient-derived IDH1-mutant tumor cells. ACT1 sensitizes cells to TMZ and inhibits growth of IDH1-mutant gliomas via an NAD-dependent mechanism. We also found that ACT1 can be used in combination with other NAD-depleting drugs, such as NAMPT inhibitors, to enhance its effect and provide a viable therapeutic window. Overall, our results suggest that ACT1 may enhance the efficacy of treatments for IDH1-mutant tumors by blocking metabolic buffering through tumor cell gap junctions.

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27

Placantonakis, D. G., A. A. Bukovsky, X. H. Zeng, H. P. Kiem, and J. P. Welsh. "Fundamental role of inferior olive connexin 36 in muscle coherence during tremor." Proceedings of the National Academy of Sciences 101, no. 18 (April 21, 2004): 7164–69. http://dx.doi.org/10.1073/pnas.0400322101.

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28

Sterman, Adam, Regina Hanstein, and David C. Spray. "The effect of connexin 36 deletion on chemotherapy-induced peripheral neuropathy (CIPN)." Journal of Clinical Oncology 34, no. 26_suppl (October 9, 2016): 1. http://dx.doi.org/10.1200/jco.2016.34.26_suppl.1.

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1 Background: CIPN is a debilitating side effect and dose limiting toxicity of many chemotherapeutic agents. CIPN induces pathological changes in dorsal root ganglia (DRG), leading to increased cross-talk among the glia that surround sensory neurons (Satellite Glial Cells, SGC’s) and between sensory neurons and their adjacent SGCs via gap junctions. Since Connexin 36 (Cx36) is the main neuronal gap junction protein, we investigated CIPN in mice with deletion of Cx36. Methods: To induce CIPN, mice were given two i.p. oxaliplatin (oxa) injections 2 days apart. Controls received saline (sal). We used transgenic mice, which were either heterozygous for Cx36 or complete Cx36 knockouts (Cx36 Het or Cx36 KO), and littermate controls (Cx36 wildtype), 6-14 per group. Tactile sensitivity of the hindpaws was assessed prior to and every week after injections for 4 weeks using von Frey filaments. The number of paw withdrawals to 10 stimulations with each filament and pain thresholds (corresponding to filament that elicits 8/10 responses) were recorded. Results: Oxa-injected wildtype mice had higher response rates to filaments compared to sal-injected controls (p < 0.05), and lower tactile thresholds (at 9 days: sal 6.0±0.0g vs. oxa 1.9±0.5g, p < 0.0001), indicating hypersensitivity. Compared with wildtype, mice lacking Cx36 (Cx36 KO) displayed significantly less tactile hypersensitivity after oxa (tactile threshold at 9 days: WT 1.9±0.5g vs. KO 4.0±0.4g, p < 0.01), whereas oxa induced tactile hypersensitivity occurred in a similar fashion in Cx36 Het mice (tactile threshold at 9 days: WT 1.9±0.5g vs. Het 1.5±0.1g). At 9 days, there were fewer responses to filaments in oxa-injected Cx36 KO mice compared to oxa-injected wildtype mice (p < 0.05), but not in oxa-injected Cx36 Het mice. Conclusions: We found that oxaliplatin induces transient CIPN, represented by tactile hypersensitivity, in wildtype mice. Deletion of the gap junction protein Cx36, as displayed in the Cx36 KO mice, resulted in significantly less CIPN. This is the first report that a neuronal gap junction protein may modulate pain sensitivity, and points to a new molecule (Cx36) as a potential novel target for CIPN therapy.

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29

Steffensen, Scott C., Katie D. Bradley, David M. Hansen, Jeffrey D. Wilcox, Rebecca S. Wilcox, David W. Allison, Collin B. Merrill, and Jeffrey G. Edwards. "The role of connexin-36 gap junctions in alcohol intoxication and consumption." Synapse 65, no. 8 (December 28, 2010): 695–707. http://dx.doi.org/10.1002/syn.20885.

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Charpantier, E., J. Cancela, and P. Meda. "Beta cells preferentially exchange cationic molecules via connexin 36 gap junction channels." Diabetologia 50, no. 11 (September 8, 2007): 2332–41. http://dx.doi.org/10.1007/s00125-007-0807-9.

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31

Mirelle Goes e Silva Costa, Hosana, Paulo Leonardo Araújo de Góis Morais, Débora Lopes Silva de Souza, Claudio Lopes de Vasconcelos, Dayane Pessoa de Araújo, Lucidio Clebeson de Oliveira, José Edvan Souza Júnior, Fausto Pierdoná Guzen, and José Rodolfo Lopes de Paiva Cavalcanti. "Physiological and Clinical Aspects of Eletrical Synapse: Emphasis of the Connexin 36." Journal of Pharmacological, Chemistry and Biological Sciences 02, no. 05 (2020): 270–83. http://dx.doi.org/10.36619/jpcbs.2020.2.68.78.

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32

Wang, Yongfu, Janna V. Denisova, Ki Sung Kang, Joseph D. Fontes, Bao Ting Zhu, and Andrei B. Belousov. "Neuronal Gap Junctions Are Required for NMDA Receptor–Mediated Excitotoxicity: Implications in Ischemic Stroke." Journal of Neurophysiology 104, no. 6 (December 2010): 3551–56. http://dx.doi.org/10.1152/jn.00656.2010.

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N-methyl-d-aspartate receptors (NMDARs) play an important role in cell survival versus cell death decisions during neuronal development, ischemia, trauma, and epilepsy. Coupling of neurons by electrical synapses (gap junctions) is high or increases in neuronal networks during all these conditions. In the developing CNS, neuronal gap junctions are critical for two different types of NMDAR-dependent cell death. However, whether neuronal gap junctions play a role in NMDAR-dependent neuronal death in the mature CNS was not known. Using Fluoro-Jade B staining, we show that a single intraperitoneal administration of NMDA (100 mg/kg) to adult wild-type mice induces neurodegeneration in three forebrain regions, including rostral dentate gyrus. However, the NMDAR-mediated neuronal death is prevented by pharmacological blockade of neuronal gap junctions (with mefloquine, 30 mg/kg) and does not occur in mice lacking neuronal gap junction protein, connexin 36. Using Western blots, electrophysiology, calcium imaging, and gas chromatography–mass spectrometry in wild-type and connexin 36 knockout mice, we show that the reduced level of neuronal death in knockout animals is not caused by the reduced expression of NMDARs, activity of NMDARs, or permeability of the blood–brain barrier to NMDA. In wild-type animals, this neuronal death is not caused by upregulation of connexin 36 by NMDA. Finally, pharmacological and genetic inactivation of neuronal gap junctions in mice also dramatically reduces neuronal death caused by photothrombotic focal cerebral ischemia. The results indicate that neuronal gap junctions are required for NMDAR-dependent excitotoxicity and play a critical role in ischemic neuronal death.

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33

Corsini, Silvia, Maria Tortora, Rossana Rauti, and Andrea Nistri. "Nicotine protects rat hypoglossal motoneurons from excitotoxic death via downregulation of connexin 36." Cell Death & Disease 8, no. 6 (June 2017): e2881-e2881. http://dx.doi.org/10.1038/cddis.2017.232.

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34

Liu, C. R., L. Xu, Y. M. Zhong, R. X. Li, and X. L. Yang. "Expression of connexin 35/36 in retinal horizontal and bipolar cells of carp." Neuroscience 164, no. 3 (December 2009): 1161–69. http://dx.doi.org/10.1016/j.neuroscience.2009.09.035.

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35

Calabrese, A., M. Zhang, V. Serre-Beinier, D. Caton, C. Mas, L. S. Satin, and P. Meda. "Connexin 36 Controls Synchronization of Ca2+ Oscillations and Insulin Secretion in MIN6 Cells." Diabetes 52, no. 2 (February 1, 2003): 417–24. http://dx.doi.org/10.2337/diabetes.52.2.417.

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36

Allison, David W., Allison J. Ohran, Sarah H. Stobbs, Manuel Mameli, C. Fernando Valenzuela, Sterling N. Sudweeks, Andrew P. Ray, Steven J. Henriksen, and Scott C. Steffensen. "Connexin-36 gap junctions mediate electrical coupling between ventral tegmental area GABA neurons." Synapse 60, no. 1 (2006): 20–31. http://dx.doi.org/10.1002/syn.20272.

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37

Liu, Xiao-Bo, and Edward G. Jones. "Fine structural localization of connexin-36 immunoreactivity in mouse cerebral cortex and thalamus." Journal of Comparative Neurology 466, no. 4 (October 13, 2003): 457–67. http://dx.doi.org/10.1002/cne.10901.

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Buhl, Derek L., Kenneth D. Harris, Sheriar G. Hormuzdi, Hanna Monyer, and György Buzsáki. "Selective Impairment of Hippocampal Gamma Oscillations in Connexin-36 Knock-Out MouseIn Vivo." Journal of Neuroscience 23, no. 3 (February 1, 2003): 1013–18. http://dx.doi.org/10.1523/jneurosci.23-03-01013.2003.

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Short, Kurt W., W. Steven Head, Michael McCaughey, and David W. Piston. "Fluorescence Imaging and Analysis of Blood Flow in Connexin-36 Mouse Pancreatic Islets." Biophysical Journal 102, no. 3 (January 2012): 191a. http://dx.doi.org/10.1016/j.bpj.2011.11.1043.

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Schock, Sarah C., Danielle LeBlanc, Antoine M. Hakim, and Charlie S. Thompson. "ATP release by way of connexin 36 hemichannels mediates ischemic tolerance in vitro." Biochemical and Biophysical Research Communications 368, no. 1 (March 2008): 138–44. http://dx.doi.org/10.1016/j.bbrc.2008.01.054.

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Brown, del Corsso, Zoidl, Donaldson, Spray, and Zoidl. "Tubulin-Dependent Transport of Connexin-36 Potentiates the Size and Strength of Electrical Synapses." Cells 8, no. 10 (September 25, 2019): 1146. http://dx.doi.org/10.3390/cells8101146.

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Abstract:

Connexin-36 (Cx36) electrical synapses strengthen transmission in a calcium/calmodulin (CaM)/calmodulin-dependent kinase II (CaMKII)-dependent manner similar to a mechanism whereby the N-methyl-D-aspartate (NMDA) receptor subunit NR2B facilitates chemical transmission. Since NR2B–microtubule interactions recruit receptors to the cell membrane during plasticity, we hypothesized an analogous modality for Cx36. We determined that Cx36 binding to tubulin at the carboxy-terminal domain was distinct from Cx43 and NR2B by binding a motif overlapping with the CaM and CaMKII binding motifs. Dual patch-clamp recordings demonstrated that pharmacological interference of the cytoskeleton and deleting the binding motif at the Cx36 carboxyl-terminal (CT) reversibly abolished Cx36 plasticity. Mechanistic details of trafficking to the gap-junction plaque (GJP) were probed pharmacologically and through mutational analysis, all of which affected GJP size and formation between cell pairs. Lys279, Ile280, and Lys281 positions were particularly critical. This study demonstrates that tubulin-dependent transport of Cx36 potentiates synaptic strength by delivering channels to GJPs, reinforcing the role of protein transport at chemical and electrical synapses to fine-tune communication between neurons.

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ZHANG, Bingtian, Zhibin CHEN, Xiaowu CHEN, Xiaokuo HE, and Chao HAN. "Research on Role of Connexin 36 in Pathogenesis of Rats with Levodopa-induced Dyskinesia." Rehabilitation Medicine 26, no. 4 (2016): 34. http://dx.doi.org/10.3724/sp.j.1329.2016.04034.

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Belousov, Andrei B., Hiroshi Nishimune, Janna V. Denisova, and Joseph D. Fontes. "A potential role for neuronal connexin 36 in the pathogenesis of amyotrophic lateral sclerosis." Neuroscience Letters 666 (February 2018): 1–4. http://dx.doi.org/10.1016/j.neulet.2017.12.027.

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Lall, Varinder K., Gareth Bruce, Larysa Voytenko, Mark Drinkhill, Kerstin Wellershaus, Klaus Willecke, Jim Deuchars, and Susan A. Deuchars. "Physiologic regulation of heart rate and blood pressure involves connexin 36–containing gap junctions." FASEB Journal 31, no. 9 (September 2017): 3966–77. http://dx.doi.org/10.1096/fj.201600919rr.

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Chen, S., and Q. Dong. "Asymmetric Dimmethylarginine Protects Neurons from Oxygen Glucose Deprivation Insult by Downregulating Connexin-36 (P01.027)." Neurology 78, Meeting Abstracts 1 (April 22, 2012): P01.027. http://dx.doi.org/10.1212/wnl.78.1_meetingabstracts.p01.027.

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Wang, Ping, Stephani C. Wang, Dongyang Li, Tong Li, Hai-Peng Yang, Liwei Wang, Yu-Feng Wang, and Vladimir Parpura. "Role of Connexin 36 in Autoregulation of Oxytocin Neuronal Activity in Rat Supraoptic Nucleus." ASN Neuro 11 (January 2019): 175909141984376. http://dx.doi.org/10.1177/1759091419843762.

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In the supraoptic nucleus (SON), the incidence of dye coupling among oxytocin (OT) neurons increases significantly in nursing mothers. However, the type(s) of connexin (Cx) involved is(are) unknown. In this study, we specifically investigated whether Cx36 plays a functional role in the coupling between OT neurons in the SON of lactating rats. In this brain region, Cx36 was mainly coimmunostained with vasopressin neurons in virgin female rats, whereas in lactating rats, Cx36 was primarily colocalized with OT neurons. In brain slices from lactating rats, application of quinine (0.1 mM), a selective blocker of Cx36, significantly reduced dye coupling among OT neurons as well as the discharge/firing frequency of spikes/action potentials and their amplitude, and transiently depolarized the membrane potential of OT neurons in whole-cell patch-clamp recordings. However, quinine significantly reduced the amplitude, but not frequency, of inhibitory postsynaptic currents in OT neurons; the duration of excitatory postsynaptic currents was reduced but not their frequency and amplitude. Furthermore, the excitatory effect of OT (1 pM) on OT neurons was significantly weakened and delayed by quinine, and burst firing was absent in the presence of this inhibitor. Lastly, Western blotting analysis revealed that the presence of combined, but not alone, quinine and OT significantly reduced the amount of Cx36 in the SON. Thus, Cx36-mediated junctional communication plays a crucial role in autoregulatory control of OT neuronal activity, likely by acting at the postsynaptic sites. The level of Cx36 is modulated by its own activity and the presence of OT.

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Katti, Christiana, Rachel Butler, and Sumathi Sekaran. "Diurnal and Circadian Regulation of Connexin 36 Transcript and Protein in the Mammalian Retina." Investigative Opthalmology & Visual Science 54, no. 1 (January 28, 2013): 821. http://dx.doi.org/10.1167/iovs.12-10375.

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Pizarro-Delgado, Javier, Ilaria Fasciani, Ana Temperan, María Romero, Daniel González-Nieto, Paloma Alonso-Magdalena, Anna Nualart-Marti, et al. "Inhibition of connexin 36 hemichannels by glucose contributes to the stimulation of insulin secretion." American Journal of Physiology-Endocrinology and Metabolism 306, no. 12 (June 15, 2014): E1354—E1366. http://dx.doi.org/10.1152/ajpendo.00358.2013.

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The existence of functional connexin36 ( Cx36) hemichannels in β-cells was investigated in pancreatic islets of rat and wild-type ( Cx36+/+), monoallelic ( Cx36+/−), and biallelic ( Cx36−/−) knockout mice. Hemichannel opening by KCl depolarization was studied by measuring ATP release and changes of intracellular ATP (ADP). Cx36+/+ islets lost ATP after depolarization with 70 mM KCl at 5 mM glucose; ATP loss was prevented by 8 and 20 mM glucose or 50 μM mefloquine (connexin inhibitor). ATP content was higher in Cx36−/− than Cx36+/+ islets and was not decreased by KCl depolarization; Cx36+/− islets showed values between that of control and homozygous islets. Five minimolar extracellular ATP increased ATP content and ATP/ADP ratio and induced a biphasic insulin secretion in depolarized Cx36+/+ and Cx36+/− but not Cx36−/− islets. Cx36 hemichannels expressed in oocytes opened upon depolarization of membrane potential, and their activation was inhibited by mefloquine and glucose (IC50 ∼8 mM). It is postulated that glucose-induced inhibition of Cx36 hemichannels in islet β-cells might avoid depolarization-induced ATP loss, allowing an optimum increase of the ATP/ADP ratio by sugar metabolism and a biphasic stimulation of insulin secretion. Gradual suppression of glucose-induced insulin release in Cx36+/− and Cx36−/− islets confirms that Cx36 gap junction channels are necessary for a full secretory stimulation and might account for the glucose intolerance observed in mice with defective Cx36 expression. Mefloquine targeting of Cx36 on both gap junctions and hemichannels also suppresses glucose-stimulated secretion. By contrast, glucose stimulation of insulin secretion requires Cx36 hemichannels' closure but keeping gap junction channels opened.

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Hempelmann, Anne, Armin Heils, and Thomas Sander. "Confirmatory evidence for an association of the connexin-36 gene with juvenile myoclonic epilepsy." Epilepsy Research 71, no. 2-3 (October 2006): 223–28. http://dx.doi.org/10.1016/j.eplepsyres.2006.06.021.

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Diemer, Tanja, Dominic Landgraf, Takako Noguchi, Haiyun Pan, Jose L. Moreno, and David K. Welsh. "Cellular circadian oscillators in the suprachiasmatic nucleus remain coupled in the absence of connexin-36." Neuroscience 357 (August 2017): 1–11. http://dx.doi.org/10.1016/j.neuroscience.2017.05.037.

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