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Journal articles on the topic 'CX546'

Author: Grafiati

Published: 4 June 2021

Last updated: 4 February 2022

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1

Le, Alexander M., Michelle Lee, Chen Su, Anthony Zou, and Jing Wang. "AMPAkines Have Novel Analgesic Properties in Rat Models of Persistent Neuropathic and Inflammatory Pain." Anesthesiology 121, no. 5 (2014): 1080–90. http://dx.doi.org/10.1097/aln.0000000000000351.

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Abstract Background: Novel analgesics that do not suppress the respiratory drive are urgently needed. Glutamate signaling through α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors plays important roles in central pain circuits. AMPAkines augment AMPA receptor function and have been shown to stimulate the respiratory drive to oppose opioid-induced hypoventilation. However, their role in chronic pain states remains unknown. Methods: The authors studied AMPAkines (CX546 and CX516) in rat spared nerve injury (SNI) model of neuropathic pain and Complete Freund’s Adjuvant (CFA) m

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Su, Chen, Hau Yeuh Lin, Runtao Yang, et al. "AMPAkines Target the Nucleus Accumbens to Relieve Postoperative Pain." Anesthesiology 125, no. 5 (2016): 1030–43. http://dx.doi.org/10.1097/aln.0000000000001336.

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Abstract Background AMPAkines augment the function of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors in the brain to increase excitatory outputs. These drugs are known to relieve persistent pain. However, their role in acute pain is unknown. Furthermore, a specific molecular and anatomic target for these novel analgesics remains elusive. Methods The authors studied the analgesic role of an AMPAkine, CX546, in a rat paw incision (PI) model of acute postoperative pain. The authors measured the effect of AMPAkines on sensory and depressive symptoms of pain using mechanical

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Zhou, W., N. Wang, C. Yang, X. M. Li, Z. Q. Zhou, and J. J. Yang. "Ketamine-induced antidepressant effects are associated with AMPA receptors-mediated upregulation of mTOR and BDNF in rat hippocampus and prefrontal cortex." European Psychiatry 29, no. 7 (2014): 419–23. http://dx.doi.org/10.1016/j.eurpsy.2013.10.005.

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AbstractKetamine exerts fast acting, robust, and lasting antidepressant effects in a sub-anesthetic dose, however, the underlying mechanisms are still not fully elucidated. Recent studies have suggested that ketamine's antidepressant effects are probably attributed to the activation of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors. The present study aimed to observe the effects of AMPA receptor modulators on mammalian target of rapamycin (mTOR) and brain-derived neurotrophic factor (BDNF) expression during the procedure of ketamine exerting antidepressant effects. There

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Nagarajan, Naveen, Christoph Quast, Andrew R. Boxall, Mohammed Shahid, and Christian Rosenmund. "Mechanism and impact of allosteric AMPA receptor modulation by the AmpakineTM CX546." Neuropharmacology 41, no. 6 (2001): 650–63. http://dx.doi.org/10.1016/s0028-3908(01)00133-2.

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Schitine, Clarissa, Sara Xapelli, Fabienne Agasse, et al. "Ampakine CX546 increases proliferation and neuronal differentiation in subventricular zone stem/progenitor cell cultures." European Journal of Neuroscience 35, no. 11 (2012): 1672–83. http://dx.doi.org/10.1111/j.1460-9568.2012.08072.x.

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6

Lipina, Tatiana, Karin Weiss, and John Roder. "The Ampakine CX546 Restores the Prepulse Inhibition and Latent Inhibition Deficits in mGluR5-Deficient Mice." Neuropsychopharmacology 32, no. 4 (2006): 745–56. http://dx.doi.org/10.1038/sj.npp.1301191.

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Pellerin, Luc, and Pierre J. Magistretti. "Ampakine CX546 bolsters energetic response of astrocytes: A novel target for cognitive-enhancing drugs acting as AMPA receptor modulators." Journal of Cerebral Blood Flow & Metabolism 25, no. 1_suppl (2005): S70. http://dx.doi.org/10.1038/sj.jcbfm.9591524.0070.

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Hachem, LD, AJ Mothe, and CH Tator. "P.089 AMPA receptor modulation as a therapeutic strategy to enhance survival of spinal cord neural stem cells." Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques 45, s2 (2018): S39—S40. http://dx.doi.org/10.1017/cjn.2018.191.

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Background: Transplantation of neural stem/progenitor cells (NSPCs) following spinal cord injury (SCI) is a promising strategy to enhance regeneration but is limited by poor survival of grafted cells. Recently, we demonstrated for the first time that the excitatory neurotransmitter glutamate, which is released after SCI, promotes survival/proliferation of spinal cord NSPCs via the AMPA subtype of glutamate receptors. Here, we examine the therapeutic potential of selective AMPA receptor modulation on NSPC survival using allosteric AMPA receptor modulators known as ampakines. Methods: NSPCs from

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Pellerin, Luc, and Pierre J. Magistretti. "Ampakinetm CX546 bolsters energetic response of astrocytes: a novel target for cognitive-enhancing drugs acting as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor modulators." Journal of Neurochemistry 92, no. 3 (2005): 668–77. http://dx.doi.org/10.1111/j.1471-4159.2004.02905.x.

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Montgomery, Kyle E., Markus Kessler, and Amy C. Arai. "Modulation of Agonist Binding to AMPA Receptors by 1-(1,4-Benzodioxan-6-ylcarbonyl)piperidine (CX546): Differential Effects across Brain Regions and GluA1–4/Transmembrane AMPA Receptor Regulatory Protein Combinations." Journal of Pharmacology and Experimental Therapeutics 331, no. 3 (2009): 965–74. http://dx.doi.org/10.1124/jpet.109.158014.

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11

Ebihara, L., and E. Steiner. "Properties of a nonjunctional current expressed from a rat connexin46 cDNA in Xenopus oocytes." Journal of General Physiology 102, no. 1 (1993): 59–74. http://dx.doi.org/10.1085/jgp.102.1.59.

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Connexin46 (cxn46) is a gap junctional protein that was cloned from a rat lens cDNA library. Expression of cxn46 in solitary Xenopus oocytes resulted in the development of a large time- and voltage-dependent current that was not observed in noninjected control oocytes or in oocytes injected with mRNA for cxn43 or cxn32. The cxn46-induced current activated at potentials positive to -20 mV. On repolarization to -40 mV, the current deactivated over a period of several seconds. Removal of external calcium caused a marked increase in the amplitude of the cxn46-induced current, shifted the steady-st

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Wu, Kuo-Jen, Seong-Jin Yu, Kak-Shan Shia, et al. "A Novel CXCR4 Antagonist CX549 Induces Neuroprotection in Stroke Brain." Cell Transplantation 26, no. 4 (2017): 571–83. http://dx.doi.org/10.3727/096368916x693563.

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C-X-C chemokine receptor type 4 (CXCR4) is a receptor for a pleiotropic chemokine CXCL12. Previous studies have shown that the acute administration of the CXCR4 antagonist AMD3100 reduced neuroinflammation in stroke brain and mobilized bone marrow hematopoietic stem cells (HSCs). The purpose of this study was to characterize the neuroprotective and neurotrophic effect of a novel CXCR4 antagonist CX549. We demonstrated that CX549 had a higher affinity for CXCR4 and was more potent than AMD3100 to inhibit CXCL12-mediated chemotaxis in culture. CX549 effectively reduced the activation of microgli

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Pelletier, R. Marc, Casimir D. Akpovi, Li Chen, Nalin M. Kumar, and María L. Vitale. "Complementary expression and phosphorylation of Cx46 and Cx50 during development and following gene deletion in mouse and in normal and orchitic mink testes." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 309, no. 3 (2015): R255—R276. http://dx.doi.org/10.1152/ajpregu.00152.2015.

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Gap junction-mediated communication helps synchronize interconnected Sertoli cell activities. Besides, coordination of germ cell and Sertoli cell activities depends on gap junction-mediated Sertoli cell–germ cell communication. This report assesses mechanisms underlying the regulation of connexin 46 (Cx46) and Cx50 in mouse testis and those accompanying a “natural” seasonal and a pathological arrest of spermatogenesis, resulting from autoimmune orchitis (AIO) in mink. Furthermore, the impact of deleting Cx46 or Cx50 on the expression, phosphorylation of junction proteins, and spermatogenesis i

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Hu, Zhengping, Manuel A. Riquelme, Sumin Gu, and Jean X. Jiang. "Regulation of Connexin Gap Junctions and Hemichannels by Calcium and Calcium Binding Protein Calmodulin." International Journal of Molecular Sciences 21, no. 21 (2020): 8194. http://dx.doi.org/10.3390/ijms21218194.

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Connexins are the structural components of gap junctions and hemichannels that mediate the communication and exchange of small molecules between cells, and between the intracellular and extracellular environment, respectively. Connexin (Cx) 46 is predominately expressed in lens fiber cells, where they function in maintaining the homeostasis and transparency of the lens. Cx46 mutations are associated with impairment of channel function, which results in the development of congenital cataracts. Cx46 gap junctions and hemichannels are closely regulated by multiple mechanisms. Key regulators of Cx

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Koval, Michael, James E. Harley, Elizabeth Hick, and Thomas H. Steinberg. "Connexin46 Is Retained as Monomers in a trans-Golgi Compartment of Osteoblastic Cells." Journal of Cell Biology 137, no. 4 (1997): 847–57. http://dx.doi.org/10.1083/jcb.137.4.847.

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Connexins are gap junction proteins that form aqueous channels to interconnect adjacent cells. Rat osteoblasts express connexin43 (Cx43), which forms functional gap junctions at the cell surface. We have found that ROS 17/2.8 osteosarcoma cells, UMR 106-01 osteosarcoma cells, and primary rat calvarial osteoblastic cells also express another gap junction protein, Cx46. Cx46 is a major component of plasma membrane gap junctions in lens. In contrast, Cx46 expressed by osteoblastic cells was predominantly localized to an intracellular perinuclear compartment, which appeared to be an aspect of the

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Banerjee, Debarshi, Satyabrata Das, Samuel A. Molina, et al. "Investigation of the Reciprocal Relationship between the Expression of Two Gap Junction Connexin Proteins, Connexin46 and Connexin43." Journal of Biological Chemistry 286, no. 27 (2011): 24519–33. http://dx.doi.org/10.1074/jbc.m110.217208.

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Connexins are the transmembrane proteins that form gap junctions between adjacent cells. The function of the diverse connexin molecules is related to their tissue-specific expression and highly dynamic turnover. Although multiple connexins have been previously reported to compensate for each other's functions, little is known about how connexins influence their own expression or intracellular regulation. Of the three vertebrate lens connexins, two connexins, connexin43 (Cx43) and connexin46 (Cx46), show reciprocal expression and subsequent function in the lens and in lens cell culture. In this

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Acuña, Rodrigo A., Manuel Varas-Godoy, Viviana M. Berthoud, Ivan E. Alfaro, and Mauricio A. Retamal. "Connexin-46 Contained in Extracellular Vesicles Enhance Malignancy Features in Breast Cancer Cells." Biomolecules 10, no. 5 (2020): 676. http://dx.doi.org/10.3390/biom10050676.

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Under normal conditions, almost all cell types communicate with their neighboring cells through gap junction channels (GJC), facilitating cellular and tissue homeostasis. A GJC is formed by the interaction of two hemichannels; each one of these hemichannels in turn is formed by six subunits of transmembrane proteins called connexins (Cx). For many years, it was believed that the loss of GJC-mediated intercellular communication was a hallmark in cancer development. However, nowadays this paradigm is changing. The connexin 46 (Cx46), which is almost exclusively expressed in the eye lens, is upre

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Retamal, Mauricio A., ShengYong Yin, Guillermo A. Altenberg, and Luis Reuss. "Modulation of Cx46 hemichannels by nitric oxide." American Journal of Physiology-Cell Physiology 296, no. 6 (2009): C1356—C1363. http://dx.doi.org/10.1152/ajpcell.00054.2009.

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Gap-junction hemichannels are composed of six protein subunits (connexins). Undocked hemichannels contribute to physiological autocrine/paracrine cell signaling, including release of signaling molecules, cell-volume regulation, and glucose uptake. In addition, hemichannels may be pathologically activated by dephosphorylation and cell-membrane depolarization. Such hemichannel opening may induce and/or accelerate cell death. It has been suggested that connexin43 (Cx43) hemichannels are sensitive to redox potential changes and that one or more intracellular cysteines is/are important for this pro

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Pelletier, R. Marc, Hamed Layeghkhavidaki, Nalin M. Kumar, and María Leiza Vitale. "Cx30.2 deletion causes imbalances in testicular Cx43, Cx46, and Cx50 and insulin receptors. Reciprocally, diabetes/obesity alters Cx30.2 in mouse testis." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 318, no. 6 (2020): R1078—R1090. http://dx.doi.org/10.1152/ajpregu.00044.2020.

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Cx30.2 protein content and localization were assessed during development. An account of Cx30.2, Cx43, Cx46, and Cx50, and insulin receptor (IR) responses to Cx30.2, Cx46, or Cx50 deficiency in mouse interstitial tissue (ITf)- and seminiferous tubule-enriched fractions (STf) is given. The impact of high glucose/insulin on Cx30.2 was investigated in spontaneously diabetic and obese db/db and ob/ob mouse testis and anterior pituitary (AP). Cx30.2 labeled contacts in vascular endothelial and Leydig cells and Sertoli cell junctions in stage V–VII. Cx30.2 expression is regulated differently in the i

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Paul, D. L., L. Ebihara, L. J. Takemoto, K. I. Swenson, and D. A. Goodenough. "Connexin46, a novel lens gap junction protein, induces voltage-gated currents in nonjunctional plasma membrane of Xenopus oocytes." Journal of Cell Biology 115, no. 4 (1991): 1077–89. http://dx.doi.org/10.1083/jcb.115.4.1077.

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Gap junctions are composed of a family of structural proteins called connexins, which oligomerize into intercellular channels and function to exchange low molecular weight metabolites and ions between adjacent cells. We have cloned a new member of the connexin family from lens cDNA, with a predicted molecular mass of 46 kD, called rat connexin46 (Cx46). Since a full-length cDNA corresponding to the 2.8-kb mRNA was not obtained, the stop codon and surrounding sequences were confirmed from rat genomic DNA. The RNA coding for this protein is abundant in lens fibers and detectable in both myocardi

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White, T. W., R. Bruzzone, S. Wolfram, D. L. Paul, and D. A. Goodenough. "Selective interactions among the multiple connexin proteins expressed in the vertebrate lens: the second extracellular domain is a determinant of compatibility between connexins." Journal of Cell Biology 125, no. 4 (1994): 879–92. http://dx.doi.org/10.1083/jcb.125.4.879.

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Gap junctions are collections of intercellular channels composed of structural proteins called connexins (Cx). We have examined the functional interactions of the three rodent connexins present in the lens, Cx43, Cx46, and Cx50, by expressing them in paired Xenopus oocytes. Homotypic channels containing Cx43, Cx46, or Cx50 all developed high conductance. heterotypic channels composed of Cx46 paired with either Cx43 or Cx50 were also well coupled, whereas Cx50 did not form functional channels with Cx43. We also examined the functional response of homotypic and heterotypic channels to transjunct

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Retamal, Mauricio A., ShengYong Yin, Guillermo A. Altenberg, and Luis Reuss. "Voltage-dependent facilitation of Cx46 hemichannels." American Journal of Physiology-Cell Physiology 298, no. 1 (2010): C132—C139. http://dx.doi.org/10.1152/ajpcell.00258.2009.

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Gap junction channels are formed by two hemichannels in series (one from each neighboring cell), which are in turn connexin hexamers. Under normal conditions, hemichannels at the plasma membrane are mostly closed but can be opened by changes in membrane voltage, extracellular divalent ion concentration, phosphorylation, pH, and redox potential. Recently, interactions between channels have been found to modulate the activity of several ion channels, including gap junction channels. Here, we studied whether connexin46 (Cx46) hemichannels display such behavior. We studied the response of the Cx46

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Martinez-Wittinghan, Francisco J., Caterina Sellitto, Leping Li, et al. "Dominant cataracts result from incongruous mixing of wild-type lens connexins." Journal of Cell Biology 161, no. 5 (2003): 969–78. http://dx.doi.org/10.1083/jcb.200303068.

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Gap junctions are composed of proteins called connexins (Cx) and facilitate both ionic and biochemical modes of intercellular communication. In the lens, Cx46 and Cx50 provide the gap junctional coupling needed for homeostasis and growth. In mice, deletion of Cx46 produced severe cataracts, whereas knockout of Cx50 resulted in significantly reduced lens growth and milder cataracts. Genetic replacement of Cx50 with Cx46 by knockin rescued clarity but not growth. By mating knockin and knockout mice, we show that heterozygous replacement of Cx50 with Cx46 rescued growth but produced dominant cata

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Tong, Jun-Jie, Bonnie C. H. Sohn, Anh Lam, D. Eric Walters, Barbara M. Vertel, and Lisa Ebihara. "Properties of two cataract-associated mutations located in the NH2 terminus of connexin 46." American Journal of Physiology-Cell Physiology 304, no. 9 (2013): C823—C832. http://dx.doi.org/10.1152/ajpcell.00344.2012.

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Mutations in connexin 46 are associated with congenital cataracts. The purpose of this project was to characterize cellular and functional properties of two congenital cataract-associated mutations located in the NH2 terminus of connexin 46: Cx46D3Y and Cx46L11S, which we found localized to gap junctional plaques like wild-type Cx46 in transfected HeLa cells. Dual two-microelectrode-voltage-clamp studies of Xenopus oocyte pairs injected with wild-type or mutant rat Cx46 showed that oocyte pairs injected with D3Y or L11S cRNA failed to induce gap junctional coupling, whereas oocyte pairs inject

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Abrams, Charles K., Alejandro Peinado, Rola Mahmoud, et al. "Alterations at Arg76 of human connexin 46, a residue associated with cataract formation, cause loss of gap junction formation but preserve hemichannel function." American Journal of Physiology-Cell Physiology 315, no. 5 (2018): C623—C635. http://dx.doi.org/10.1152/ajpcell.00157.2018.

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The connexins are members of a family of integral membrane proteins that form gap junction channels between apposed cells and/or hemichannels across the plasma membranes. The importance of the arginine at position 76 (Arg76) in the structure and/or function of connexin 46 (Cx46) is highlighted by its conservation across the entire connexin family and the occurrence of pathogenic mutations at this (or the corresponding homologous) residue in a number of human diseases. Two mutations at Arg76 in Cx46 are associated with cataracts in humans, highlighting the importance of this residue. We examine

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Tenbroek, E., M. Arneson, L. Jarvis, and C. Louis. "The distribution of the fiber cell intrinsic membrane proteins MP20 and connexin46 in the bovine lens." Journal of Cell Science 103, no. 1 (1992): 245–57. http://dx.doi.org/10.1242/jcs.103.1.245.

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MP20 is an intrinsic membrane protein previously identified in mammalian lens fiber cells. To identify a possible role for this protein in the lens, the distribution of MP20 and connexin46 has now been examined. Western immunoblotting with an anti-peptide antibody generated to the C-terminal 8 amino acids of MP20 confirmed the presence of this protein in the lens of several different mammalian species. A monoclonal antibody 5H1 was prepared that, in Western blots of bovine lesn membranes, recognized the same component as an antibody to rat connexin46 (Cx46). The apparent molecular mass of this

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Ebihara, Lisa, Yegor Korzyukov, Sorabh Kothari, and Jun-Jie Tong. "Cx46 hemichannels contribute to the sodium leak conductance in lens fiber cells." American Journal of Physiology-Cell Physiology 306, no. 5 (2014): C506—C513. http://dx.doi.org/10.1152/ajpcell.00353.2013.

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The lens is proposed to have an internal microcirculation system consisting of continuously circulating ionic fluxes that play an essential role in maintaining lens transparency. One of the key components of this system is the sodium leak conductance. Here we investigate the contribution of Cx46 hemichannels to the basal membrane permeability of peripheral fiber cells isolated from transgenic mouse lenses lacking Cx50 or both Cx50 and Cx46 (dKO) using the whole cell patch-clamp technique. Our results show that Cx46 hemichannels were largely closed at a resting voltage of −60 mV in the presence

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Das Sarma, Jayasri, Rita A. Meyer, Fushan Wang, Valsamma Abraham, Cecilia W. Lo, and Michael Koval. "Multimeric connexin interactions prior to the trans-Golgi network." Journal of Cell Science 114, no. 22 (2001): 4013–24. http://dx.doi.org/10.1242/jcs.114.22.4013.

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Cells that express multiple connexins have the capacity to form heteromeric (mixed) gap junction hemichannels. We used a dominant negative connexin construct, consisting of bacterial β-galactosidase fused to the C terminus of connexin43 (Cx43/β-gal), to examine connexin compatibility in NIH 3T3 cells. Cx43/β-gal is retained in a perinuclear compartment and inhibits Cx43 transport to the cell surface. The intracellular connexin pool induced by Cx43/β-gal colocalized with a medial Golgi apparatus marker and was readily disassembled by treatment with brefeldin A. This was unexpected, since previo

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Abraham, Valsamma, Michael L. Chou, Philip George, et al. "Heterocellular gap junctional communication between alveolar epithelial cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 280, no. 6 (2001): L1085—L1093. http://dx.doi.org/10.1152/ajplung.2001.280.6.l1085.

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We analyzed the pattern of gap junction protein (connexin) expression in vivo by indirect immunofluorescence. In normal rat lung sections, connexin (Cx)32 was expressed by type II cells, whereas Cx43 was more ubiquitously expressed and Cx46 was expressed by occasional alveolar epithelial cells. In response to bleomycin-induced lung injury, Cx46 was upregulated by alveolar epithelial cells, whereas Cx32 and Cx43 expression were largely unchanged. Given that Cx46 may form gap junction channels with either Cx43 or Cx32, we examined the ability of primary alveolar epithelial cells cultured for 6 d

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Pelletier, R. Marc, Casimir D. Akpovi, Li Chen, and María Leiza Vitale. "Cholesterol metabolism and Cx43, Cx46, and Cx50 gap junction protein expression and localization in normal and diabetic and obese ob/ob and db/db mouse testes." American Journal of Physiology-Endocrinology and Metabolism 314, no. 1 (2018): E21—E38. http://dx.doi.org/10.1152/ajpendo.00215.2017.

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Decreased fertility and birth rates arise from metabolic disorders. This study assesses cholesterol metabolism and Cx46, Cx50, and Cx43 expression in interstitium- and seminiferous tubule-enriched fractions of leptin-deficient ( ob/ob) and leptin receptor-deficient ( db/db) mice, two type 2 diabetes and obesity models associated with infertility. Testosterone levels decreased and glucose and free and esterified cholesterol (FC and EC) levels increased in serum, whereas FC and EC levels decreased in the interstitium, in ob/ob and db/db mice. In tubules, a decrease in EC caused FC-to-EC ratios t

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White, Thomas W., Daniel A. Goodenough, and David L. Paul. "Targeted Ablation of Connexin50 in Mice Results in Microphthalmia and Zonular Pulverulent Cataracts." Journal of Cell Biology 143, no. 3 (1998): 815–25. http://dx.doi.org/10.1083/jcb.143.3.815.

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In the ocular lens, gap junctional communication is a key component of homeostatic mechanisms preventing cataract formation. Gap junctions in rodent lens fibers contain two known intercellular channel-forming proteins, connexin50 (Cx50) and Cx46. Since targeted ablation of Cx46 has been shown to cause senile-type nuclear opacities, it appears that Cx50 alone cannot meet homeostatic requirements. To determine if lens pathology arises from a reduction in levels of communication or the loss of a connexin-specific function, we have generated mice with a targeted deletion of the Cx50 gene. Cx50-nul

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Abraham, Valsamma, Michael L. Chou, Kristine M. DeBolt, and Michael Koval. "Phenotypic control of gap junctional communication by cultured alveolar epithelial cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 276, no. 5 (1999): L825—L834. http://dx.doi.org/10.1152/ajplung.1999.276.5.l825.

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We examined phenotype-specific changes in gap junction protein [connexin (Cx)] expression and function by cultured rat alveolar type II cells. Type II cells cultured on extracellular matrix in medium containing keratinocyte growth factor (KGF) and 2% fetal bovine serum (FBS; KGF/2) retained expression of surfactant protein C and the 180-kDa lamellar body membrane protein (lbm180). These markers were lost when cells were cultured in medium containing 10% FBS (MEM/10). With RT-PCR, cells cultured in MEM/10 showed transient increases in Cx43 and Cx46 mRNA expression, whereas Cx32 and Cx26 decreas

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Bao, Li, Frederick Sachs, and Gerhard Dahl. "Connexins are mechanosensitive." American Journal of Physiology-Cell Physiology 287, no. 5 (2004): C1389—C1395. http://dx.doi.org/10.1152/ajpcell.00220.2004.

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Connexins form gap junction channels that provide a hydrophilic path between cell interiors. Some connexins, particularly the lens connexins, Cx46 and Cx50 and their orthologs, can form functional hemichannels in nonjunctional membranes. These hemichannels are a nonselective conduit to the extracellular medium and may jeopardize cell survival. The physiological function of hemichannels has remained elusive, but it has been postulated that hemichannels are involved in ATP-release caused by mechanical stimulation. Here we show with single-channel and whole cell electrophysiological studies that

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Krintel, Christian, Kasper Harpsøe, Linda G. Zachariassen, et al. "Structural analysis of the positive AMPA receptor modulators CX516 and Me-CX516 in complex with the GluA2 ligand-binding domain." Acta Crystallographica Section D Biological Crystallography 69, no. 9 (2013): 1645–52. http://dx.doi.org/10.1107/s0907444913011839.

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Brady Trexler, E., Feliksas F. Bukauskas, Michael V. L. Bennett, Thaddeus A. Bargiello, and Vytas K. Verselis. "Rapid and Direct Effects of pH on Connexins Revealed by the Connexin46 Hemichannel Preparation." Journal of General Physiology 113, no. 5 (1999): 721–42. http://dx.doi.org/10.1085/jgp.113.5.721.

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pH is a potent modulator of gap junction (GJ) mediated cell–cell communication. Mechanisms proposed for closure of GJ channels by acidification include direct actions of H+ on GJ proteins and indirect actions mediated by soluble intermediates. Here we report on the effects of acidification on connexin (Cx)46 cell–cell channels expressed in Neuro-2a cells and Cx46 hemichannels expressed in Xenopus oocytes. Effects of acidification on hemichannels were examined macroscopically and in excised patches that permitted rapid (&lt;1 ms) and uniform pH changes at the exposed hemichannel face. Both

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Cheng, Catherine, Roberta B. Nowak, Junyuan Gao, et al. "Lens ion homeostasis relies on the assembly and/or stability of large connexin 46 gap junction plaques on the broad sides of differentiating fiber cells." American Journal of Physiology-Cell Physiology 308, no. 10 (2015): C835—C847. http://dx.doi.org/10.1152/ajpcell.00372.2014.

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The eye lens consists of layers of tightly packed fiber cells, forming a transparent and avascular organ that is important for focusing light onto the retina. A microcirculation system, facilitated by a network of gap junction channels composed of connexins 46 and 50 (Cx46 and Cx50), is hypothesized to maintain and nourish lens fiber cells. We measured lens impedance in mice lacking tropomodulin 1 (Tmod1, an actin pointed-end capping protein), CP49 (a lens-specific intermediate filament protein), or both Tmod1 and CP49. We were surprised to find that simultaneous loss of Tmod1 and CP49, which

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37

Verselis, Vytas K., and Miduturu Srinivas. "Divalent Cations Regulate Connexin Hemichannels by Modulating Intrinsic Voltage-dependent Gating." Journal of General Physiology 132, no. 3 (2008): 315–27. http://dx.doi.org/10.1085/jgp.200810029.

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Connexin hemichannels are robustly regulated by voltage and divalent cations. The basis of voltage-dependent gating, however, has been questioned with reports that it is not intrinsic to hemichannels, but rather is derived from divalent cations acting as gating particles that block the pore in a voltage-dependent manner. Previously, we showed that connexin hemichannels possess two types of voltage-dependent gating, termed Vj and loop gating, that in Cx46 operate at opposite voltage polarities, positive and negative, respectively. Using recordings of single Cx46 hemichannels, we found both form

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Rubinos, Clio, Helmuth A. Sánchez, Vytas K. Verselis, and Miduturu Srinivas. "Mechanism of inhibition of connexin channels by the quinine derivative N-benzylquininium." Journal of General Physiology 139, no. 1 (2011): 69–82. http://dx.doi.org/10.1085/jgp.201110678.

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The anti-malarial drug quinine and its quaternary derivative N-benzylquininium (BQ+) have been shown to inhibit gap junction (GJ) channels with specificity for Cx50 over its closely related homologue Cx46. Here, we examined the mechanism of BQ+ action using undocked Cx46 and Cx50 hemichannels, which are more amenable to analyses at the single-channel level. We found that BQ+ (300 µM–1 mM) robustly inhibited Cx50, but not Cx46, hemichannel currents, indicating that the Cx selectivity of BQ+ is preserved in both hemichannel and GJ channel configurations. BQ+ reduced Cx50 hemichannel open probabi

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Pinto, Bernardo I., Amaury Pupo, Isaac Garcia, et al. "Voltage Dependent Inhibition of Cx46 Hemichannels by Calcium." Biophysical Journal 112, no. 3 (2017): 255a. http://dx.doi.org/10.1016/j.bpj.2016.11.1392.

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40

Retamal, Mauricio A., Mariana C. Fiori, Ainoa Fernandez-Olivares, et al. "4-Hydroxynonenal induces Cx46 hemichannel inhibition through its carbonylation." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1865, no. 8 (2020): 158705. http://dx.doi.org/10.1016/j.bbalip.2020.158705.

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Udugama, Maheshi, Elaine Sanij, Hsiao P. J. Voon, et al. "Ribosomal DNA copy loss and repeat instability in ATRX-mutated cancers." Proceedings of the National Academy of Sciences 115, no. 18 (2018): 4737–42. http://dx.doi.org/10.1073/pnas.1720391115.

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ATRX (alpha thalassemia/mental retardation X-linked) complexes with DAXX to deposit histone variant H3.3 into repetitive heterochromatin. Recent genome sequencing studies in cancers have revealed mutations in ATRX and their association with ALT (alternative lengthening of telomeres) activation. Here we report depletion of ATRX in mouse ES cells leads to selective loss in ribosomal RNA gene (rDNA) copy number. Supporting this, ATRX-mutated human ALT-positive tumors also show a substantially lower rDNA copy than ALT-negative tumors. Further investigation shows that the rDNA copy loss and repeat

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Rubinos, Clio, Krista Villone, Pallavi V. Mhaske, Thomas W. White, and Miduturu Srinivas. "Functional effects of Cx50 mutations associated with congenital cataracts." American Journal of Physiology-Cell Physiology 306, no. 3 (2014): C212—C220. http://dx.doi.org/10.1152/ajpcell.00098.2013.

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Mutations in connexin50 (Cx50) cause dominant cataracts in both humans and mice. The exact mechanisms by which mutations cause these variable phenotypes are poorly understood. We have examined the functional properties of gap junctions made by three Cx50 mutations, V44E, D47N, and V79L, expressed in mammalian cell lines. V44E trafficked to the plasma membrane properly and formed gap junctional plaques. However, the mutant did not form functional gap junctions when expressed alone, or with wild-type (WT) Cx46 and Cx50, indicating that V44E is a dominant negative inhibitor of WT connexin functio

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Tong, Jun-Jie, Xiaoqin Liu, Lixian Dong, and Lisa Ebihara. "Exchange of Gating Properties Between Rat Cx46 and Chicken Cx45.6." Biophysical Journal 87, no. 4 (2004): 2397–406. http://dx.doi.org/10.1529/biophysj.104.039594.

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Oh, Seunghoon. "Bisphenol A and 4-tert-Octylphenol Inhibit Cx46 Hemichannel Currents." Korean Journal of Physiology & Pharmacology 19, no. 1 (2015): 73. http://dx.doi.org/10.4196/kjpp.2015.19.1.73.

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45

Mulkearns-Hubert, Erin E., Luke A. Torre-Healy, Daniel J. Silver, et al. "Development of a Cx46 Targeting Strategy for Cancer Stem Cells." Cell Reports 27, no. 4 (2019): 1062–72. http://dx.doi.org/10.1016/j.celrep.2019.03.079.

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46

Pfahnl, Arnold, and G. Dahl. "Gating of cx46 gap junction hemichannels by calcium and voltage." Pfl�gers Archiv European Journal of Physiology 437, no. 3 (1999): 345–53. http://dx.doi.org/10.1007/s004240050788.

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47

Sanches, D. S., C. G. Pires, H. Fukumasu, et al. "Expression of Connexins in Normal and Neoplastic Canine Bone Tissue." Veterinary Pathology 46, no. 5 (2009): 846–59. http://dx.doi.org/10.1354/vp.08-vp-0263-s-fl.

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Previous studies showed that intercellular communication by gap junctions has a role in bone formation. The main connexin involved in the development, differentiation, and regulation of bone tissue is connexin (Cx) 43. In addition, Cx46 is also expressed, mostly localized within the trans-Golgi region. Alterations in the expression pattern and aberrant location of these connexins are associated with oncogenesis, demonstrating a deficient gap junctional intercellular communication (GJIC) capacity in neoplastic tissues. In this study, we evaluated normal and neoplastic bone tissues regarding the

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Verheule, Sander, Marjan J. A. van Kempen, Sjoerd Postma, Martin B. Rook, and Habo J. Jongsma. "Gap junctions in the rabbit sinoatrial node." American Journal of Physiology-Heart and Circulatory Physiology 280, no. 5 (2001): H2103—H2115. http://dx.doi.org/10.1152/ajpheart.2001.280.5.h2103.

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In comparison to the cellular basis of pacemaking, the electrical interactions mediating synchronization and conduction in the sinoatrial node are poorly understood. Therefore, we have taken a combined immunohistochemical and electrophysiological approach to characterize gap junctions in the nodal area. We report that the pacemaker myocytes in the center of the rabbit sinoatrial node express the gap junction proteins connexin (Cx)40 and Cx46. In the periphery of the node, strands of pacemaker myocytes expressing Cx43 intermingle with strands expressing Cx40 and Cx46. Biophysical properties of

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Shakespeare, Teresa I., Caterina Sellitto, Leping Li, et al. "Interaction between Connexin50 and Mitogen-activated Protein Kinase Signaling in Lens Homeostasis." Molecular Biology of the Cell 20, no. 10 (2009): 2582–92. http://dx.doi.org/10.1091/mbc.e08-12-1257.

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Both connexins and signal transduction pathways have been independently shown to play critical roles in lens homeostasis, but little is known about potential cooperation between these two intercellular communication systems. To investigate whether growth factor signaling and gap junctional communication interact during the development of lens homeostasis, we examined the effect of mitogen-activated protein kinase (MAPK) signaling on coupling mediated by specific lens connexins by using a combination of in vitro and in vivo assays. Activation of MAPK signaling pathways significantly increased c

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White, T. W., D. L. Paul, D. A. Goodenough, and R. Bruzzone. "Functional analysis of selective interactions among rodent connexins." Molecular Biology of the Cell 6, no. 4 (1995): 459–70. http://dx.doi.org/10.1091/mbc.6.4.459.

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One consequence of the diversity in gap junction structural proteins is that cells expressing different connexins may come into contact and form intercellular channels that are mixed in connexin content. We have systematically examined the ability of adjacent cells expressing different connexins to communicate, and found that all connexins exhibit specificity in their interactions. Two extreme examples of selectivity were observed. Connexin40 (Cx40) was highly restricted in its ability to make heterotypic channels, functionally interacting with Cx37, but failing to do so when paired with Cx26,

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