Pannexins in the musculoskeletal system: new targets for development and disease progression.

Allen, M. R. & Burr, D. B. in Basic and Applied Bone Biology (eds David B. Burr & Matthew R. Allen) 75–90 (Academic Press, 2014).

Plotkin, L. I. & Bellido, T. Beyond gap junctions: connexin43 and bone cell signaling. Bone 52, 157–166 (2013).

pubmed: 23041511

Stains, J. P. & Civitelli, R. Gap junctions in skeletal development and function. Biochim. Biophys. Acta 1719, 69–81 (2005).

pubmed: 16359941

Bellido, T., Plotkin, L. I. & Bruzzaniti, A. in Basic and Applied Bone Biology (eds David B. Burr & Matthew R. Allen) 27–45 (Academic Press, 2014).

Sáez, J. C., Cisterna, B. A., Vargas, A. & Cardozo, C. P. Regulation of pannexin and connexin channels and their functional role in skeletal muscles. Cell Mol. Life Sci. 72, 2929–2935 (2015).

pubmed: 26084874

Tomei, E. J. & Wolniak, S. M. Kinesin-2 and kinesin-9 have atypical functions during ciliogenesis in the male gametophyte of Marsilea vestita. BMC Cell Biol. 17, 29 (2016).

pubmed: 27421907 pmcid: 4947347

Bhat, E. A. & Sajjad, N. Human Pannexin 1 channel: Insight in structure-function mechanism and its potential physiological roles. Mol. Cell Biochem. 476, 1529–1540 (2021).

pubmed: 33394272

Pelegrin, P. & Surprenant, A. Pannexin-1 mediates large pore formation and interleukin-1beta release by the ATP-gated P2X7 receptor. EMBO J. 25, 5071–5082 (2006).

pubmed: 17036048 pmcid: 1630421

Scemes, E., Suadicani, S. O., Dahl, G. & Spray, D. C. Connexin and pannexin mediated cell-cell communication. Neuron Glia Biol. 3, 199–208 (2007).

pubmed: 18634611 pmcid: 2588549

Alhouayek, M., Sorti, R., Gilthorpe, J. D. & Fowler, C. J. Role of pannexin-1 in the cellular uptake, release and hydrolysis of anandamide by T84 colon cancer cells. Sci. Rep. 9, 7622 (2019).

pubmed: 31110238 pmcid: 6527687

Chekeni, F. B. et al. Pannexin 1 channels mediate ‘find-me’ signal release and membrane permeability during apoptosis. Nature 467, 863–867 (2010).

pubmed: 20944749 pmcid: 3006164

Moorer, M. C. et al. Defective signaling, osteoblastogenesis and bone remodeling in a mouse model of connexin 43 C-terminal truncation. J. Cell Sci. 130, 531–540 (2017).

pubmed: 28049723 pmcid: 5312734

Narahari, A. K. et al. ATP and large signaling metabolites flux through caspase-activated Pannexin 1 channels. Elife 10, e64787 (2021).

pubmed: 33410749 pmcid: 7806264

Pacheco-Costa, R. et al. Defective cancellous bone structure and abnormal response to PTH in cortical bone of mice lacking Cx43 cytoplasmic C-terminus domain. Bone 81, 632–643 (2015).

pubmed: 26409319 pmcid: 4640960

Dubyak, G. R. Both sides now: multiple interactions of ATP with pannexin-1 hemichannels. Focus on “A permeant regulating its permeation pore: inhibition of pannexin 1 channels by ATP”. Am. J. Physiol. Cell Physiol. 296, C235–C241 (2009).

pubmed: 19179656 pmcid: 2643857

Panchin, Y. V. Evolution of gap junction proteins–the pannexin alternative. J. Exp. Biol. 208, 1415–1419 (2005).

pubmed: 15802665

Panchin, Y. et al. A ubiquitous family of putative gap junction molecules. Curr. Biol. 10, R473–R474 (2000).

pubmed: 10898987

Donahue, H. J., Qu, R. W. & Genetos, D. C. Joint diseases: from connexins to gap junctions. Nat. Rev. Rheumatol. 14, 42–51 (2017).

pubmed: 29255213

Bond, S. R. et al. Pannexin 3 is a novel target for Runx2, expressed by osteoblasts and mature growth plate chondrocytes. J. Bone Min. Res. 26, 2911–2922 (2011).

Penuela, S. et al. Pannexin 1 and pannexin 3 are glycoproteins that exhibit many distinct characteristics from the connexin family of gap junction proteins. J. Cell Sci. 120, 3772–3783 (2007).

pubmed: 17925379

Xiao, Z. et al. Analysis of the extracellular matrix vesicle proteome in mineralizing osteoblasts. J. Cell Physiol. 210, 325–335 (2007).

pubmed: 17096383

Baranova, A. et al. The mammalian pannexin family is homologous to the invertebrate innexin gap junction proteins. Genomics 83, 706–716 (2004).

pubmed: 15028292

Harber, P. & McCoy, J. M. Predicate calculus, artificial intelligence, and workers’ compensation. J. Occup. Med. 31, 484–489 (1989).

pubmed: 2523962

Riquelme, M. A. et al. The ATP required for potentiation of skeletal muscle contraction is released via pannexin hemichannels. Neuropharmacology 75, 594–603 (2013).

pubmed: 23583931

Langlois, S. et al. Pannexin 1 and pannexin 3 channels regulate skeletal muscle myoblast proliferation and differentiation. J. Biol. Chem. 289, 30717–30731 (2014).

pubmed: 25239622 pmcid: 4215249

Buvinic, S. et al. ATP released by electrical stimuli elicits calcium transients and gene expression in skeletal muscle. J. Biol. Chem. 284, 34490–34505 (2009).

pubmed: 19822518 pmcid: 2787310

Cea, L. A. et al. De novo expression of connexin hemichannels in denervated fast skeletal muscles leads to atrophy. Proc. Natl. Acad. Sci. USA 110, 16229–16234 (2013).

pubmed: 24043768 pmcid: 3791696

Kanjanamekanant, K., Luckprom, P. & Pavasant, P. P2X7 receptor-Pannexin1 interaction mediates stress-induced interleukin-1 beta expression in human periodontal ligament cells. J. Periodontal. Res. 49, 595–602 (2014).

pubmed: 24219423

Vogt, A., Hormuzdi, S. G. & Monyer, H. Pannexin1 and Pannexin2 expression in the developing and mature rat brain. Brain Res. Mol. Brain Res. 141, 113–120 (2005).

pubmed: 16143426

Ishikawa, M. et al. Pannexin 3 functions as an ER Ca

pubmed: 21690309 pmcid: 3216329

Iwamoto, T. et al. Pannexin 3 regulates proliferation and differentiation of odontoblasts via its hemichannel activities. PLoS One 12, e0177557 (2017).

pubmed: 28494020 pmcid: 5426780

Le Vasseur, M., Lelowski, J., Bechberger, J. F., Sin, W. C. & Naus, C. C. Pannexin 2 protein expression is not restricted to the CNS. Front. Cell Neurosci. 8, 392 (2014).

pubmed: 25505382 pmcid: 4243559

Pillon, N. J. et al. Nucleotides released from palmitate-challenged muscle cells through pannexin-3 attract monocytes. Diabetes 63, 3815–3826 (2014).

pubmed: 24917574

Deng, Z. et al. Cryo-EM structures of the ATP release channel pannexin 1. Nat. Struct. Mol. Biol. 27, 373–381 (2020).

pubmed: 32231289

Jin, Q. et al. Cryo-EM structures of human pannexin 1 channel. Cell Res. 30, 449–451 (2020).

pubmed: 32246089 pmcid: 7196119

Michalski, K. et al. The Cryo-EM structure of pannexin 1 reveals unique motifs for ion selection and inhibition. Elife 9, e54670 (2020).

pubmed: 32048993 pmcid: 7108861

Mou, L. et al. Structural basis for gating mechanism of Pannexin 1 channel. Cell Res. 30, 452–454 (2020).

pubmed: 32284561 pmcid: 7196076

Qu, R. et al. Cryo-EM structure of human heptameric Pannexin 1 channel. Cell Res. 30, 446–448 (2020).

pubmed: 32203128 pmcid: 7196123

Ruan, Z., Orozco, I. J., Du, J. & Lu, W. Structures of human pannexin 1 reveal ion pathways and mechanism of gating. Nature 584, 646–651 (2020).

pubmed: 32494015 pmcid: 7814660

Ambrosi, C. et al. Pannexin1 and Pannexin2 channels show quaternary similarities to connexons and different oligomerization numbers from each other. J. Biol. Chem. 285, 24420–24431 (2010).

pubmed: 20516070 pmcid: 2915678

Zhang, H. et al. Cryo-EM structure of human heptameric pannexin 2 channel. Nat. Commun. 14, 1118 (2023).

pubmed: 36869038 pmcid: 9984531

Kawate, T. & Gouaux, E. Fluorescence-detection size-exclusion chromatography for precrystallization screening of integral membrane proteins. Structure 14, 673–681 (2006).

pubmed: 16615909

Milks, L. C., Kumar, N. M., Houghten, R., Unwin, N. & Gilula, N. B. Topology of the 32-kd liver gap junction protein determined by site-directed antibody localizations. EMBO J. 7, 2967–2975 (1988).

pubmed: 2460334 pmcid: 454678

Yeager, M. & Gilula, N. B. Membrane topology and quaternary structure of cardiac gap junction ion channels. J. Mol. Biol. 223, 929–948 (1992).

pubmed: 1371548

Beckmann, A., Grissmer, A., Krause, E., Tschernig, T. & Meier, C. Pannexin-1 channels show distinct morphology and no gap junction characteristics in mammalian cells. Cell Tissue Res. 363, 751–763 (2016).

pubmed: 26386583

Huang, Y., Grinspan, J. B., Abrams, C. K. & Scherer, S. S. Pannexin1 is expressed by neurons and glia but does not form functional gap junctions. Glia 55, 46–56 (2007).

pubmed: 17009242

Wang, N. et al. Connexin targeting peptides as inhibitors of voltage- and intracellular Ca

pubmed: 24007825

Wang, N. et al. Paracrine signaling through plasma membrane hemichannels. Biochim. Biophys. Acta 1828, 35–50 (2013).

pubmed: 22796188

Weinger, J. M. & Holtrop, M. E. An ultrastructural study of bone cells: the occurrence of microtubules, microfilaments and tight junctions. Calcif. Tissue Res. 14, 15–29 (1974).

pubmed: 4820235

Bruzzone, R., Hormuzdi, S. G., Barbe, M. T., Herb, A. & Monyer, H. Pannexins, a family of gap junction proteins expressed in brain. Proc. Natl. Acad. Sci. USA 100, 13644–13649 (2003).

pubmed: 14597722 pmcid: 263867

Ishikawa, M. et al. Pannexin 3 and connexin 43 modulate skeletal development through their distinct functions and expression patterns. J. Cell Sci. 129, 1018–1030 (2016).

pubmed: 26759176 pmcid: 4813316

Cooreman, A. et al. Connexin and pannexin (hemi)channels: emerging targets in the treatment of liver disease. Hepatology 69, 1317–1323 (2019).

pubmed: 30300925

Vinken, M. et al. Connexins and their channels in cell growth and cell death. Cell Signal 18, 592–600 (2006).

pubmed: 16183253

Flores, J. A. et al. Connexin-46/50 in a dynamic lipid environment resolved by CryoEM at 1.9 A. Nat. Commun. 11, 4331 (2020).

pubmed: 32859914 pmcid: 7455559

Lee, H. J. et al. Cryo-EM structure of human Cx31.3/GJC3 connexin hemichannel. Sci. Adv. 6, eaba4996 (2020).

pubmed: 32923625 pmcid: 7455182

Maeda, S. et al. Structure of the connexin 26 gap junction channel at 3.5 A resolution. Nature 458, 597–602 (2009).

pubmed: 19340074

Myers, J. B. et al. Structure of native lens connexin 46/50 intercellular channels by cryo-EM. Nature 564, 372–377 (2018).

pubmed: 30542154 pmcid: 6309215

Unger, V. M., Kumar, N. M., Gilula, N. B. & Yeager, M. Three-dimensional structure of a recombinant gap junction membrane channel. Science 283, 1176–1180 (1999).

pubmed: 10024245

Bhaskaracharya, A. et al. Probenecid blocks human P2X7 receptor-induced dye uptake via a pannexin-1 independent mechanism. PLoS ONE 9, e93058 (2014).

pubmed: 24671093 pmcid: 3966854

Chiu, Y. H., Schappe, M. S., Desai, B. N. & Bayliss, D. A. Revisiting multimodal activation and channel properties of Pannexin 1. J. Gen. Physiol. 150, 19–39 (2018).

pubmed: 29233884 pmcid: 5749114

Iwamoto, T. et al. Pannexin 3 regulates intracellular ATP/cAMP levels and promotes chondrocyte differentiation. J. Biol. Chem. 285, 18948–18958 (2010).

pubmed: 20404334 pmcid: 2881817

Ma, W., Hui, H., Pelegrin, P. & Surprenant, A. Pharmacological characterization of pannexin-1 currents expressed in mammalian cells. J. Pharm. Exp. Ther. 328, 409–418 (2009).

Li, S., Bjelobaba, I. & Stojilkovic, S. S. Interactions of Pannexin1 channels with purinergic and NMDA receptor channels. Biochim. Biophys. Acta Biomembr. 1860, 166–173 (2018).

pubmed: 28389204

Velasquez, S. & Eugenin, E. A. Role of Pannexin-1 hemichannels and purinergic receptors in the pathogenesis of human diseases. Front. Physiol. 5, 96 (2014).

pubmed: 24672487 pmcid: 3953678

Silverman, W. R. et al. The pannexin 1 channel activates the inflammasome in neurons and astrocytes. J. Biol. Chem. 284, 18143–18151 (2009).

pubmed: 19416975 pmcid: 2709345

Locovei, S., Wang, J. & Dahl, G. Activation of pannexin 1 channels by ATP through P2Y receptors and by cytoplasmic calcium. FEBS Lett. 580, 239–244 (2006).

pubmed: 16364313

Prochnow, N. et al. Pannexin1 stabilizes synaptic plasticity and is needed for learning. PLoS One 7, e51767 (2012).

pubmed: 23284764 pmcid: 3527502

Burboa, P. C., Puebla, M., Gaete, P. S., Duran, W. N. & Lillo, M. A. Connexin and pannexin large-pore channels in microcirculation and neurovascular coupling function. Int. J. Mol. Sci. 23, 7303 (2022).

pubmed: 35806312 pmcid: 9266979

Qu, Y. et al. Pannexin-1 is required for ATP release during apoptosis but not for inflammasome activation. J. Immunol. 186, 6553–6561 (2011).

pubmed: 21508259

Kanneganti, T. D. et al. Pannexin-1-mediated recognition of bacterial molecules activates the cryopyrin inflammasome independent of Toll-like receptor signaling. Immunity 26, 433–443 (2007).

pubmed: 17433728

Seminario-Vidal, L. et al. Rho signaling regulates pannexin 1-mediated ATP release from airway epithelia. J. Biol. Chem. 286, 26277–26286 (2011).

pubmed: 21606493 pmcid: 3143590

Phelan, P. Innexins: members of an evolutionarily conserved family of gap-junction proteins. Biochim. Biophys. Acta 1711, 225–245 (2005).

pubmed: 15921654

Berendsen, A. D. & Olsen, B. R. Bone development. Bone 80, 14–18 (2015).

pubmed: 26453494 pmcid: 4602167

Yang, L., Tsang, K. Y., Tang, H. C., Chan, D. & Cheah, K. S. Hypertrophic chondrocytes can become osteoblasts and osteocytes in endochondral bone formation. Proc. Natl. Acad. Sci. USA 111, 12097–12102 (2014).

pubmed: 25092332 pmcid: 4143064

Cheung, W. Y. et al. Pannexin-1 and P2X7-receptor are required for apoptotic osteocytes in fatigued bone to trigger RANKL production in neighboring bystander osteocytes. J. Bone Min. Res. 31, 890–899 (2016).

Caskenette, D. et al. Global deletion of Panx3 produces multiple phenotypic effects in mouse humeri and femora. J. Anat. 228, 746–756 (2016).

pubmed: 26749194 pmcid: 4831336

Shao, Q. et al. A germline variant in the PANX1 gene has reduced channel function and is associated with multisystem dysfunction. J. Biol. Chem. 291, 12432–12443 (2016).

pubmed: 27129271 pmcid: 4933456

Ishikawa, M., Iwamoto, T., Fukumoto, S. & Yamada, Y. Pannexin 3 inhibits proliferation of osteoprogenitor cells by regulating Wnt and p21 signaling. J. Biol. Chem. 289, 2839–2851 (2014).

pubmed: 24338011

Delgado-Calle, J. & Bellido, T. Osteocytes and skeletal pathophysiology. Curr. Mol. Biol. Rep. 1, 157–167 (2015).

pubmed: 26693137 pmcid: 4673661

Aguirre, J. I. et al. Osteocyte apoptosis is induced by weightlessness in mice and precedes osteoclast recruitment and bone loss. J. Bone Min. Res. 21, 605–615 (2006).

Delgado-Calle, J. & Bellido, T. The osteocyte as a signaling cell. Physiol. Rev. 102, 379–410 (2022).

pubmed: 34337974

Emerton, K. B. et al. Osteocyte apoptosis and control of bone resorption following ovariectomy in mice. Bone 46, 577–583 (2010).

pubmed: 19925896

Kennedy, O. D. et al. Activation of resorption in fatigue-loaded bone involves both apoptosis and active pro-osteoclastogenic signaling by distinct osteocyte populations. Bone 50, 1115–1122 (2012).

pubmed: 22342796 pmcid: 3366436

Kennedy, O. D., Laudier, D. M., Majeska, R. J., Sun, H. B. & Schaffler, M. B. Osteocyte apoptosis is required for production of osteoclastogenic signals following bone fatigue in vivo. Bone 64, 132–137 (2014).

pubmed: 24709687 pmcid: 4070223

Bakker, A., Klein-Nulend, J. & Burger, E. Shear stress inhibits while disuse promotes osteocyte apoptosis. Biochem. Biophys. Res. Commun. 320, 1163–1168 (2004).

pubmed: 15249211

Noble, B. Bone microdamage and cell apoptosis. Eur. Cell Mater. 6, 46–55 (2003). discusssion 55.

pubmed: 14710370

Tomkinson, A., Gevers, E. F., Wit, J. M., Reeve, J. & Noble, B. S. The role of estrogen in the control of rat osteocyte apoptosis. J. Bone Min. Res. 13, 1243–1250 (1998).

Verborgt, O., Gibson, G. J. & Schaffler, M. B. Loss of osteocyte integrity in association with microdamage and bone remodeling after fatigue in vivo. J. Bone Min. Res. 15, 60–67 (2000).

McCutcheon, S., Majeska, R. J., Spray, D. C., Schaffler, M. B. & Vazquez, M. Apoptotic osteocytes induce RANKL production in bystanders via purinergic signaling and activation of pannexin channels. J. Bone Min. Res. 35, 966–977 (2020).

Liu, W. et al. TGF-beta1 facilitates cell-cell communication in osteocytes via connexin43- and pannexin1-dependent gap junctions. Cell Death Discov. 5, 141 (2019).

pubmed: 31666990 pmcid: 6814792

Aguilar-Perez, A. et al. Age- and sex-dependent role of osteocytic pannexin1 on bone and muscle mass and strength. Sci. Rep. 9, 13903 (2019).

pubmed: 31554905 pmcid: 6761284

Courvoisier, A., Sailhan, F., Laffenetre, O. & Obert, L., French Study Group of, B. M. P. i. O. S. Bone morphogenetic protein and orthopaedic surgery: can we legitimate its off-label use? Int. Orthop. 38, 2601–2605 (2014).

pubmed: 25267430

Kalitina, T. A. [Survival of Coxsackie viruses of group B 3 and 5 serotypes in sausage meat]. Vopr. Pitan. 25, 74–77 (1966).

pubmed: 6000303

Song, K. et al. Identification of a key residue mediating bone morphogenetic protein (BMP)-6 resistance to noggin inhibition allows for engineered BMPs with superior agonist activity. J. Biol. Chem. 285, 12169–12180 (2010).

pubmed: 20048150 pmcid: 2852956

Wang, L. et al. Bone formation induced by BMP-2 in human osteosarcoma cells. Int. J. Oncol. 43, 1095–1102 (2013).

pubmed: 23900689 pmcid: 3829777

Takeno, A., Kanazawa, I., Tanaka, K. I., Notsu, M. & Sugimoto, T. Phloretin suppresses bone morphogenetic protein-2-induced osteoblastogenesis and mineralization via inhibition of phosphatidylinositol 3-kinases/Akt pathway. Int. J. Mol. Sci. 20, 2481 (2019).

pubmed: 31137461 pmcid: 6566987

Ghosh-Choudhury, N. et al. c-Abl-dependent molecular circuitry involving Smad5 and phosphatidylinositol 3-kinase regulates bone morphogenetic protein-2-induced osteogenesis. J. Biol. Chem. 288, 24503–24517 (2013).

pubmed: 23821550 pmcid: 3750149

Mukherjee, A., Wilson, E. M. & Rotwein, P. Selective signaling by Akt2 promotes bone morphogenetic protein 2-mediated osteoblast differentiation. Mol. Cell Biol. 30, 1018–1027 (2010).

pubmed: 19995912

Sun, M. et al. Effects of matrix stiffness on the morphology, adhesion, proliferation and osteogenic differentiation of mesenchymal stem cells. Int. J. Med. Sci. 15, 257–268 (2018).

pubmed: 29483817 pmcid: 5820855

Afzal, F. et al. Smad function and intranuclear targeting share a Runx2 motif required for osteogenic lineage induction and BMP2 responsive transcription. J. Cell Physiol. 204, 63–72 (2005).

pubmed: 15573378

Zaidi, S. K. et al. Integration of Runx and Smad regulatory signals at transcriptionally active subnuclear sites. Proc. Natl. Acad. Sci. USA 99, 8048–8053 (2002).

pubmed: 12060751 pmcid: 123018

Lohman, A. W. et al. Expression of pannexin isoforms in the systemic murine arterial network. J. Vasc. Res. 49, 405–416 (2012).

pubmed: 22739252

Plotkin, L. I. & Stains, J. P. Connexins and pannexins in the skeleton: gap junctions, hemichannels and more. Cell Mol. Life Sci. 72, 2853–2867 (2015).

pubmed: 26091748 pmcid: 4503509

Rauch, A. et al. Glucocorticoids suppress bone formation by attenuating osteoblast differentiation via the monomeric glucocorticoid receptor. Cell Metab. 11, 517–531 (2010).

pubmed: 20519123

Song, F., Sun, H., Huang, L., Fu, D. & Huang, C. The role of Pannexin3-modified human dental pulp-derived mesenchymal stromal cells in repairing rat cranial critical-sized bone defects. Cell Physiol. Biochem. 44, 2174–2188 (2017).

pubmed: 29241211

Tomita, M., Reinhold, M. I., Molkentin, J. D. & Naski, M. C. Calcineurin and NFAT4 induce chondrogenesis. J. Biol. Chem. 277, 42214–42218 (2002).

pubmed: 12239209

Beals, C. R., Clipstone, N. A., Ho, S. N. & Crabtree, G. R. Nuclear localization of NF-ATc by a calcineurin-dependent, cyclosporin-sensitive intramolecular interaction. Genes Dev. 11, 824–834 (1997).

pubmed: 9106655

Esseltine, J. L. & Laird, D. W. Next-generation connexin and pannexin cell biology. Trends Cell Biol. 26, 944–955 (2016).

pubmed: 27339936

Koga, T. et al. NFAT and osterix cooperatively regulate bone formation. Nat. Med. 11, 880–885 (2005).

pubmed: 16041384

Nakashima, K. et al. The novel zinc finger-containing transcription factor osterix is required for osteoblast differentiation and bone formation. Cell 108, 17–29 (2002).

pubmed: 11792318

Ishikawa, M. et al. Pannexin 3 ER Ca

pubmed: 31822768 pmcid: 6904572

Boyden, L. M. et al. High bone density due to a mutation in LDL-receptor-related protein 5. N. Engl. J. Med. 346, 1513–1521 (2002).

pubmed: 12015390

Guntur, A. R. & Rosen, C. J. Bone as an endocrine organ. Endocr. Pr. 18, 758–762 (2012).

Cheung, W. Y. et al. in Journal Of Bone And Mineral Research. S288-S288 (WILEY-BLACKWELL 111 RIVER ST, HOBOKEN 07030-5774, NJ USA).

Deosthale, P. et al. Sex-specific differences in direct osteoclastic versus indirect osteoblastic effects underlay the low bone mass of Pannexin1 deletion in TRAP-expressing cells in mice. Bone Rep. 16, 101164 (2022).

pubmed: 35028339 pmcid: 8739454

Oh, S. K. et al. Pannexin 3 is required for normal progression of skeletal development in vertebrates. FASEB J. 29, 4473–4484 (2015).

pubmed: 26183770

Bond, S. R., Abramyan, J., Fu, K., Naus, C. C. & Richman, J. M. Pannexin 3 is required for late stage bone growth but not for initiation of ossification in avian embryos. Dev. Dyn. 245, 913–924 (2016).

pubmed: 27295565 pmcid: 5006391

Charge, S. B. & Rudnicki, M. A. Cellular and molecular regulation of muscle regeneration. Physiol. Rev. 84, 209–238 (2004).

pubmed: 14715915

Riquelme, M. A. et al. Pannexin channels mediate the acquisition of myogenic commitment in C2C12 reserve cells promoted by P2 receptor activation. Front. Cell Dev. Biol. 3, 25 (2015).

pubmed: 26000275 pmcid: 4422085

Jorquera, G. et al. Cav1.1 controls frequency-dependent events regulating adult skeletal muscle plasticity. J. Cell Sci. 126, 1189–1198 (2013).

pubmed: 23321639

Rose, A. J., Alsted, T. J., Kobbero, J. B. & Richter, E. A. Regulation and function of Ca

pubmed: 17272343 pmcid: 2075445

Suarez-Berumen, K. et al. Pannexin 1 regulates skeletal muscle regeneration by promoting bleb-based myoblast migration and fusion through a novel lipid based signaling mechanism. Front. Cell Dev. Biol. 9, 736813 (2021).

pubmed: 34676213 pmcid: 8523994

Freeman, E. et al. Sex-dependent role of Pannexin 1 in regulating skeletal muscle and satellite cell function. J. Cell Physiol. 237, 3944–3959 (2022).

pubmed: 35938715

Martel-Pelletier, J. et al. Osteoarthritis. Nat. Rev. Dis. Prim. 2, 16072 (2016).

pubmed: 27734845

Glyn-Jones, S. et al. Osteoarthritis. Lancet 386, 376–387 (2015).

pubmed: 25748615

Jiang, Y. Osteoarthritis year in review 2021: biology. Osteoarthr. Cartil. 30, 207–215 (2022).

Appleton, C. T., Pitelka, V., Henry, J. & Beier, F. Global analyses of gene expression in early experimental osteoarthritis. Arthritis Rheum. 56, 1854–1868 (2007).

pubmed: 17530714

O’Donnell, B. L. & Penuela, S. Pannexin 3 channels in health and disease. Purinergic Signal 17, 577–589 (2021).

pubmed: 34250568 pmcid: 8677855

Moon, P. M. et al. Deletion of Panx3 prevents the development of surgically induced osteoarthritis. J. Mol. Med. 93, 845–856 (2015).

pubmed: 26138248

Moon, P. M. et al. Global deletion of Pannexin 3 resulting in accelerated development of aging-induced osteoarthritis in mice. Arthritis Rheumatol. 73, 1178–1188 (2021).

pubmed: 33426805

Xiao, J., Li, Y., Zhang, J., Xu, G. & Zhang, J. Pannexin 3 activates P2X7 receptor to mediate inflammation and cartilage matrix degradation in temporomandibular joint osteoarthritis. Cell Biol. Int. 47, 1183–1197 (2023).

pubmed: 37021698

Francisco, V. et al. A new immunometabolic perspective of intervertebral disc degeneration. Nat. Rev. Rheumatol. 18, 47–60 (2022).

pubmed: 34845360

Serjeant, M. et al. The role of Panx3 in age-associated and injury-induced intervertebral disc degeneration. Int. J. Mol. Sci. 22, 1080 (2021).

pubmed: 33499145 pmcid: 7865929

Liu, N. et al. microRNA-206 promotes skeletal muscle regeneration and delays progression of Duchenne muscular dystrophy in mice. J. Clin. Invest. 122, 2054–2065 (2012).

pubmed: 22546853 pmcid: 3366415

McNally, E. M. & Pytel, P. Muscle diseases: the muscular dystrophies. Annu. Rev. Pathol. 2, 87–109 (2007).

pubmed: 18039094

Arias-Calderon, M. et al. Characterization of a multiprotein complex involved in excitation-transcription coupling of skeletal muscle. Skelet. Muscle 6, 15 (2016).

pubmed: 27069569 pmcid: 4827232

Cea, L. A. et al. Fast skeletal myofibers of MDX mouse, model of Duchenne muscular dystrophy, express connexin hemichannels that lead to apoptosis. Cell Mol. Life Sci. 73, 2583–2599 (2016).

pubmed: 26803842

Valladares, D. et al. Electrical stimuli are anti-apoptotic in skeletal muscle via extracellular ATP. Alteration of this signal in Mdx mice is a likely cause of dystrophy. PLoS One 8, e75340 (2013).

pubmed: 24282497 pmcid: 3839923

Pham, T. L. et al. Expression of Pannexin 1 and Pannexin 3 during skeletal muscle development, regeneration, and Duchenne muscular dystrophy. J. Cell Physiol. 233, 7057–7070 (2018).

pubmed: 29744875

An, S. et al. Connexin43 in musculoskeletal system: new targets for development and disease progression. Aging Dis. 13, 1715–1732 (2022).

pubmed: 36465186 pmcid: 9662276

Lohman, A. W. & Isakson, B. E. Differentiating connexin hemichannels and pannexin channels in cellular ATP release. FEBS Lett. 588, 1379–1388 (2014).

pubmed: 24548565 pmcid: 3996918

Brigid Hogan, R. B. Manipulating the mouse embryo. a laboratory manual, 2nd Edition. Genet. Res. 66, 296–300 (1994).

Lecanda, F. et al. Connexin43 deficiency causes delayed ossification, craniofacial abnormalities, and osteoblast dysfunction. J. Cell Biol. 151, 931–944 (2000).

pubmed: 11076975 pmcid: 2169447

Ishikawa, M. & Yamada, Y. The role of Pannexin 3 in bone biology. J. Dent. Res. 96, 372–379 (2017).

pubmed: 27837015

Lengner, C. J. et al. Osteoblast differentiation and skeletal development are regulated by Mdm2-p53 signaling. J. Cell Biol. 172, 909–921 (2006).

pubmed: 16533949 pmcid: 2063734

Uribe, P. et al. Soluble silica stimulates osteogenic differentiation and gap junction communication in human dental follicle cells. Sci. Rep. 10, 9923 (2020).

pubmed: 32555274 pmcid: 7303172

van der Heyden, M. A. et al. Identification of connexin43 as a functional target for Wnt signalling. J. Cell Sci. 111, 1741–1749 (1998).

pubmed: 9601103

Lohman, A. W. et al. Pannexin 1 channels regulate leukocyte emigration through the venous endothelium during acute inflammation. Nat. Commun. 6, 7965 (2015).

pubmed: 26242575 pmcid: 4824045

Wang, J., Ma, M., Locovei, S., Keane, R. W. & Dahl, G. Modulation of membrane channel currents by gap junction protein mimetic peptides: size matters. Am. J. Physiol. Cell Physiol. 293, C1112–C1119 (2007).

pubmed: 17652431

Weilinger, N. L., Tang, P. L. & Thompson, R. J. Anoxia-induced NMDA receptor activation opens pannexin channels via Src family kinases. J. Neurosci. 32, 12579–12588 (2012).

pubmed: 22956847 pmcid: 6621249

Plotkin, L. I. et al. Connexin 43 is required for the anti-apoptotic effect of bisphosphonates on osteocytes and osteoblasts in vivo. J. Bone Min. Res. 23, 1712–1721 (2008).

Poornima, V., Vallabhaneni, S., Mukhopadhyay, M. & Bera, A. K. Nitric oxide inhibits the pannexin 1 channel through a cGMP-PKG dependent pathway. Nitric Oxide 47, 77–84 (2015).

pubmed: 25917852

Dobrowolski, R., Sommershof, A. & Willecke, K. Some oculodentodigital dysplasia-associated Cx43 mutations cause increased hemichannel activity in addition to deficient gap junction channels. J. Membr. Biol. 219, 9–17 (2007).

pubmed: 17687502

Esseltine, J. L. et al. Connexin43 mutant patient-derived induced pluripotent stem cells exhibit altered differentiation potential. J. Bone Min. Res. 32, 1368–1385 (2017).

Katz, J. N., Arant, K. R. & Loeser, R. F. Diagnosis and treatment of hip and knee osteoarthritis: a review. JAMA 325, 568–578 (2021).

pubmed: 33560326 pmcid: 8225295

Hochberg, M. C. Serious joint-related adverse events in randomized controlled trials of anti-nerve growth factor monoclonal antibodies. Osteoarthr. Cartil. 23, S18–S21 (2015).

van der Kraan, P. M. & van den Berg, W. B. Chondrocyte hypertrophy and osteoarthritis: role in initiation and progression of cartilage degeneration? Osteoarthr. Cartil. 20, 223–232 (2012).

Billaud, M. et al. Pannexin1 regulates alpha1-adrenergic receptor- mediated vasoconstriction. Circ. Res. 109, 80–85 (2011).

pubmed: 21546608 pmcid: 3135971

Masuda, T. et al. Dorsal horn neurons release extracellular ATP in a VNUT-dependent manner that underlies neuropathic pain. Nat. Commun. 7, 12529 (2016).

pubmed: 27515581 pmcid: 4990655

Conesa-Buendia, F. M. et al. Tenofovir causes bone loss via decreased bone formation and increased bone resorption, which can be counteracted by dipyridamole in mice. J. Bone Min. Res. 34, 923–938 (2019).

Hirata, H. et al. Connexin 39.9 protein is necessary for coordinated activation of slow-twitch muscle and normal behavior in zebrafish. J. Biol. Chem. 287, 1080–1089 (2012).

pubmed: 22075003

Naus, C. C. & Giaume, C. Bridging the gap to therapeutic strategies based on connexin/pannexin biology. J. Transl. Med. 14, 330 (2016).

pubmed: 27899102 pmcid: 5129631

Dahl, G., Qiu, F. & Wang, J. The bizarre pharmacology of the ATP release channel pannexin1. Neuropharmacology 75, 583–593 (2013).

pubmed: 23499662

Bruzzone, R., Barbe, M. T., Jakob, N. J. & Monyer, H. Pharmacological properties of homomeric and heteromeric pannexin hemichannels expressed in Xenopus oocytes. J. Neurochem. 92, 1033–1043 (2005).

pubmed: 15715654

Molica, F. et al. Selective inhibition of Panx1 channels decreases hemostasis and thrombosis in vivo. Thromb. Res. 183, 56–62 (2019).

pubmed: 31669824

Michalski, K. & Kawate, T. Carbenoxolone inhibits Pannexin1 channels through interactions in the first extracellular loop. J. Gen. Physiol. 147, 165–174 (2016).

pubmed: 26755773 pmcid: 4727946

Freeman, T. J. et al. Inhibition of Pannexin 1 reduces the tumorigenic properties of human melanoma cells. Cancers 11, 102 (2019).

pubmed: 30654593 pmcid: 6356688

Chen, K. W., Demarco, B. & Broz, P. Pannexin-1 promotes NLRP3 activation during apoptosis but is dispensable for canonical or noncanonical inflammasome activation. Eur. J. Immunol. 50, 170–177 (2020).

pubmed: 31411729

Jankowski, J. et al. Epithelial and endothelial pannexin1 channels mediate AKI. J. Am. Soc. Nephrol. 29, 1887–1899 (2018).

pubmed: 29866797 pmcid: 6050932

Sharma, A. K. et al. Pannexin-1 channels on endothelial cells mediate vascular inflammation during lung ischemia-reperfusion injury. Am. J. Physiol. Lung Cell Mol. Physiol. 315, L301–L312 (2018).

pubmed: 29745255 pmcid: 6139659

Furukawa, M., Matsueda, M. & Takagai, Y. Ultrasonic mist generation assist argon-nitrogen mix gas effect on radioactive strontium quantification by online solid-phase extraction with inductively coupled plasma mass spectrometry. Anal. Sci. 34, 471–476 (2018).

pubmed: 29563355

Feig, J. L. et al. The antiviral drug tenofovir, an inhibitor of Pannexin-1-mediated ATP release, prevents liver and skin fibrosis by downregulating adenosine levels in the liver and skin. PLoS One 12, e0188135 (2017).

pubmed: 29145453 pmcid: 5690602

Davidson, J. S. & Baumgarten, I. M. Glycyrrhetinic acid derivatives: a novel class of inhibitors of gap-junctional intercellular communication. Structure-activity relationships. J. Pharm. Exp. Ther. 246, 1104–1107 (1988).

Davidson, J. S., Baumgarten, I. M. & Harley, E. H. Reversible inhibition of intercellular junctional communication by glycyrrhetinic acid. Biochem. Biophys. Res. Commun. 134, 29–36 (1986).

pubmed: 3947327

Goldberg, G. S. et al. Evidence that disruption of connexon particle arrangements in gap junction plaques is associated with inhibition of gap junctional communication by a glycyrrhetinic acid derivative. Exp. Cell Res. 222, 48–53 (1996).

pubmed: 8549672

Guan, X., Wilson, S., Schlender, K. K. & Ruch, R. J. Gap-junction disassembly and connexin 43 dephosphorylation induced by 18 beta-glycyrrhetinic acid. Mol. Carcinog. 16, 157–164 (1996).

pubmed: 8688151

Armanini, D., Karbowiak, I., Krozowski, Z., Funder, J. W. & Adam, W. R. The mechanism of mineralocorticoid action of carbenoxolone. Endocrinology 111, 1683–1686 (1982).

pubmed: 6290195

Kuzuya, M. et al. Structures of human pannexin-1 in nanodiscs reveal gating mediated by dynamic movement of the N terminus and phospholipids. Sci. Signal 15, eabg6941 (2022).

pubmed: 35133866

Willebrords, J., Maes, M., Crespo Yanguas, S. & Vinken, M. Inhibitors of connexin and pannexin channels as potential therapeutics. Pharm. Ther. 180, 144–160 (2017).

Chen, X., Yuan, S., Mi, L., Long, Y. & He, H. Pannexin1: insight into inflammatory conditions and its potential involvement in multiple organ dysfunction syndrome. Front. Immunol. 14, 1217366 (2023).

pubmed: 37711629 pmcid: 10498923

Grek, C. L. et al. Targeting connexin 43 with alpha-connexin carboxyl-terminal (ACT1) peptide enhances the activity of the targeted inhibitors, tamoxifen and lapatinib, in breast cancer: clinical implication for ACT1. BMC Cancer 15, 296 (2015).

pubmed: 25881004 pmcid: 4407347

Caufriez, A. et al. Determination of structural features that underpin the pannexin1 channel inhibitory activity of the peptide

pubmed: 37210827

Zhang, Y., Sun, Y., Wang, Z. & Huang, L. Fluorescein-5-thiosemicarbazide as a probe for directly imaging of mucin-type O-linked glycoprotein within living cells. Glycoconj. J. 29, 445–452 (2012).

pubmed: 22797904

Boassa, D., Nguyen, P., Hu, J., Ellisman, M. H. & Sosinsky, G. E. Pannexin2 oligomers localize in the membranes of endosomal vesicles in mammalian cells while Pannexin1 channels traffic to the plasma membrane. Front. Cell Neurosci. 8, 468 (2014).

pubmed: 25698922

Hedskog, L. et al. Modulation of the endoplasmic reticulum-mitochondria interface in Alzheimer’s disease and related models. Proc. Natl. Acad. Sci. USA 110, 7916–7921 (2013).

pubmed: 23620518 pmcid: 3651455

Yang, Y., Wang, L., Chen, L. & Li, L. Pannexin-2, a novel mitochondrial-associated membrane protein, may become the new strategy to treat and prevent neurological disorders. Acta Biochim. Biophys. Sin. 52, 1178–1180 (2020).

pubmed: 32770209

Grimston, S. K., Watkins, M. P., Brodt, M. D., Silva, M. J. & Civitelli, R. Enhanced periosteal and endocortical responses to axial tibial compression loading in conditional connexin43 deficient mice. PLoS One 7, e44222 (2012).

pubmed: 22970183 pmcid: 3438198

Lecanda, F. et al. Gap junctional communication modulates gene expression in osteoblastic cells. Mol. Biol. Cell 9, 2249–2258 (1998).

pubmed: 9693379 pmcid: 25477

Li, Z., Zhou, Z., Saunders, M. M. & Donahue, H. J. Modulation of connexin43 alters expression of osteoblastic differentiation markers. Am. J. Physiol. Cell Physiol. 290, C1248–C1255 (2006).

pubmed: 16319124

Schiller, P. C., Roos, B. A. & Howard, G. A. Parathyroid hormone up-regulation of connexin 43 gene expression in osteoblasts depends on cell phenotype. J. Bone Min. Res. 12, 2005–2013 (1997).

Watkins, M. et al. Osteoblast connexin43 modulates skeletal architecture by regulating both arms of bone remodeling. Mol. Biol. Cell 22, 1240–1251 (2011).

pubmed: 21346198 pmcid: 3078079

Hung, C. T., Allen, F. D., Mansfield, K. D. & Shapiro, I. M. Extracellular ATP modulates [Ca2 + ]i in retinoic acid-treated embryonic chondrocytes. Am. J. Physiol. 272, C1611–C1617 (1997).

pubmed: 9176153

Lima, F., Niger, C., Hebert, C. & Stains, J. P. Connexin43 potentiates osteoblast responsiveness to fibroblast growth factor 2 via a protein kinase C-delta/Runx2-dependent mechanism. Mol. Biol. Cell 20, 2697–2708 (2009).

pubmed: 19339281 pmcid: 2688549

Niger, C. et al. ERK acts in parallel to PKCdelta to mediate the connexin43-dependent potentiation of Runx2 activity by FGF2 in MC3T3 osteoblasts. Am. J. Physiol. Cell Physiol. 302, C1035–C1044 (2012).

pubmed: 22277757 pmcid: 3330735

Plotkin, L. I., Manolagas, S. C. & Bellido, T. Transduction of cell survival signals by connexin-43 hemichannels. J. Biol. Chem. 277, 8648–8657 (2002).

pubmed: 11741942

Stains, J. P. & Civitelli, R. Gap junctions regulate extracellular signal-regulated kinase signaling to affect gene transcription. Mol. Biol. Cell 16, 64–72 (2005).

pubmed: 15525679 pmcid: 539152

Hashida, Y. et al. Communication-dependent mineralization of osteoblasts via gap junctions. Bone 61, 19–26 (2014).

pubmed: 24389413

Niger, C. et al. The transcriptional activity of osterix requires the recruitment of Sp1 to the osteocalcin proximal promoter. Bone 49, 683–692 (2011).

pubmed: 21820092 pmcid: 3170016

Niger, C. et al. The regulation of runt-related transcription factor 2 by fibroblast growth factor-2 and connexin43 requires the inositol polyphosphate/protein kinase Cdelta cascade. J. Bone Min. Res. 28, 1468–1477 (2013).

Stains, J. P., Lecanda, F., Screen, J., Towler, D. A. & Civitelli, R. Gap junctional communication modulates gene transcription by altering the recruitment of Sp1 and Sp3 to connexin-response elements in osteoblast promoters. J. Biol. Chem. 278, 24377–24387 (2003).

pubmed: 12700237

Ilvesaro, J., Tavi, P. & Tuukkanen, J. Connexin-mimetic peptide Gap 27 decreases osteoclastic activity. BMC Musculoskelet. Disord. 2, 10 (2001).

pubmed: 11747476 pmcid: 61034

Ilvesaro, J., Vaananen, K. & Tuukkanen, J. Bone-resorbing osteoclasts contain gap-junctional connexin-43. J. Bone Min. Res. 15, 919–926 (2000).

Jones, S. J. & Boyde, A. Questions of quality and quantity–a morphological view of bone biology. Kaibogaku Zasshi 69, 229–243 (1994).

pubmed: 8091941

Zappitelli, T. et al. The G60S connexin 43 mutation activates the osteoblast lineage and results in a resorption-stimulating bone matrix and abrogation of old-age-related bone loss. J. Bone Min. Res. 28, 2400–2413 (2013).

Zhang, Y. et al. Enhanced osteoclastic resorption and responsiveness to mechanical load in gap junction deficient bone. PLoS One 6, e23516 (2011).

pubmed: 21897843 pmcid: 3163577

Batra, N. et al. Mechanical stress-activated integrin alpha5beta1 induces opening of connexin 43 hemichannels. Proc. Natl. Acad. Sci. USA 109, 3359–3364 (2012).

pubmed: 22331870 pmcid: 3295295

Burra, S. et al. Dendritic processes of osteocytes are mechanotransducers that induce the opening of hemichannels. Proc. Natl. Acad. Sci. USA 107, 13648–13653 (2010).

pubmed: 20643964 pmcid: 2922284

Parsons, J. T., Martin, K. H., Slack, J. K., Taylor, J. M. & Weed, S. A. Focal adhesion kinase: a regulator of focal adhesion dynamics and cell movement. Oncogene 19, 5606–5613 (2000).

pubmed: 11114741

Qin, L., Liu, W., Cao, H. & Xiao, G. Molecular mechanosensors in osteocytes. Bone Res. 8, 23 (2020).

pubmed: 32550039 pmcid: 7280204

Siller-Jackson, A. J. et al. Adaptation of connexin 43-hemichannel prostaglandin release to mechanical loading. J. Biol. Chem. 283, 26374–26382 (2008).

pubmed: 18676366 pmcid: 2546557

Bivi, N. et al. Cell autonomous requirement of connexin 43 for osteocyte survival: consequences for endocortical resorption and periosteal bone formation. J. Bone Min. Res. 27, 374–389 (2012).

Kar, R., Riquelme, M. A., Werner, S. & Jiang, J. X. Connexin 43 channels protect osteocytes against oxidative stress-induced cell death. J. Bone Min. Res. 28, 1611–1621 (2013).

Lloyd, S. A., Loiselle, A. E., Zhang, Y. & Donahue, H. J. Evidence for the role of connexin 43-mediated intercellular communication in the process of intracortical bone resorption via osteocytic osteolysis. BMC Musculoskelet. Disord. 15, 122 (2014).

pubmed: 24716486 pmcid: 3984635

Hellio Le Graverand, M. P. et al. Formation and phenotype of cell clusters in osteoarthritic meniscus. Arthritis Rheum. 44, 1808–1818 (2001).

pubmed: 11508433

Kolomytkin, O. V. et al. IL-1beta-induced production of metalloproteinases by synovial cells depends on gap junction conductance. Am. J. Physiol. Cell Physiol. 282, C1254–C1260 (2002).

pubmed: 11997239

Marino, A. A. et al. Increased intercellular communication through gap junctions may contribute to progression of osteoarthritis. Clin. Orthop. Relat. Res. 224–232, https://doi.org/10.1097/01.blo.0000129346.29945.3b (2004).

Tsuchida, S. et al. Silencing the expression of connexin 43 decreases inflammation and joint destruction in experimental arthritis. J. Orthop. Res. 31, 525–530 (2013).

pubmed: 23165424

Gago-Fuentes, R. et al. The C-terminal domain of connexin43 modulates cartilage structure via chondrocyte phenotypic changes. Oncotarget 7, 73055–73067 (2016).

pubmed: 27682878 pmcid: 5341963

Chen, Q. et al. Carcinoma-astrocyte gap junctions promote brain metastasis by cGAMP transfer. Nature 533, 493–498 (2016).

pubmed: 27225120 pmcid: 5021195

Ormonde, S. et al. Regulation of connexin43 gap junction protein triggers vascular recovery and healing in human ocular persistent epithelial defect wounds. J. Membr. Biol. 245, 381–388 (2012).

pubmed: 22797940

Macia, E. et al. Characterization of gap junction remodeling in epicardial border zone of healing canine infarcts and electrophysiological effects of partial reversal by rotigaptide. Circ. Arrhythm. Electrophysiol. 4, 344–351 (2011).

pubmed: 21493965 pmcid: 3116056

Ghatnekar, G. S., Grek, C. L., Armstrong, D. G., Desai, S. C. & Gourdie, R. G. The effect of a connexin43-based Peptide on the healing of chronic venous leg ulcers: a multicenter, randomized trial. J. Invest. Dermatol. 135, 289–298 (2015).

pubmed: 25072595

Jiang, J. et al. Interaction of alpha Carboxyl Terminus 1 peptide with the connexin 43 carboxyl terminus preserves left ventricular function after ischemia-reperfusion injury. J. Am. Heart Assoc. 8, e012385 (2019).

pubmed: 31422747 pmcid: 6759879

Kim, Y. et al. Tonabersat prevents inflammatory damage in the central nervous system by blocking Connexin43 hemichannels. Neurotherapeutics 14, 1148–1165 (2017).

pubmed: 28560708 pmcid: 5722754

O’Carroll, S. J., Alkadhi, M., Nicholson, L. F. & Green, C. R. Connexin 43 mimetic peptides reduce swelling, astrogliosis, and neuronal cell death after spinal cord injury. Cell Commun. Adhes. 15, 27–42 (2008).

pubmed: 18649176

Abudara, V. et al. The connexin43 mimetic peptide Gap19 inhibits hemichannels without altering gap junctional communication in astrocytes. Front. Cell Neurosci. 8, 306 (2014).

pubmed: 25374505 pmcid: 4204617

Silverman, W., Locovei, S. & Dahl, G. Probenecid, a gout remedy, inhibits pannexin 1 channels. Am. J. Physiol. Cell Physiol. 295, C761–C767 (2008).

pubmed: 18596212 pmcid: 2544448

Wang, J., Jackson, D. G. & Dahl, G. The food dye FD&C Blue No. 1 is a selective inhibitor of the ATP release channel Panx1. J. Gen. Physiol. 141, 649–656 (2013).

pubmed: 23589583 pmcid: 3639576

Locovei, S., Scemes, E., Qiu, F., Spray, D. C. & Dahl, G. Pannexin1 is part of the pore forming unit of the P2X(7) receptor death complex. FEBS Lett. 581, 483–488 (2007).

pubmed: 17240370 pmcid: 1868681

Xiao, F., Waldrop, S. L., Khimji, A. K. & Kilic, G. Pannexin1 contributes to pathophysiological ATP release in lipoapoptosis induced by saturated free fatty acids in liver cells. Am. J. Physiol. Cell Physiol. 303, C1034–C1044 (2012).

pubmed: 22972801 pmcid: 3492830

Linsdell, P. Inhibition of cystic fibrosis transmembrane conductance regulator chloride channel currents by arachidonic acid. Can. J. Physiol. Pharm. 78, 490–499 (2000).

Brough, D., Pelegrin, P. & Rothwell, N. J. Pannexin-1-dependent caspase-1 activation and secretion of IL-1beta is regulated by zinc. Eur. J. Immunol. 39, 352–358 (2009).

pubmed: 19130485 pmcid: 2696683

Pannexins in the musculoskeletal system: new targets for development and disease progression.

Journal

Informations de publication

Résumé

Identifiants

Substances chimiques

Types de publication

Langues

Sous-ensembles de citation

Pagination

Subventions

Informations de copyright

Références

Auteurs

Yan Luo (Y)

Shengyuan Zheng (S)

Wenfeng Xiao (W)

Hang Zhang (H)

Yusheng Li (Y)

Articles similaires

[Redispensing of expensive oral anticancer medicines: a practical application].

Smoking Cessation and Incident Cardiovascular Disease.

Evaluation of Low-Value Services Across Major Medicare Advantage Insurers and Traditional Medicare.

Effectiveness of Virtual Yoga for Chronic Low Back Pain: A Randomized Clinical Trial.

Classifications MeSH