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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/06/16 20:13:49」(JST)

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Connexins, or gap junction proteins, are a family of structurally-related transmembrane proteins that assemble to form vertebrate gap junctions (an entirely different family of proteins, the innexins, form gap junctions in invertebrates).^[1] Each gap junction is composed of two hemichannels, or connexons, which are themselves each constructed out of six connexin molecules. Gap junctions are essential for many physiological processes, such as the coordinated depolarization of cardiac muscle, proper embryonic development, and the conducted response in microvasculature. For this reason, mutations in connexin-encoding genes can lead to functional and developmental abnormalities.

Structure

Connexins are four-pass transmembrane proteins with both C and N cytoplasmic termini, a cytoplasmic loop (CL) and two extra-cellular loops, (EL-1) and (EL-2). Connexins are assembled in groups of six to form hemichannels, or connexons, and two hemichannels then combine to form a gap junction. The connexin gene family is diverse, with twenty-one identified members in the sequenced human genome, and twenty in the mouse (nineteen of which are orthologous pairs). They usually weigh between 26 and 60 kDa, and have an average length of 380 amino acids. The various connexins have been observed to combine into both homomeric and heteromeric gap junctions, each of which may exhibit different functional properties including pore conductance, size selectivity, charge selectivity, voltage gating, and chemical gating.

Nomenclature

In recent literature, connexins are most commonly named according to their molecular weights, e.g. Cx26 is the connexin protein of 26 kDa. However, this can lead to confusion when connexin genes from different species are compared, e.g. human Cx36 is homologous to zebrafish Cx35. A competing nomenclature is the Gja/Gjb system, where connexins are sorted by their α and β forms, then assigned an identifying number, e.g. Gja1 corresponds to Cx43. The nomenclature of the connexin genes and proteins is currently under review by the HUGO Gene Nomenclature Committee.

Biosynthesis and Internalization

A remarkable aspect of connexins is that they have a relatively short half life of only a few hours.^[2] The result is the presence of a dynamic cycle by which connexins are synthesized and replaced. It has been suggested that this short life span allows for more finely regulated physiological processes to take place, such as in the myometrium.

From the Nucleus to the Membrane

As they are being translated by ribosomes, connexins are inserted into the membrane of the endoplasmic reticulum (ER) (Bennett and Zukin, 2004). It is in the ER that connexins are properly folded, yielding two extracellular loops, EL-1 and EL-2. It is also in the ER that the oligomerization of connexin molecules into hemichannels begins, a process which may continue in the UR-Golgi intermediate compartment as well.^[2] The arrangements of these hemichannels can be homotypic, heterotypic, and combined heterotypic/heteromeric.

After exiting the ER and passing through the ERGIC, the folded connexins will usually enter the cis-Golgi network.^[3] However, some connexins, such as Cx26 may be transported independent of the Golgi.^[4]^[5]^[6]^[7]^[8]

Gap Junction Assembly

After being inserted into the plasma membrane of the cell, the hemichannels freely diffuse within the lipid bilayer.^[9] Through the aid of specific proteins, mainly cadherins, the hemichannels are able to dock with hemichannels of adjacent cells forming gap junctions.^[10] Recent studies have shown the existence of communication between adherens junctions and gap junctions,^[11] suggesting a higher level of coordination than previously thought.

Life cycle and protein associations of connexins. Connexins are synthesized on ER-bound ribosomes and inserted into the ER cotranslationally. This is followed by oligomerization between the ER and trans-Golgi network (depending on the connexin type) into connexons, which are then delivered to the membrane via the actin or microtubule networks. Connexons may also be delivered to the plasma membrane by direct transfer from the rough ER. Upon insertion into the membrane, connexons may remain as hemichannels or they dock with compatible connexons on adjacent cells to form gap junctions. Newly delivered connexons are added to the periphery of pre-formed gap junctions, while the central "older" gap junction fragment are degraded by internalization of a double-membrane structure called an annular junction into one of the two cells, where subsequent lysosomal or proteasomal degradation occurs, or in some cases the connexons are recycled to the membrane (indicated by dashed arrow). During their life cycle, connexins associate with different proteins, including (1) cytoskeletal components as microtubules, actin, and actin-binding proteins α-spectrin and drebrin, (2) junctional molecules including adherens junction components such as cadherins, α-catenin, and β-catenin, as well as tight junction components such as ZO-1 and ZO-2, (3) enzymes such as kinases and phosphatases which regulate the assembly, function, and degradation, and (4) other proteins such as caveolin. Dbouk et al., 2009.^[12]

Function

Connexin gap junctions are found only in vertebrates. A functionally analogous but genetically unrelated group of proteins, the pannexins are expressed in both vertebrate and invertebrate species. The innexin proteins, invertebrate gap junction proteins, are probably pannexins. They have a similar structure, but don't share any sequence homology.

Within the CNS, gap junctions provide electrical coupling between progenitor cells, neurons, and glial cells. By using specific connexin KO mice, studies revealed that cell coupling is essential for visual signaling. In the retina, ambient light levels influence cell coupling provided by gap junction channels, adapting the visual function for various lighting conditions. Cell coupling is governed by several mechanisms, including connexin expression.^[13]

List of human connexins

Connexin	Gene	Location and Function
Cx43	GJA1	Expressed at the surface of vasculature with atherosclerotic plaque, and up-regulated during atherosclerosis in mice. May have pathological effects. Also expressed between granulosa cells, which is required for proliferation. Normally expressed in astrocytes, also detected in most of the human astrocytomas and in the astroglial component of glioneuronal tumors. ^[14] It is also the main cardiac connexin, found mainly in ventricular myocardium. ^[15] Associated with oculodentodigital dysplasia.
Cx46	GJA3
Cx37	GJA4	Induced in vascular smooth muscle during coronary arteriogenesis. Cx37 mutations are not lethal. Forms gap junctions between oocytes and granulosa cells, and are required for oocyte survival.
Cx40	GJA5	Expressed selectively in atrial myocytes. Responsible for mediating the coordinated electrical activation of atria.^[16]
Cx33	GJA6 (GJA6P)	Pseudogene in humans
Cx50	GJA8	Gap Junctions between A-typ Horizontal cells in Mouse and Rabbit Retina^[17]
Cx59	GJA10
Cx62	GJA10	Human Cx62 complies Cx57 (Mouse). Location in axon-bearing B-typ Horizontal Cell in Rabbit Retina^[18]
Cx32	GJB1	Major component of the peripheral myelin. Mutations in the human gene cause X-linked Charcot-Marie-Tooth disease, a hereditary neuropathy. In human normal brain CX32 expressed in neurons and oligodendrocytes.^[14]
Cx26	GJB2	Mutated in Vohwinkel syndrome as well as Keratitis-Icthyosis-Deafness (KID) Syndrome.
Cx31	GJB3	Can be associated with Erythrokeratodermia variabilis.
Cx30.3	GJB4	Fonseca et al. confirmed Cx30.3 expression in thymocytes.^[19] Can be associated with Erythrokeratodermia variabilis.
Cx31.1	GJB5
Cx30	GJB6	Mutated in Clouston syndrome (hidrotic ectodermal dysplasia)
Cx25	GJB7
Cx45	GJC1/GJA7	Human pancreatic ductal epithelial cells.^[20] Atrio-ventricular node.
Cx47	GJC2/GJA12	Expressed in oligodentrocytes
Cx30.2	GJC3	Expressed in structures of the inner ear. Thought to have a role in ion transport for signal transduction in hair cells.^[21]
Cx36	GJD2/GJA9	Pancreatic beta cell function, mediating the release of insulin. Neurones throughout the Central Nervous System where they allow synchronisation of action potential firing between networks of neurones.^[22]
Cx31.9	GJD3/GJC1
Cx39	GJD4
Cx40.1	GJD4
Cx23	GJE1
Cx29	GJE1

References

^ Lodish, Harvey F.; Arnold Berk, Paul Matsudaira, Chris A. Kaiser, Monty Krieger, Mathew P. Scott, S. Lawrence Zipursky, James Darnell (2004). Molecular Cell Biology (5th ed.). New York: W.H. Freeman and Company. pp. 230–1. ISBN 0-7167-4366-3. http://www.ncbi.nlm.nih.gov/books/bv.fcgi?call=bv.View..ShowTOC&rid=mcb.TOC&depth=10.
^ ^a ^b Laird DW (March 2006). "Life cycle of connexins in health and disease". The Biochemical Journal 394 (3): 527–43. DOI:10.1042/BJ20051922. PMC 1383703. PMID 16492141. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1383703.
^ Musil, LS; Goodenough DA (1993). "Multisubunit assembly of an integral plasma membrane channel protein, gap junction connexin43, occurs after exit from the ER". Cell 74 (6): 1065–1077. DOI:10.1016/0092-8674(93)90728-9. PMID 7691412.
^ Evans, W. H.; Ahmad, S., Diez, J., George, C. H., Kendall, J. M. and Martin, P. E. (1999). "Trafficking pathways leading to the formation of gap junctions". Novartis Found. Symp.. Novartis Foundation Symposia 219: 44–54. DOI:10.1002/9780470515587.ch4. ISBN 978-0-470-51558-7. PMID 10207897.
^ George, C. H., Kendall, J. M. and Evans, W. H. (1999). "Intracellular trafficking pathways in the assembly of connexins into gap junctions". J. Biol. Chem. 274 (13): 8678–8685. DOI:10.1074/jbc.274.13.8678. PMID 10085106.
^ George, C. H., Kendall, J. M., Campbell, A. K. and Evans, W. H. (1998). "Connexin–aequorin chimerae report cytoplasmic calcium environments along trafficking pathways leading to gap junction biogenesis in living COS-7 cells". J. Biol. Chem. 274 (45): 29822–29829. DOI:10.1074/jbc.273.45.29822. PMID 9792698.
^ Martin, P. E., George, C. H., Castro, C., Kendall, J. M., Capel, J., Campbell, A. K., Revilla, A., Barrio, L. C. and Evans, W. H. (1998). "Assembly of chimeric connexin–aequorin proteins into functional gap junction channels. Reporting intracellular and plasma membrane calcium environments". J. Biol. Chem. 273 (3): 1719–1726. DOI:10.1074/jbc.273.3.1719. PMID 9430718.
^ Martin, P. E., Errington, R. J. and Evans, W. H. (2001). "Gap junction assembly: multiple connexin fluorophores identify complex trafficking pathways". Cell Commun. Adhes. 8 (4–6): 243–248. DOI:10.3109/15419060109080731. PMID 12064596.
^ Thomas, T., Jordan, K., Simek, J., Shao, Q., Jedeszko, C., Walton, P. and Laird, D. W. (2005). "Mechanisms of Cx43 and Cx26 transport to the plasma membrane and gap junction regeneration". J. Cell Sci 118 (Pt 19): 4451–4462. DOI:10.1242/jcs.02569. PMID 16159960.
^ Jongen, W. M., Fitzgerald, D. J., Asamoto, M., Piccoli, C., Slaga, T. J., Gros, D., Takeichi, M. and Yamasaki, H. (1991). "Regulation of connexin 43-mediated gap junctional intercellular communication by Ca2+ in mouse epidermal cells is controlled by E- cadherin". J. Cell Biol. 114 (3): 545–555. DOI:10.1083/jcb.114.3.545. PMC 2289094. PMID 1650371. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2289094.
^ Wei, C. J., Francis, R., Xu, X. and Lo, C. W. (2005). "Connexin43 associated with an N-cadherin-containing multiprotein complex is required for gap junction formation in NIH3T3 cells". J. Biol. Chem. 280 (20): 19925–36. DOI:10.1074/jbc.M412921200. PMID 15741167.
^ Connexins: a myriad of functions extending beyond assembly of gap junction channels. Dbouk HA, Mroue RM, El-Sabban ME, Talhouk RS. Cell Commun Signal. 2009 Mar 12;7:4. doi:10.1186/1478-811X-7-4 PMID 19284610
^ Kihara AH, de Castro LM, Moriscot AS, Hamassaki DE. (May 2006). "Prolonged dark adaptation changes connexin expression in the mouse retina". J Neurosci Res 83 (7): 1331–41. DOI:10.1002/jnr.20815. PMID 16496335.
^ ^a ^b Aronica E, Gorter J, Jansen G et al. (2001). "Expression of connexin 43 and connexin 32 gap-junction proteins in epilepsy-associated brain tumors and in the perilesional epileptic cortex". Acta Neuropathol. 101 (5): 449–59. PMID 11484816.
^ http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9130448
^ Gollob MH et al. (June 22 2006). "Somatic mutations in the connexin 40 gene (GJA5) in atrial fibrillation". N Engl J Med 354 (25): 2677–88. DOI:10.1056/NEJMoa052800. PMID 16790700.
^ Massey, Stephen (January, 16. 2009). Connexins: A Guide (1st ed.). Springer-Verlag Gmbh. pp. 3-?. ISBN 1-934115-46-0.
^ Beyer, Eric C.; Berthound, Viviana M. (January, 16. 2009). Connexins: A Guide (1st ed.). Springer-Verlag Gmbh. pp. 387–417. ISBN 1-934115-46-0.
^ Fonseca PC, Nihei OK, Urban-Maldonado M, Abreu S, de Carvalho AC, Spray DC, Savino W, Alves LA (June 2004). "Characterization of connexin 30.3 and 43 in thymocytes". Immuno lett. 94 (1–2): 65–75. DOI:10.1016/j.imlet.2004.03.019. PMID 15234537.
^ Tai M-H; Olson, LK; Madhukar, BV; Linning, KD; Van Camp, L; Tsao, MS; Trosko, JE (2003). "Characterization of Gap Junctional Intercellular Communication in Immortalized Human Pancreatic Ductal Epithelial Cells With Stem Cell Characteristics". Pancreas 26 (1): e18–e26. DOI:10.1097/00006676-200301000-00025. PMID 12499933.
^ del Castillo I et al. (January 24 2002). "A deletion involving the connexin 30 gene in nonsyndromic hearing impairment". N Engl J Med 346 (4): 343–9. DOI:10.1056/NEJMoa012052. PMID 11807148.
^ Connors BW, Long MA (2004). "Electrical synapses in the mammalian brain". Annu Rev Neurosci 27: 393–418. DOI:10.1146/annurev.neuro.26.041002.131128. PMID 15217338.

External links

Media related to connexins at Wikimedia Commons
Connexins at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

1. 小児における聴覚障害：病因 hearing impairment in children etiology
2. 小児における聴覚障害：評価 hearing impairment in children evaluation
3. ビスホスホネートの薬理学 pharmacology of bisphosphonates
4. 分娩の生理学 physiology of parturition
5. 心房細動の機序 mechanisms of atrial fibrillation

English Journal

Hippocampal GABAergic interneurons coexpressing alpha7-nicotinic receptors and connexin-36 are able to improve neuronal viability under oxygen-glucose deprivation.

Voytenko LP1, Lushnikova IV2, Savotchenko AV3, Isaeva EV3, Skok MV4, Lykhmus OY4, Patseva MA2, Skibo GG2.
Brain research.Brain Res.2015 Aug 7;1616:134-45. doi: 10.1016/j.brainres.2015.04.061. Epub 2015 May 9.
The hippocampal interneurons are very diverse by chemical profiles and rather inconsistent by sensitivity to CI. Some hippocampal GABAergic interneurons survive certain time after ischemia while ischemia-sensitive interneurons and pyramidal neurons are damaged. GABAergic signaling, nicotinic recepto
PMID 25966616

Connexin 43 mediates PFOS-induced apoptosis in astrocytes.

Dong L1, Yang X2, Gu W2, Zhao K2, Ge H3, Zhou J3, Bai X4.
Chemosphere.Chemosphere.2015 Aug;132:8-16. doi: 10.1016/j.chemosphere.2015.02.041. Epub 2015 Mar 13.
Perfluorooctane sulfonate (PFOS) is a man-made environmental pollutant that is toxic to mammals. However, the neurotoxic effects of PFOS remain largely unexplored. In this study, we determined the role of an astrocyte specific gap junction protein, connexin 43 (Cx43), in PFOS-induced apoptosis. The
PMID 25770831

Establishment of an interleukin‑1β‑induced inflammation‑activated endothelial cell‑smooth muscle cell‑mononuclear cell co‑culture model and evaluation of the anti‑inflammatory effects of tanshinone IIA on atherosclerosis.

Li Y1, Guo Y1, Chen Y1, Wang Y1, You Y1, Yang Q1, Weng X1, Li Q1, Zhu X1, Zhou B1, Liu X1, Gong Z1, Zhang R1.
Molecular medicine reports.Mol Med Rep.2015 Aug;12(2):1665-76. doi: 10.3892/mmr.2015.3668. Epub 2015 Apr 23.
Increasing evidence supports the hypothesis that inflammatory reactions serves an important function in the formation, progression and plaque rupture of atherosclerosis. Interleukin (IL)‑1 primarily induces inflammation and is closely associated with the inflammatory environment and the formation
PMID 25936371

Japanese Journal

Characteristics of the Localization of Connexin 43 in Satellite Cells during Skeletal Muscle Regeneration In Vivo

,
ACTA HISTOCHEMICA ET CYTOCHEMICA 48(2), 53-60, 2015
… In the sequence of events for myotube formation, intercellular communication through gap junctions composed of connexin 43 (Cx43) plays critical roles in regulating the alignment and fusion of myoblasts in advances of myotube formation in vitro. …
NAID 130005068298

Characteristics of the Localization of Connexin 43 in Satellite Cells during Skeletal Muscle Regeneration In Vivo

,
ACTA HISTOCHEMICA ET CYTOCHEMICA advpub(0), 2015
… In the sequence of events for myotube formation, intercellular communication through gap junctions composed of connexin 43 (Cx43) plays critical roles in regulating the alignment and fusion of myoblasts in advances of myotube formation in vitro. …
NAID 130005066161

Antiarrhythmic Peptide AAP10 Prevents Arrhythmias Induced by Protein Kinase C Activation in Rabbit Left Ventricular Wedges

, ,
International Heart Journal advpub(0), 2015
… Changes in connexin43 (Cx43) and nonphosphorylated Cx43 on S368 were measured by Western blot analysis.In the PMA group, the QT interval was shortened, the interval from the peak to the end of the electrocardiographic T wave (Tp-e) and induced nonsustained ventricular tachycardia (VT) were increased, and the expressions of Cx43 and nonphosphorylated Cx43 on S368 were decreased compared with the control group. …
NAID 130004941347

Related Pictures

★リンクテーブル★

リンク元	「gap junction protein」

「gap junction protein」

Connexin
	An open gap junction, composed of six identical connexin proteins. Each of these six units is a single polypeptide which passes the membrane four times (referred to as four-pass transmembrane proteins).
Identifiers
Symbol	Connexin
Pfam	PF00029
InterPro	IPR013092
PROSITE	PDOC00341
TCDB	1.A.24
OPM superfamily	215
OPM protein	2zw3
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

　　[★]

ギャップ結合タンパク質、ギャップジャンクションタンパク質

関: connexin

[0] Lodish, Harvey F.; Arnold Berk, Paul Matsudaira, Chris A. Kaiser, Monty Krieger, Mathew P. Scott, S. Lawrence Zipursky, James Darnell (2004). Molecular Cell Biology (5th ed.). New York: W.H. Freeman and Company. pp. 230–1. ISBN 0-7167-4366-3. http://www.ncbi.nlm.nih.gov/books/bv.fcgi?call=bv.View..ShowTOC&rid=mcb.TOC&depth=10.

[Laird2006-1] Laird DW (March 2006). "Life cycle of connexins in health and disease". The Biochemical Journal 394 (3): 527–43. DOI:10.1042/BJ20051922. PMC 1383703. PMID 16492141. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1383703.

[2] Musil, LS; Goodenough DA (1993). "Multisubunit assembly of an integral plasma membrane channel protein, gap junction connexin43, occurs after exit from the ER". Cell 74 (6): 1065–1077. DOI:10.1016/0092-8674(93)90728-9. PMID 7691412.

[3] Evans, W. H.; Ahmad, S., Diez, J., George, C. H., Kendall, J. M. and Martin, P. E. (1999). "Trafficking pathways leading to the formation of gap junctions". Novartis Found. Symp.. Novartis Foundation Symposia 219: 44–54. DOI:10.1002/9780470515587.ch4. ISBN 978-0-470-51558-7. PMID 10207897.

[4] George, C. H., Kendall, J. M. and Evans, W. H. (1999). "Intracellular trafficking pathways in the assembly of connexins into gap junctions". J. Biol. Chem. 274 (13): 8678–8685. DOI:10.1074/jbc.274.13.8678. PMID 10085106.

[5] George, C. H., Kendall, J. M., Campbell, A. K. and Evans, W. H. (1998). "Connexin–aequorin chimerae report cytoplasmic calcium environments along trafficking pathways leading to gap junction biogenesis in living COS-7 cells". J. Biol. Chem. 274 (45): 29822–29829. DOI:10.1074/jbc.273.45.29822. PMID 9792698.

[6] Martin, P. E., George, C. H., Castro, C., Kendall, J. M., Capel, J., Campbell, A. K., Revilla, A., Barrio, L. C. and Evans, W. H. (1998). "Assembly of chimeric connexin–aequorin proteins into functional gap junction channels. Reporting intracellular and plasma membrane calcium environments". J. Biol. Chem. 273 (3): 1719–1726. DOI:10.1074/jbc.273.3.1719. PMID 9430718.

[7] Martin, P. E., Errington, R. J. and Evans, W. H. (2001). "Gap junction assembly: multiple connexin fluorophores identify complex trafficking pathways". Cell Commun. Adhes. 8 (4–6): 243–248. DOI:10.3109/15419060109080731. PMID 12064596.

[8] Thomas, T., Jordan, K., Simek, J., Shao, Q., Jedeszko, C., Walton, P. and Laird, D. W. (2005). "Mechanisms of Cx43 and Cx26 transport to the plasma membrane and gap junction regeneration". J. Cell Sci 118 (Pt 19): 4451–4462. DOI:10.1242/jcs.02569. PMID 16159960.

[9] Jongen, W. M., Fitzgerald, D. J., Asamoto, M., Piccoli, C., Slaga, T. J., Gros, D., Takeichi, M. and Yamasaki, H. (1991). "Regulation of connexin 43-mediated gap junctional intercellular communication by Ca2+ in mouse epidermal cells is controlled by E- cadherin". J. Cell Biol. 114 (3): 545–555. DOI:10.1083/jcb.114.3.545. PMC 2289094. PMID 1650371. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2289094.

[10] Wei, C. J., Francis, R., Xu, X. and Lo, C. W. (2005). "Connexin43 associated with an N-cadherin-containing multiprotein complex is required for gap junction formation in NIH3T3 cells". J. Biol. Chem. 280 (20): 19925–36. DOI:10.1074/jbc.M412921200. PMID 15741167.

[Dbouk09-11] Connexins: a myriad of functions extending beyond assembly of gap junction channels. Dbouk HA, Mroue RM, El-Sabban ME, Talhouk RS. Cell Commun Signal. 2009 Mar 12;7:4. doi:10.1186/1478-811X-7-4 PMID 19284610

[Kihara-12] Kihara AH, de Castro LM, Moriscot AS, Hamassaki DE. (May 2006). "Prolonged dark adaptation changes connexin expression in the mouse retina". J Neurosci Res 83 (7): 1331–41. DOI:10.1002/jnr.20815. PMID 16496335.

[Aronica-13] Aronica E, Gorter J, Jansen G et al. (2001). "Expression of connexin 43 and connexin 32 gap-junction proteins in epilepsy-associated brain tumors and in the perilesional epileptic cortex". Acta Neuropathol. 101 (5): 449–59. PMID 11484816.

[14] ttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9130448

[15] Gollob MH et al. (June 22 2006). "Somatic mutations in the connexin 40 gene (GJA5) in atrial fibrillation". N Engl J Med 354 (25): 2677–88. DOI:10.1056/NEJMoa052800. PMID 16790700.

[16] Massey, Stephen (January, 16. 2009). Connexins: A Guide (1st ed.). Springer-Verlag Gmbh. pp. 3-?. ISBN 1-934115-46-0.

[17] Beyer, Eric C.; Berthound, Viviana M. (January, 16. 2009). Connexins: A Guide (1st ed.). Springer-Verlag Gmbh. pp. 387–417. ISBN 1-934115-46-0.

[18] Fonseca PC, Nihei OK, Urban-Maldonado M, Abreu S, de Carvalho AC, Spray DC, Savino W, Alves LA (June 2004). "Characterization of connexin 30.3 and 43 in thymocytes". Immuno lett. 94 (1–2): 65–75. DOI:10.1016/j.imlet.2004.03.019. PMID 15234537.

[19] Tai M-H; Olson, LK; Madhukar, BV; Linning, KD; Van Camp, L; Tsao, MS; Trosko, JE (2003). "Characterization of Gap Junctional Intercellular Communication in Immortalized Human Pancreatic Ductal Epithelial Cells With Stem Cell Characteristics". Pancreas 26 (1): e18–e26. DOI:10.1097/00006676-200301000-00025. PMID 12499933.

[20] Castillo I et al. (January 24 2002). "A deletion involving the connexin 30 gene in nonsyndromic hearing impairment". N Engl J Med 346 (4): 343–9. DOI:10.1056/NEJMoa012052. PMID 11807148.

[21] Connors BW, Long MA (2004). "Electrical synapses in the mammalian brain". Annu Rev Neurosci 27: 393–418. DOI:10.1146/annurev.neuro.26.041002.131128. PMID 15217338.

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connexin