Pannexin 2 protein expression is not restricted to the CNS

Frontiers in Cellular Neuroscience

Volumn 8, Issue NOV, 2014, Pages

  Vasseur, Maxence Le ^a   Lelowski, Jonathan ^a   Bechberger, John F ^a   Sin, Wun Chey ^a   Naus, Christian C ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

Central nervous system (CNS); Gap junction; Gene transcription; Mouse; MRNA; Pannexin 2; Protein distribution; Protein expression

Indexed keywords

GAP JUNCTION PROTEIN; MESSENGER RNA; MONOCLONAL ANTIBODY; PANNEXIN 1; PANNEXIN 2; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; ANTIBODY LABELING; ARTICLE; ASTROCYTOSIS; CENTRAL NERVOUS SYSTEM; CONTROLLED STUDY; CYTOPLASM; DENSITOMETRY; EPITOPE MAPPING; GENETIC TRANSCRIPTION; IMMUNOFLUORESCENCE; IMMUNOHISTOCHEMISTRY; IMMUNOREACTIVITY; MONTE CARLO METHOD; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN EXPRESSION; PROTEIN ISOLATION; PROTEIN LOCALIZATION; PROTEIN TRANSPORT; REAL TIME POLYMERASE CHAIN REACTION; RNA ISOLATION; UPREGULATION; WESTERN BLOTTING;

EID: 84912524105     PISSN: 16625102     EISSN: None     Source Type: Journal    
DOI: 10.3389/fncel.2014.00392     Document Type: Article

References (44)

1. Ambrosi, C., Gassmann, O., Pranskevich, J. N., Boassa, D., Smock, A., Wang, J., et al. (2010). Pannexin1 and pannexin2 channels show quaternary similarities to connexons and different oligomerization numbers from each other. J. Biol. Chem. 285, 24420–24431. doi:10.1074/jbc.m110.115444
2. Baranova, A., Ivanov, D., Petrash, N., Pestova, A., Skoblov, M., Kelmanson, I., et al. (2004). The mammalian pannexin family is homologous to the invertebrate innexin gap junction proteins. Genomics 83, 706–716. doi:10.1016/j.ygeno.2003.09.025
3. Barbe, M. T. (2006). Cell-cell communication beyond connexins: the pannexin channels. Physiology 21, 103–114. doi:10.1152/physiol.00048.2005
4. Bargiotas, P., Krenz, A., Hormuzdi, S. G., Ridder, D. A., Herb, A., Barakat, W., et al. (2011). Pannexins in ischemia-induced neurodegeneration. Proc. Natl. Acad. Sci. U S A 108, 20772–20777. doi:10.1073/pnas.1018262108
5. Bejarano, E., Yuste, A., Patel, B., Stout, R. F. Jr., Spray, D. C., and Cuervo, A. M. (2014). Connexins modulate autophagosome biogenesis. Nat. Cell Biol. 16, 401–414. doi:10.1038/ncb2934
6. Bhalla-Gehi, R., Penuela, S., Churko, J. M., Shao, Q., and Laird, D. W. (2010). Pannexin1 and pannexin3 delivery, cell surface dynamics and cytoskeletal interactions. J. Biol. Chem. 285, 9147–9160. doi:10.1074/jbc.m109.082008
7. Boassa, D., Ambrosi, C., Qiu, F., Dahl, G., Gaietta, G., and Sosinsky, G. (2007). Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane. J. Biol. Chem. 282, 31733–31743. doi:10.1074/jbc.m702422200
8. Bond, S. R., Wang, N., Leybaert, L., and Naus, C. C. (2012). Pannexin 1 ohnologs in the teleost lineage. J. Membr. Biol. 245, 483–493. doi:10.1007/s00232-012-9497-4
9. Bruzzone, R., Hormuzdi, S. G., Barbe, M. T., Herb, A., and Monyer, H. (2003). Pannexins, a family of gap junction proteins expressed in brain. Proc. Natl. Acad. Sci. U S A 100, 13644–13649. doi:10.1073/pnas.2233464100
10. de Sousa Abreu, R., Penalva, L. O., Marcotte, E. M., and Vogel, C. (2009). Global signatures of protein and mRNA expression levels. Mol. Biosyst. 5, 1512–1526. doi:10.1039/b908315d
11. Diezmos, E. F., Sandow, S. L., Markus, I., Shevy Perera, D., Lubowski, D. Z., King, D. W., et al. (2013). Expression and localization of pannexin-1 hemichannels in human colon in health and disease. Neurogastroenterol. Motil. 25, e395–e405. doi:10.1111/nmo.12130
12. Dvoriantchikova, G., Ivanov, D., Panchin, Y., and Shestopalov, V. I. (2006). Expression of pannexin family of proteins in the retina. FEBS Lett. 580, 2178–2182. doi:10.1016/j.febslet.2006.03.026
13. Foss, E. J., Radulovic, D., Shaffer, S. A., Goodlett, D. R., Kruglyak, L., and Bedalov, A. (2011). Genetic variation shapes protein networks mainly through non-transcriptional mechanisms. PLoS Biol. 9:e1001144. doi:10.1371/journal.pbio.1001144
14. Gassmann, M., Grenacher, B., Rohde, B., and Vogel, J. (2009). Quantifying westernblots: pitfalls of densitometry. Electrophoresis 30, 1845–1855. doi:10.1002/elps.200800720
15. Guescini, M., Sisti, D., Rocchi, M. B. L., Stocchi, L., and Stocchi, V. (2008). A newreal-time PCR method to overcome significant quantitative inaccuracy due toslight amplification inhibition. BMC Bioinformatics 9:326. doi:10.1186/1471-2105-9-326
16. Gürtler, A., Kunz, N., Gomolka, M., Hornhardt, S., Friedl, A. A., McDonald, K., et al. (2013). Stain-free technology as a normalization tool in western blot analysis. Anal. Biochem. 433, 105–111. doi:10.1016/j.ab.2012.10.010
17. Ishikawa, M., Iwamoto, T., Nakamura, T., Doyle, A., Fukumoto, S., and Yamada, Y. (2011). Pannexin 3 functions as an ER Ca(2+) channel, hemichannel and gap junction to promote osteoblast differentiation. J. Cell Biol. 193, 1257–1274. doi:10.1083/jcb.201101050
18. Kim, M.-S., Pinto, S. M., Getnet, D., Nirujogi, R. S., Manda, S. S., Chaerkady, R., et al. (2014). A draft map of the human proteome. Nature 509, 575–581. doi:10.1038/nature13302
19. Kurtenbach, S., Prochnow, N., Kurtenbach, S., Klooster, J., Zoidl, C., Dermietzel, R., et al. (2013). Pannexin1 channel proteins in the zebrafish retina have shared and unique properties. PloS One 8:e77722. doi:10.1371/journal.pone.0077722
20. Ladner, C. L., Yang, J., Turner, R. J., and Edwards, R. A. (2004). Visible fluorescent detection of proteins in polyacrylamide gels without staining. Anal. Biochem.326, 13–20. doi:10.1016/j.ab.2003.10.047
21. Lai, C., Bechberger, J., and Naus, C. (2009). Pannexin2 as a novel growth regulator in C6 glioma cells. Oncogene 28, 4402–4408. doi:10.1038/onc.2009.283
22. Lai, C. P. K., Bechberger, J. F., Thompson, R. J., MacVicar, B. A., Bruzzone, R., and Naus, C. C. (2007). Tumor-suppressive effects of pannexin 1 in C6 glioma cells. Cancer Res. 67, 1545–1554. doi:10.1158/0008-5472.can-06-1396
23. Le, H. T., Sin, W. C., Lozinsky, S., Bechberger, J., Vega, J. L., Guo, X. Q., et al. (2014). Gap junction intercellular communication mediated by connexin43 in astrocytes is essential for their resistance to oxidative stress. J. Biol. Chem. 289,1345–1354. doi:10.1074/jbc.m113.508390
24. Panchin, Y. V. (2005). Evolution of gap junction proteins–the pannexin alternative. J. Exp. Biol. 208, 1415–1419. doi:10.1242/jeb.01547
25. Panchin, Y., Kelmanson, I., Matz, M., Lukyanov, K., Usman, N., and Lukyanov, S. (2000). A ubiquitous family of putative gap junction molecules. Curr. Biol. 10,R473–R474. doi:10.1016/s0960-9822(00)00576-5
26. Penuela, S., Bhalla, R., Gong, X. Q., Cowan, K. N., Celetti, S. J., Cowan, B. J., et al. (2007). 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. doi:10.1242/jcs.009514
27. Penuela, S., Bhalla, R., Nag, K., and Laird, D. W. (2009). Glycosylation regulates pannexin intermixing and cellular localization. Mol. Biol. Cell 20, 4313–4323. doi:10.1091/mbc.e09-01-0067
28. Pfaffl, M. W. (2001). A new mathematical model for relative quantification in realtime RT-PCR. Nucleic Acids Res. 29:e45. doi:10.1093/nar/29.9.e45
29. Poon, I. K. H., Chiu, Y.-H., Armstrong, A. J., Kinchen, J. M., Juncadella, I. J., Bayliss, D. A., et al. (2014). Unexpected link between an antibiotic, pannexin channelsand apoptosis. Nature 507, 329–334. doi:10.1038/nature13147
30. Raj, A., Peskin, C. S., Tranchina, D., Vargas, D. Y., and Tyagi, S. (2006). Stochastic mRNA synthesis in mammalian cells. PLoS Biol. 4:e309. doi:10.1371/journal.pbio.0040309
31. Ritz, C., and Spiess, A.-N. (2008). qpcR: an R package for sigmoidal model selection in quantitative real-time polymerase chain reaction analysis. Bioinformatics 24, 1549–1551. doi:10.1093/bioinformatics/btn227
32. Sahu, G., Sukumaran, S., and Bera, A.K. (2014). Pannexins form gap junctions with electrophysiological and pharmacological properties distinct from connexins. Sci. Rep. 4:4955. doi:10.1038/srep04955
33. Sosinsky, G. E., Boassa, D., Dermietzel, R., Duffy, H. S., Laird, D. W., MacVicar, B., et al. (2011). Pannexin channels are not gap junction hemichannels. Channels (Austin) 5, 193–197. doi:10.4161/chan.5.3.15765
34. Spiess, A.-N., Feig, C., and Ritz, C. (2008). Highly accurate sigmoidal fitting of realtime PCR data by introducing a parameter for asymmetry. BMC Bioinformatics 9:221. doi:10.1186/1471-2105-9-221
35. Swayne, L. A., Sorbara, C. D., and Bennett, S. A. L. (2010). Pannexin 2 is expressed by postnatal hippocampal neural progenitors and modulates neuronal commitment. J. Biol. Chem. 285, 24977–24986. doi:10.1074/jbc.m110.130054
36. Vanden Abeele, F., Bidaux, G., Gordienko, D., Beck, B., Panchin, Y. V., Baranova, A. V., et al. (2006). Functional implications of calcium permeability of the channel formed by pannexin 1. J. Cell Biol. 174, 535–546. doi:10.1083/jcb.200601115
37. Vogt, A., Hormuzdi, S. G., and Monyer, H. (2005). Pannexin1 and pannexin2 expression in the developing and mature rat brain. Brain Res. Mol. Brain Res. 141, 113–120. doi:10.1016/j.molbrainres.2005.08.002
38. Vonesch, C., and Unser, M. (2008). A fast thresholded landweber algorithm for wavelet-regularized multidimensional deconvolution. IEEE Trans. Image Process. 17, 539–549. doi:10.1109/tip.2008.917103
39. Wicki-Stordeur, L. E., Boyce, A. K. J., and Swayne, L. A. (2013). Analysis of a pannexin 2-pannexin 1 chimeric protein supports divergent roles for pannexin C-termini in cellular localization. Cell Commun. Adhes. 20, 73–79. doi:10.3109/15419061.2013.791681
40. Wilhelm, M., Schlegl, J., Hahne, H., Gholami, A. M., Lieberenz, M., Savitski, M. M., et al. (2014). Mass-spectrometry-based draft of the human proteome. Nature 509, 582–587. doi:10.1038/nature13319
41. Zappalà, A., Li Volti, G., Serapide, M. F., Pellitteri, R., Falchi, M., La Delia, F., et al. (2007). Expression of pannexin2 protein in healthy and ischemized brain of adult rats. Neuroscience 148, 653–667. doi:10.1016/j.neuroscience.2007.06.028
42. Zellner, M., Babeluk, R., Diestinger, M., Pirchegger, P., Skeledzic, S., and Oehler, R. (2008). Fluorescence-based western blotting for quantitation of protein biomarkers in clinical samples. Electrophoresis 29, 3621–3627. doi:10.1002/elps.200700935
43. Zhang, H., Chen, Y., and Zhang, C. (2012). Patterns of heterogeneous expression of pannexin 1 and pannexin 2 transcripts in the olfactory epithelium and olfactory bulb. J. Mol. Histol. 43, 651–660. doi:10.1007/s10735-012-9443-x
44. Zoidl, G., Kremer, M., Zoidl, C., Bunse, S., and Dermietzel, R. (2008). Molecular diversity of connexin and pannexin genes in the retina of the zebrafish danio rerio. Cell Commun. Adhes. 15, 169–183. doi:10.1080/15419060802014081