ROLE OF ANKYRING IN LINKING THE SPECTRIN-BASED MEMBRANE SKELETON TO INTEGRAL MEMBRANE PROTEINS THE NA+/CA++ EXCHANGER, THE NA+/K+ ATPASE, AND VOLTAGE-GATED SODIUM CHANNELS AND ITS CONTRIBUTION TO EPILEPSY

Sanjay Kumar Choubey1, Prashant Srivastava2, Saurabh Shukla3, Gomase V.S.4
1Yeshwant College of Information Technology (Bioinformatics & Biotechnology), Parbhani, MS
2Yeshwant College of Information Technology (Bioinformatics & Biotechnology), Parbhani, MS
3Yeshwant College of Information Technology (Bioinformatics & Biotechnology), Parbhani, MS
4School of Technology, S.R.T.M. University, Sub-Centre, Latur, 413512, India

Received : -     Accepted : -     Published : 15-06-2010
Volume : 1     Issue : 1       Pages : 1 - 9
J Biotechnol Lett 1.1 (2010):1-9
DOI : http://dx.doi.org/10.9735/0976-7045.1.1.1-9

Conflict of Interest : None declared

Cite - MLA : Sanjay Kumar Choubey, et al "ROLE OF ANKYRING IN LINKING THE SPECTRIN-BASED MEMBRANE SKELETON TO INTEGRAL MEMBRANE PROTEINS THE NA+/CA++ EXCHANGER, THE NA+/K+ ATPASE, AND VOLTAGE-GATED SODIUM CHANNELS AND ITS CONTRIBUTION TO EPILEPSY." Journal of Biotechnology Letters 1.1 (2010):1-9. http://dx.doi.org/10.9735/0976-7045.1.1.1-9

Cite - APA : Sanjay Kumar Choubey, Prashant Srivastava, Saurabh Shukla, Gomase V.S. (2010). ROLE OF ANKYRING IN LINKING THE SPECTRIN-BASED MEMBRANE SKELETON TO INTEGRAL MEMBRANE PROTEINS THE NA+/CA++ EXCHANGER, THE NA+/K+ ATPASE, AND VOLTAGE-GATED SODIUM CHANNELS AND ITS CONTRIBUTION TO EPILEPSY. Journal of Biotechnology Letters, 1 (1), 1-9. http://dx.doi.org/10.9735/0976-7045.1.1.1-9

Cite - Chicago : Sanjay Kumar Choubey, Prashant Srivastava, Saurabh Shukla, and Gomase V.S. "ROLE OF ANKYRING IN LINKING THE SPECTRIN-BASED MEMBRANE SKELETON TO INTEGRAL MEMBRANE PROTEINS THE NA+/CA++ EXCHANGER, THE NA+/K+ ATPASE, AND VOLTAGE-GATED SODIUM CHANNELS AND ITS CONTRIBUTION TO EPILEPSY." Journal of Biotechnology Letters 1, no. 1 (2010):1-9. http://dx.doi.org/10.9735/0976-7045.1.1.1-9

Copyright : © 2010, Sanjay Kumar Choubey, et al, Published by Bioinfo Publications. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution and reproduction in any medium, provided the original author and source are credited.

Abstract

There are specific alterations in the structure or function of ion channels in the epileptic brain. Few of the alterations may trigger hyperexcitability and the others prevent nerve cells from being damaged due to epileptic discharges. Ion channels assist in regulation of the excitation in the CNS. Mutation in ion channel genes contributes to epileptic seizures. AnkyrinG, a family of adaptor proteins helps in association of integral membrane proteins to the spectrin-actin based membrane skeleton. Abscence of AnkyrinG expression may lead to impaired ability in generating action potential. Sodium ion channel requires AnkyrinG for its proper localization. In absence of AnkyrinG clustering of voltage gated sodium channel is affected which is required for generating action potential.

References

[1] Davis, J.Q., S. Lambert, and V. Bennett. (1996). Molecular composition of the node of Ranvier: identification of ankyrin-binding cell adhesion molecules neurofascin (mucin+/third FNIII domain-) and NrCAM at nodal axon segments. J. Cell Biol. 135:1355– 1367.  
» CrossRef   » Google Scholar   » PubMed   » DOAJ   » CAS   » Scopus  

[2] Davis, J.Q., T. McLaughlin, and V. Bennett. (1993) Ankyrin-binding proteins related to nervous system cell adhesion molecules: candidates to provide transmembrane and intercellular connections in adult brain. J. Cell Biol. 121: 121–133.  
» CrossRef   » Google Scholar   » PubMed   » DOAJ   » CAS   » Scopus  

[3] Hortsch, M. (2000) Structural and functional evolution of the L1 family: are four adhesion molecules better than one? Mol. Cell Neurosci. 15: 1–10.  
» CrossRef   » Google Scholar   » PubMed   » DOAJ   » CAS   » Scopus  

[4] Jenkins, S.M., K. Kizhatil, N.R. Kramarcy, A. Sen, R. Sealock, and V. Bennett. (2001) FIGQY-phosphorylation defines discrete populations of L1 cell adhesion molecules at sites of cell-cell contact and in migrating neurons. J. Cell Sci. In press.  
» CrossRef   » Google Scholar   » PubMed   » DOAJ   » CAS   » Scopus  

[5] Kaplan, M.R., A. Meyer-Franke, S. Lambert, V. Bennett, I.D. Duncan, S.R. Levinson,and B.A. Barres. (1997) Induction of sodium channel clustering by oligodendrocytes. Nature. 386: 724–728.  
» CrossRef   » Google Scholar   » PubMed   » DOAJ   » CAS   » Scopus