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American Journal of Advanced Drug Delivery

ISSN - 2321-547X

Review Article - (2020) Volume 8, Issue 4

CHEMICAL ENGINEERING IN HUMAN BODY

 

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Abstract

Ion channels are pore–forming membrane proteins that allow ions to pass through the channel pore. Their functions include establishing a resting membrane potential, shaping action potentials and other electrical signals by gating the flow of ions across the cell membrane, controlling the flow of ions across secretory and epithelial cells, and regulating cell volume. Ion channels are present in the membranes of all cells. Ion channels are one of the two classes of ionophoric proteins, the other being ion transporters. The study of ion channels often involves biophysics, electrophysiology, and pharmacology, while using techniques including voltage clamp, patch clamp, immunohistochemistry, X–ray crystallography, fluoroscopy, and RT–PCR. Their classification as molecules is referred to as channelomics. The fundamental properties of currents mediated by ion channels were analyzed by the British biophysicists Alan Hodgkin and Andrew Huxley as part of their Nobel Prize–winning research on the action potential, published in 1952. They built on the work of other physiologists, such as Cole and Baker's research into voltage–gated membrane pores from 1941. The existence of on channels was confirmed in the 1970s by Bernard Katz and Ricardo Miledi using noise analysis. It was then shown more directly with an electrical recording technique known as the "patch clamp", which led to a Nobel Prize to Erwin Neher and Bert Sakmann, the technique's inventors. Hundreds if not thousands of researchers continue to pursue a more detailed understanding of how these proteins work. In recent years the development of automated patch clamp devices helped to increase significantly the throughput in ion channel screening.

The Nobel Prize in Chemistry for 2003 was awarded to Roderick MacKinnon for his studies on the physico–chemical properties of ion channel structure and function, including x–ray crystallographic structure studies.

References

  1. Abdul Kadir L, Stacey M, Barrett–Jolley R et al. Emerging roles of the membrane potential: action beyond the action potential. Front Physiol. (2018) 9: 1661.
  2. Alexander SP, Mathie A, Peters JA. Ion channels. British Journal of Pharmacology. (2011) 164: S137–S174.
  3. Purves D, Augustine GJ, Fitzpatrick D et al. Chapter 4: Channels and transporters. Neuroscience. 2nd edition. (2001).   
  4. Siegel GJ, Agranoff BW, Albers RW et al. Basic neurochemistry: molecular, cellular, and medical aspects. Am Soc Neurochem. (1999).
  5. Camerino DC, Tricarico D and Desaphy JF. Ion channel pharmacology. Neurother. (2007) 4: 184–198
  6. Verkman AS and Galietta LJ. Chloride channels as drug targets. Nat Rev Drug Discov. (2009) 8 (2): 153-171
  7. Camerino DC, Desaphy JF, Tricarico D et al. Therapeutic approaches to ion channel diseases. Adv Genet (2008) 64: 81-145.
  8. Gabashvili IS, Sokolowski BH, Morton CC et al. Ion channel gene expression in the inner ear. J Assoc Res Otolaryngol (2007) 8: 305-28.
  9. Vicini S. New perspectives in the functional role of GABA(A) channel heterogeneity. Mol Neurobiol (1999) 19: 97–110.
  10. Hanukoglu I. ASIC and ENaC type sodium channels: conformational states and the structures of the ion selectivity filters. FEBS J. (2017) 284: 525-545.
  11. Hansen SB. Lipid agonism: The PIP2 paradigm of ligand–gated ion channels. Bba-Mol Cell Biol L. (2015) 1851: 620-8.
  12. Hansen SB, Tao X and MacKinnon R. Structural basis of PIP2 activation of the classical inward rectifier K+ channel Kir2.2. Nature. (2011) 477: 495-8.
  13. Gao Y, Cao E, Julius D et al. TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action. Nature. (2016) 534: 347-51.
  14. Cabanos C, Wang M, Han X et al. A soluble fluorescent binding assay reveals PIP2 antagonism of TREK–1 channels. Cell Rep. (2017) 20: 1287-1294.
  15. Brown DA, Passmore GM. Neural KCNQ (Kv7) channels. Br J Pharmacol. (2009) 156: 1185-1195
  16. Kintzer AF, Stroud RM. Structure, inhibition and regulation of two–pore channel TPC1 from Arabidopsis thaliana. Nature. (2016) 531: 258-62.
  17. Spalding EP, Harper JF. The ins and outs of cellular Ca(2+) transport. Curr Opin Plant Biol. (2011) 14: 715-20.

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