Abstract
A cell membrane’s primary role is to create a barrier against materials transferring between cellular exterior and interior regions. However, the presence of certain natural or artificial agents (especially during treatment) such as membrane proteins (MPs), antimicrobial peptides (AMPs), etc., occasionally induces transient or stable transport events into cell membranes. These properties are often found to be highly dynamic, time dependent, and specific to the agents inducing them. The events also fall into different classes due to the diversity of their structures and mechanisms. In this chapter, we discuss in detail a few classes of such events with a special focus on their membrane effects.
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References
Andersen, O.S., Sawyer, D.B., and Koeppe II, R.E.: Bio membrane structure and Function. edited by K. R. K. Easwaran and B. Gaber (Schenectady, New York: Adenine), 227–244 (1992)
Andreu, D., Rivas, L.: Animal antibacterial peptides: an overview. Biopolymers 47, 415–433 (1999)
Anishkin, A., Sukharev, S., Colombini, M.: Searching for the molecular arrangement of trans-membrane ceramide channels. Biophys. J. 90, 2414–2426 (2006)
Apell, H.J.& Karlish, S.J.: Functional properties of Na, K-ATPase, and their structural implications, as detected with biophysical techniques. J. Membr. Biol. 180, 1–9 (2001)
Arseniev, A.S., Barsukov, I.L., Bystrov, V.F., and Ovchinnikov, Y.A.: Biol. Membr. 3, 437–62 (1986)
Ashrafuzzaman, Md. and Tuszynski, J.A.: Ion pore formation in membranes due to complex interactions between lipids and antimicrobial peptides or biomolecules. Handbook on Nanoscience, Engineering and nanotechnology. Edited by Goddard, Brenner, Lyshevki and Iafrate; Taylor& Francis Group (CRC press) (2011)
Ashrafuzzaman, Md., Tseng, C.-Y., Tuszynski, J.A. Chemotherapy drugs form ion pores in membranes due to physical interactions with lipids. (submitted) (2011)
Ashrafuzzaman, Md., Duszyk, M. and Tuszynski, J. A.: Chemotherapy drugs Thiocolchicoside and Taxol Permeabilize Lipid Bilayer Membranes by Forming Ion Pores. J. of Physics: Conf. Series 329, 012029.1–16 (2011)
Ashrafuzzaman, Md., Andersen, O.S., and McElhaney, R.N. The antimicrobial peptide gramicidin S permeabilizes phospholipid bilayer membranes without forming discrete ion channels. Biochim. Biophys. Acta 1778, 2814–2822 (2008)
Ashrafuzzaman, Md., Lampson, M.A., Greathouse, D.V., Koeppe II, R.E., Andersen, O.S.: Manipulating lipid bilayer material properties by biologically active amphipathic molecules. J. Phys.: Condens. Mat. 18, S1235–1255 (2006)
Ashrafuzzaman, M. and Tuszynski, J. Regulation of channel functions due to coupling with a lipid bilayer. Biophys. J. 98, 51a (2010) and J. Comp. Nanosci. 9, 564–570 (2012)
Bechinger, B. structure and functions of channel-forming peptides: Magainins, Secropins, Melittin and Alamethicin. J. Membr. Bio. 156: 197–211, (1997)
Bechinger, B. (1999) The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy, Biochim. Biophys. Acta 1462, 157–183.
S.E. Blondelle, R.A. Houghten, Biochemistry 31 (1992) 12688–12694.
Boheim, G. (1974) Statistical analysis of alamethicin channels in black lipid membranes. J. Mem. Biol. 19:277–303.
Brown, M.F.: Modulation of rhodopsin function by properties of the membrane bilayer. Chem. Phys. Lipids 73: 159–180 (1994)
Castano, S., Desbat, B., Laguerre, M., Dufourq, J.: Structure, orientation and affinity for interfaces and lipids of ideally amphipathic lytic \(L_iK_j\)(i=2j) peptides. Biochim. Biophys. Acta 1416, 176–194 (1999)
Cruciani, R.A., Barker, J.L., Durell, S.R., Raghunathan, G., Guy, H.R., Zasloff, M., Stanley, E.F.: Magainin 2, a natural antibiotic from frog skin, forms ion channels in lipid bilayer membranes. Eur J Pharmacol.226(4), 287–296 (1992)
Gadsby, D.C., Rakowski, R.F.& De Weer, P.: Extracellular access to the Na, K Pump: Pathway similar to ion channel. Science 260, 100–103 (1993)
Garty, H., Karlish, S.J.: Role of FXYD proteins in ion transport. Annu. Rev. Physiol. 68, 431–459 (2006)
Gazit, E., Lee, W.J., Brey, P.T., Shai, Y.: Biochemistry 33, 10681–10692 (1994)
Geering, K.: The functional role of \(\beta \) subunits in oligomeric P-type ATPases. J. Bioenerg. Biomembr. 33, 425–438 (2001)
Glynn, I. M.: Annual review prize lecture. ‘All hands to the sodium pump’. J. Physiol. (Lond.) 462, 1–30 (1993)
Grant, E., Beeler, T.J., Taylor, K.M.P., Gable, K., Roseman, M.A.: Biochemistry 31, 9912–9918, (1992)
Gruner, S.M.: Lipid membrane curvature elasticity and protein function in Biologically Inspired Physics, edited by L. Peliti (New York: Plenum): 127–135 (1991)
He, K., Ludtke, S.J., Huang, H.W., and Worcester, D.L.: Antimicrobial peptide pores in membranes detected by neutron in-plane scattering. Biochemistry 34, 15614–15618 (1995)
Helfrich, W.: Elastic properties of lipid bilayers: theory and possible experiments. Z. Naturforsch. 28C, 693–703 (1973)
Israelachvili, J.N.: Refinement of the fluid-mosaic model of membrane structure. Biochim. Biophys. Acta 469, 221–225 (1977)
Ketchem, R.R., Roux, B., and Cross, T.A. 1997. High-resolution polypeptide structure in a lamellar phase lipid environment from solid state NMR derived orientational constraints. structure 5: 1655–69.
S. Lambotte, P. Jasperse, B. Bechinger, Biochemistry 37 (1998) 16–22.
Ludtke, S.J., He, K., Heller, W.T., Harroun, T.A., Yang, L., and Huang, H.W. 1996. Membrane pores induced by magainin. Biochemistry 35:13723–13728.
Lutsenko, S.& Kaplan, J. H. An essential role for the extracellular domain of the Na, K-ATPase \(\beta \)-subunit in cation occlusion. Biochemistry 32, 6737–6743 (1993).
K. Matsuzaki, Biochim. Biophys. Acta 1376 (1998) 391–400.
Matsuzaki, K., Murase, O., Tokuda, H., Fujii, N., and Miyajima, K. 1996. An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation. Biochemistry 35: 11361–11368.
K. Matsuzaki, K. Sugishita, N. Fujii, K. Miyajima, Biochemistry 34 (1995) 3423–3429.
J. P. Morth, B. P. Pedersen, M. S. Toustrup-Jensen, T. L.-M. Sørensen, J. Petersen, J. P. Andersen, B. Vilsen, P. Nissen. Crystal structure of the sodium-potassium pump. NATURE 450: 1043–50 (2007)
O’Connell, A.M., Koeppe II, R.E., and Andersen, O.S. 1990. Kinetics of gramicidin channel formation in lipidbilayers: trans-membrane monomer association. Science 250: 1256–1259.
Perozo, E., Cortes, D.M., and Cuello, L.G. 1999. Structural Rearrangements Underlying \(K^+\)- Channel Activation Gating. Science 285: 73–78.
Perozo, E., Cortes, D.M., Sompornpisut, P., Kloda, A., and Martinac, B. 2002. Open channel structure of MscL and the gating mechanism of mechanosensitive channels. Nature 418: 942–948.
Post, R. L., Hegyvary, C.& Kume, S. Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase. J. Biol. Chem. 247, 6530–6540 (1972).
Y. Pouny, D. Rapaport, A. Mor, P. Nicolas, Y. Shai, Biochemistry 31 (1992) 12416–12423.
Sackmann, E. 1984. In Biological Membranes, edited by D. Chapman (London: Academic): 105.
S. Samanta, J. Stiban, T.K. Maugel, M. Colombini. Visualization of ceramide channels by transmission electron microscopy. Biochim. Biophys. Acta 1808: 1196–201 (2011)
M.S.P. Sansom: Curr. Opin. Colloid Interface Sci. 3 518–524 (1998)
P. Schlieper, E. De Robertis: Arch. Biochem. Biophys. 184 204–208 (1977)
J. Seelig, P. M. Macdonald and P. G. Scherer. phospholipid head groups as sensors of electric charge in membranes. Biochemistry 26; 7535–7541 (1987)
Shepherd, J. C. W.,& Buldt, G.: Biochim. Biophys. Acta 514, 83–94 (1978)
L. J. Siskind, A. Davoody, N. Lewin, S. Marshall, and M. Colombini.: Enlargement and Contracture of C2-Ceramide Channels. Biophysical Journal 85: 1560–1575 (2003)
Skou, J. C.: The influence of some cations on an adenosine triphosphatase from peripheral nerves. Biochim. Biophys. Acta 1000, 439–446 (1957)
Sobko, A.A., Kotova, E.A., Antonenko, Y.N., Zakharov, S.D., and Cramer, W.A.: Lipid dependence of the channel properties of a colicin E1-lipidtoroidal pore. The J. of Biol. Chem. 281: 14408–16 (2006)
Therien, A. G.& Blostein, R.: Mechanisms of sodium pump regulation. Am. J. Physiol. Cell Physiol. 279, C541–C566 (2000)
Townsley, L.E., Tucker, W.A., Sham, S., and Hinton, J.F.: structures of gramicidins A, B, and C incorporated into sodium dodecyl sulfate micelles. Biochemistry 40: 11676–11686 (2001)
Toyoshima, C., and Mizutani, T.: Crystal structure of the calcium pump with a bound ATP analogue. Nature 430: 529–535 (2004)
E.M. Tytler, J.P. Segrest, R.M. Epand, S.Q. Nie, R.F. Epand, V.K. Mishna, Y.V. Venkatachalapathi, G.M. Anantharamaiah, J. Biol. Chem. 268 22121 (1993)
Unwin, P.N.T., and Ennis, P.D.: Two configurations of a channel-forming membrane protein. Nature 307: 609–613 (1984)
Wieprecht, T., Dathe, M., Krause, E., Beyermann, M., Maloy, W.L., MacDonald, D.L., Bienert, M. FEBS Lett. 417: 135–140, (1997)
Yang, L., Harroun, T., Weiss, T.M., Ding, L., and Huang, H.W. Barrel-stave model or toroidal model? A case study on melittin pores. Biophys. J. 81: 1475–1485, (2001)
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Ashrafuzzaman, M., Tuszynski, J. (2012). The Membrane as a Transporter, Ion Channels and Membrane Pumps. In: Membrane Biophysics. Biological and Medical Physics, Biomedical Engineering. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-16105-6_4
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