Abstract
The dendrotoxins are a family of homologous proteins that are isolated from mamba snake venoms: namely, α-dendrotoxin (α-Dtx, β2-Dtx, γ-Dtx, and δ-Dtx from the venom of the Eastern green mamba (Dendroaspis angusticeps), two closely related peptides, toxin I and toxin K, from the venom of the black mamba (Dendroaspis polylepis plylepis), and Dv14 from the Western green mamba venom (Dendroaspis viridis) (Harvey and Karlson, 1980; 1982; Joubert and Taljaard, 1980: Strydom, 1973: Benishin et al., 1988; Harvey and Anderson, 1991) . They consist of 57–60 amino acids residue in single polypeptide chains, containing three intramolecular disulfide bonds. The crystal structure of α-dendrotoxin has been solved (Skarzynski, 1992). Dendrotoxins are highly homologous to Kunitz-type serine proteinase inhibitors, such as bovine pancreatic trypsin inhibitor (BPTI or aprotinin) (see Fig. 1). However, BPTI does not have K+ channel-blocking properties (Marshall and Harvey, 1992), and although dendrotoxins inhibit some proteinase (Marshall and Harvey, 1990), this amy be unrelated to their ability to block K+ channels. More recently, three dendrotoxins homologues, the kalicludines, were isolated from the sea anemone: Anemonia sulcata (Schweitz et al., 1995). They are several orders of magnitude less active than toxin I, and they may be more closely related to proteinase inhibitors.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Anderson, A.J. (1985). The effects of protease inhibitor homologues from mamba snake venoms on autonomic neurotransmission. Toxicon 23: 947–954
Anderson, A.J. and Harvey, A.L. (1988). Effects of the potassium channel blocking dendrotoxins on acetylcholine release and motor nerve terminal activity. Br. J. Pharmacol. 93, 215–221
Anderson, A.J., Harvey, A.L., Rowan, E.G. and Strong, P.N. (1988). Effects of charybdotoxin, a blocker of Ca2+ -activated K+ channels, on motor nerve terminals. Brit. J. Pharmacol. 95, 1329–1335
Angaut-Petit, D., Molgo, J., Connold, A.L. and Faille, L. (1987). The levator auris longus muscle of the mouse: a convenient preparation for studies of short-and long-term presynaptic effects of drugs or toxins. Neurosci. Lett. 82, 83–88
Awan, K.A. and Dolly, J.O. (1991). K+ channel sub-types in rat brain: characteristic locations revealed using 13-bungarotoxin, α-and β-dendrotoxins. Neuroscience 40, 29–39
Barrett, J.C. and Harvey, A.L. (1979). Effects of the venom of the green mamba Dendroaspis angusticeps on skeletal muscle and neuromuscular transmission. Br. J. Pharmacol. 167, 199–205
Benishin, C.G., Sorensen, R.G., Brown, W.E., Krueger, B.K. and Blaustein, M.P. (1988). Four polypeptide components of green mamba venom selectively block certain potassium channels in rat brain synaptosomes. Mol. Pharmacol. 34, 152–159
Benoit, E. and Dubois, J.M. (1986). Toxin I from the snake Dendroaspis polylepis polylepis: a high specific blocker of one type of potassium channel in myelinated nerve fibre. Brain Res. 37, 374–377
Black, A.R., Donegan, C.M., Denny, B.J. and Dolly, J.O. (1988). Solubilization and physical characterization of acceptors for dendrotoxin and β-bungarotoxin from synaptic membranes of rat brain. Biochemistry 27, 6814–6820.
Braga, M.F.M., Anderson, A.J., Harvey, A.L. and Rowan, E.G. (1992). Apparent block of K+ currents in mouse motor nerve terminals by tetrodotoxin, it-conotoxin and reduced external sodium. Brit. J. Pharmacol. 106, 91–94.
Brau, M.E., Dreyer, F., Jonas, P., Repp, H. and Vogel, W. (1990). A Icf current in Xenopus nerve fibres selectively blocked by bee and snake toxins: binding and voltage-clamp experiments. J. Physiol. 420, 365–385.
Corrette, B.J., Repp, H., Dreyer, F. and Schwarz, J.R. (1991). Two types of fast K+ channels in rat myelinated nerve fibres and their sensitivity to dendrotoxin. Pflugers Arch. 418, 408–416.
Danse, J.M., Rowan, E.G., Gasparini, S., Ducancel, F., Vatanpour, H., Young, L.C., Poorheidari, G., Lajeunesse, E., Drevet, P., Menez, R., Pinkasfeld, S., Boulain, J.-C., Harvey A.L. and Menez, A. (1994). On the site by which a-dendrotoxin binds to voltage-dependent potassium channels: site-directed mutagenesis reveals that the lysine triplet 28–30 is not essential for binding. FEBS Lett. 356, 28–30.
Dolly, J.O., Halliwell, J.V., Black, J.D., Williams, R.S., Pelchen-Matthews, A., Breeze, A.L., Mehraban, F., Othman, I.B. and Black, A.R. (1984). Botulinum neurotoxin and dendrotoxin as probes for studies on transmitter release. J. Physiol. (Paris), 79, 280–303.
Dreyer, F. and Peper, K. (1974). A mono-layer preparation of innervated skeletal muscle fibres of M. cutaneous pectoris of the frog. Plugers Arch. 348, 257–262.
Ginsborg, B.L. and Warriner, J. (1960). The isolated chick biventer cervicis nerve-muscle preparation. Brit. J. Pharmacol. 15, 410–411.
Grissmer, S., Nguyen, A.N., Aiyar, J., Hanson, D.C., Mather, R.J. and Gutman, G.A. (1994). Pharmacological characterization of 5 cloned voltage-gated K+ channels, types KV1.1, KV1.2, KV1.3, KV1.5, and KV3.1, stably expressed in mammalian cell lines. Mol. Pharmacol. 45, 1227–1234.
Halliwell, J.V., Othman, I.B., Pelchen-Matthews, A. and Dolly, J.O. (1986). Central action of dendrotoxin: selective reduction of transient K conductance in hippo-campus and binding to localized acceptors. Proc. Natl. Acad. Sci. USA 83, 493–497.
Harvey, A.L. and Anderson, A.J. (1991). Dendrotoxins: snake toxins that block potassium channels and facilitate neurotransmitter release. Snake Toxins (Harvey AL, ed) pp 131–164: New York Pergamon Press
Harvey, A.L. and Karlsson, E. (1980). Dendrotoxin from the venom of the green mamba, Dendroaspis angusticeps. A neurotoxin that enhances acetylcholine release at neuromuscular junctions. Naunyn-Schmiedebergs Arch. Pharmacol. 312, 1–6.
Harvey, A.L. and Karlsson, E. (1982). Protease inhibitor homologues from mamba venoms: facilitation of acetylcholine release and interactions with prejunctional blocking toxins. Br. J. Pharmacol. 77, 133–161.
Harvey, A.L., Anderson, A.J. and Karlsson, E. (1984). Facilitation of transmitter release by neurotoxins from snake venoms. J. Physiol. (Paris) 79, 222–227.
Hurst, R.S., Busch, A.E., Kavanaugh, M.P., Osborne, P.B., North, R.A. and Adelman, J.P. (1991). Identification of amino acid residues involved in dendrotoxin block of rat voltage-dependent potassium channels. Mol. Pharmaco1.140, 572–576.
Jonas, P., Brau, M.E., Hermsteiner, M. and Vogel, W. (1989). Single-channel recording in myelinated nerve fibres reveals one type of Na channel but different K channels. Proc. Nat. Acad. Sci. USA 86, 7238–7242.
Joubert, F.J. and Taljaard, N. (1980). The amino acid sequence of two proteinase inhibitor homologues from Dendroaspis angusticeps venom. Hoppe Seylers Z. Physiol. Chem. 361, 661–674.
Mallart, A. (1985). Electric current flowinside perineurial sheaths of mouse motor nerves. J. Physiol. 368, 565–575.
Marshall, D.L. and Harvey, A.L. (1990). Reexamination of the protease inhibitor activities of the dendrotoxins from mamba venoms. Toxicon 28, 157–158.
Marshall, D.L. and Harvey, A.L. (1992). Protease inhibitor homologs of dendrotoxin do no bind to dendrotoxin acceptors on synaptosomal membranes or facilitate neuromuscular transmission. Biol. Chem. Hoppe-Seyler 373, 707–714.
McArdle, J.J., Angaut-Petit, D., Mallart, A., Bournaud, R., Faille, L. and Brigant, J.L. (1981). Advantages of the triangularis sterni muscle for investigation of synaptic phenomena. J. Neurosci. Methods 4, 109–116.
McGivern, J., Scholfield, C.H. and Dolly, J.O. (1993). Action of a-dendrotoxin on K+ currents in nerve terminal regions of axon in rat olfactory cortex. Br. J. Pharmacol. 109, 535–538.
Moczydlowski, E., Lucchesi, K. and Ravindran, A. (1988). An emerging pharmacology of peptide toxins targeted against potassium channels. J. Membrane Biol. 105, 95–111.
Muniz, Z.M., Diniz, C.R. and Dolly, J.O. (1990). Characterisation of binding sites for δ-dendrotoxin in guinea-pig synaptosomes: relationship to acceptors for the K+ channel probe a-dendrotoxin. J. Neurochem. 54, 343–346.
Parcej, D.N. and Dolly, J.O. (1989). Dendrotoxin acceptor from bovine synaptic plasma membranes. Biochem. J. 257, 899–903.
Penner, R. and Dreyer F. (1986). Two different presynaptic calcium currents in mouse motor nerve terminals. Pflugers Arch. 406, 190–197.
Rehm, H. and Lazdunski, M. (1988). Purification and subunit structure of a putative K+-channel protein identified by its binding properties for dendrotoxin I. Proc. Natl. Acad. Sci. USA 85, 4919–4923.
Rehm, H., Pelzer, S., Cochet, C., Chambaz, E., Tempel, B.L., Trautwein, W., Pelzer, D. and Lazdunski, M. (1989a). Dendrotoxin-binding brain membrane protein displays a K+ channel activity that is stimulated by both cAMP-dependent and endogenous phosphorylations. Biochemistry 28, 6455–6460.
Rehm, H., Newitt, R.A. and Tempel, B.L. (1989b). Immunological evidence for a relationship between the dendrotoxinbinding protein and the mammalian homologue of the Drosophila shaker K+ channel. FEBS Lett. 249, 224–228.
Schweitz, H., Bruhn, T., Guillemare, E., Moinier, D., Lancelin, J.-M., Beress, L. and Lazdunski, M. (1995). Kalicludines and kaliseptine. Two different classes of sea anemone toxins for voltage-sensitive K+ channels. J. Biol. Chem. 270, 25121–25126.
Scott, V.E.S., Parcej, D.N., Keen, J.N., Findlay, J.B.C. and Dolly, J.O. (1990). a-Dendrotoxin acceptor from bovine brain is a K+ channel protein. Evidence from the N-terminal sequence of its larger subunit. J. Biol. Chem. 265, 20094–20097.
Skarzynski, T. (1992). Crystal-structure of alpha-dendrotoxin from the green mamba venom and its comparison with the structure of bovine pancreatic trypsininhibitor. J. Mol. Biol. 224, 671–683.
Sorensen, R.G. and M.P. Blaustein (1989). Rat brain dendrotoxin receptors associated with voltage-gated potassium channels: dendrotoxin binding and receptor solubilization. Mol. Pharmacol. 36, 689–698.
Sorensen, R.G. and M.P. Blaustein (1992). Dendrotoxin acceptor sites: identification and labelling of brain potassium channels. Methods in Neurosci. 8, 235–246.
Strydom, D.J. (1973). Protease inhibitors as snake venom toxins. Nature New Biol. 243, 88–89.
Stuhmer, W., Ruppersberg, J.P., Schroter, K.H., Sakmann, B., Stocker, M., Giese, K.P., Perschke, A., Baumann, A. and Pongs, O. (1989). Molecular basis of functional diversity of voltage-gated po-tassium channels in mammalian brain EMBO J. 8, 3295–3244.
Tytgat, J., Debont, T.,Carmeliet and Daenens, P.(1995).The a-dendrotoxin footprint on a mammalian potassium channel. J. Biol. Chem. 270,24776–24781
Weller, U., Bernhardt, Y., Siemen, D., Dreyer, F., Vogel, W. and Habermann, E. (1985). Electrophysiological and neurobiochemical evidence for the blockade of a potassium channel by dendrotoxin. Naunyn-Schmiedeberg’s Arch. Pharmacol. 330, 77–83
Werkman, T.R., Kawamura, T., Yokoyama, S., Higashida, H., and Rogawski, M.A. (1992). Charybdotoxin, dendrotoxin and mast cell degranulating peptide block the voltage-activated K+ current of fibroblast cells stably transfected with NGK1 (KV1.2) K+-channel. Neuroscience 50, 935–946.
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2000 Springer Basel AG
About this chapter
Cite this chapter
Harvey, A.L., Rowan, E.G. (2000). Dendrotoxins and BPTI-like Proteins. In: Rochat, H., Martin-Eauclaire, MF. (eds) Animal Toxins. Methods and Tools in Biosciences and Medicine. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-8466-2_17
Download citation
DOI: https://doi.org/10.1007/978-3-0348-8466-2_17
Publisher Name: Birkhäuser, Basel
Print ISBN: 978-3-7643-6020-7
Online ISBN: 978-3-0348-8466-2
eBook Packages: Springer Book Archive