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Gene Review

Apamin  -  apamin protein

Apis mellifera

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Disease relevance of Apamin


High impact information on Apamin

  • Single apamin-blocked Ca-activated K+ channels of small conductance in cultured rat skeletal muscle [6].
  • We show here for the first time that muscle membranes of patients with myotonic muscular dystrophy contain the receptor for apamin, a bee venom toxin known to be a specific and high-affinity blocker of one class of Ca2+-activated K+ channels in mammalian muscle [4].
  • Apamin is a neurotoxic polypeptide of known structure isolated from bee venom [7].
  • The Ca2+-dependent slow K+ conductance in cultured rat muscle cells: characterization with apamin [8].
  • Voltage-clamp analyses have shown that apamin, at low concentrations, specifically blocks the Ca2+-dependent slow K+ conductance in rat myotubes and myosacs . A specific binding site for apamin in rat muscle cell membranes has been characterized with the use of a highly radiolabelled apamin derivative [( 125I]apamin) [8].

Chemical compound and disease context of Apamin


Biological context of Apamin

  • From a cDNA library prepared from venom glands of worker bees, clones encoding the precursors of apamin and MCD peptide have been isolated [9].
  • The sequence of this segment shows 81% identity to the DNA sequence preceding the first exon of the apamin gene and both contain a putative TATA box [9].
  • Starting from the 5'-end, these exons are arranged in the following order: three exons of the mast cell-degranulating (MCD) peptide precursor, two exons of the gene for the apamin precursor, and finally a 3'-exon present in both cDNAs [9].
  • The structural features of apamin, a natural octadecapeptide from bee venom, enabling binding to its receptor and the expression of toxicity in mice, have been delineated by studying the effects on binding and toxicity of chemical modifications and amino acid substitutions in synthetic analogues [1].
  • Apamin (10-100 nM) inhibited K(+) current activation and cell volume recovery from swelling [10].

Anatomical context of Apamin

  • Ion pair reagents were required to resolve the strongly basic peptides, secapin, mast cell degranulating (MCD-) peptide and apamin, by reversed-phase (RP) HPLC [11].
  • Apamin converted the hyperpolarization caused by ATP or Adr into a transient depolarization which produced contraction of the muscle cells [12].
  • In contrast, saturable binding of 125I-apamin to rat liver plasma membranes was virtually undetectable, thereby providing a correlation with the ability to measure apamin-sensitive Ca(2+)-activated potassium currents in rabbit and guinea pig hepatocytes but not in rat hepatocytes [13].
  • Affinity labeling was abolished on both liver and brain membranes by apamin, scyllatoxin, dequalinium, gallamine, and d-tubocurarine [13].
  • (iv) Apamin receptors detected with 125I-labeled apamin are present at fetal stages with biochemical characteristics identical to those found in myotubes in culture [14].

Associations of Apamin with chemical compounds

  • Thus, apamin folding is very cooperative, but the native structure is only modestly stabilized by urea- or temperature-denaturable secondary structure [15].
  • In contrast to apamin, it is hardly neurotoxic upon intravenous injection in mice [2].
  • An Amino Acid Outside the Pore Region Influences Apamin Sensitivity in Small Conductance Ca2+-activated K+ Channels [16].
  • 5. Apamin (10 nM) also abolished the increase in 42K efflux which follows the application of the alpha-adrenoceptor agonist amidephrine to rabbit liver slices; the concurrent rises in 45Ca efflux and glucose release were unaffected [17].
  • Apamin, in contrast to quinine or A23187, also failed to affect bioelectrical activity in mouse islet cells [18].

Other interactions of Apamin


Analytical, diagnostic and therapeutic context of Apamin


  1. Binding and toxicity of apamin. Characterization of the active site. Labbé-Jullié, C., Granier, C., Albericio, F., Defendini, M.L., Ceard, B., Rochat, H., Van Rietschoten, J. Eur. J. Biochem. (1991) [Pubmed]
  2. Neurotoxicity of apamin and MCD peptide upon central application. Habermann, E. Naunyn Schmiedebergs Arch. Pharmacol. (1977) [Pubmed]
  3. Possible increases in potassium conductance by apamin in mammalian ventricular papillary muscles: a comparison with the effects on enzymatically isolated ventricular cells. Nakagawa, A., Nakamura, S., Arita, M. J. Cardiovasc. Pharmacol. (1989) [Pubmed]
  4. Expression of apamin receptor in muscles of patients with myotonic muscular dystrophy. Renaud, J.F., Desnuelle, C., Schmid-Antomarchi, H., Hugues, M., Serratrice, G., Lazdunski, M. Nature (1986) [Pubmed]
  5. Possible role of apamin-sensitive K+ channels in myotonic dystrophy. Behrens, M.I., Jalil, P., Serani, A., Vergara, F., Alvarez, O. Muscle Nerve (1994) [Pubmed]
  6. Single apamin-blocked Ca-activated K+ channels of small conductance in cultured rat skeletal muscle. Blatz, A.L., Magleby, K.L. Nature (1986) [Pubmed]
  7. Apamin blocks certain neurotransmitter-induced increases in potassium permeability. Banks, B.E., Brown, C., Burgess, G.M., Burnstock, G., Claret, M., Cocks, T.M., Jenkinson, D.H. Nature (1979) [Pubmed]
  8. The Ca2+-dependent slow K+ conductance in cultured rat muscle cells: characterization with apamin. Hugues, M., Schmid, H., Romey, G., Duval, D., Frelin, C., Lazdunski, M. EMBO J. (1982) [Pubmed]
  9. The precursors of the bee venom constituents apamin and MCD peptide are encoded by two genes in tandem which share the same 3'-exon. Gmachl, M., Kreil, G. J. Biol. Chem. (1995) [Pubmed]
  10. Molecular characterization of volume-sensitive SK(Ca) channels in human liver cell lines. Roman, R., Feranchak, A.P., Troetsch, M., Dunkelberg, J.C., Kilic, G., Schlenker, T., Schaack, J., Fitz, J.G. Am. J. Physiol. Gastrointest. Liver Physiol. (2002) [Pubmed]
  11. Isolation and structure analysis of bee venom mast cell degranulating peptide. Dotimas, E.M., Hamid, K.R., Hider, R.C., Ragnarsson, U. Biochim. Biophys. Acta (1987) [Pubmed]
  12. The action of apamin on guinea-pig taenia caeci. Maas, A.J., Den Hertog, A., Ras, R., Van den Akker, J. Eur. J. Pharmacol. (1980) [Pubmed]
  13. Comparable 30-kDa apamin binding polypeptides may fulfill equivalent roles within putative subtypes of small conductance Ca(2+)-activated K+ channels. Wadsworth, J.D., Doorty, K.B., Strong, P.N. J. Biol. Chem. (1994) [Pubmed]
  14. The all-or-none role of innervation in expression of apamin receptor and of apamin-sensitive Ca2+-activated K+ channel in mammalian skeletal muscle. Schmid-Antomarchi, H., Renaud, J.F., Romey, G., Hugues, M., Schmid, A., Lazdunski, M. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  15. Cooperative disulfide bond formation in apamin. Chau, M.H., Nelson, J.W. Biochemistry (1992) [Pubmed]
  16. An Amino Acid Outside the Pore Region Influences Apamin Sensitivity in Small Conductance Ca2+-activated K+ Channels. Nolting, A., Ferraro, T., D'hoedt, D., Stocker, M. J. Biol. Chem. (2007) [Pubmed]
  17. Effects of quinine and apamin on the calcium-dependent potassium permeability of mammalian hepatocytes and red cells. Burgess, G.M., Claret, M., Jenkinson, D.H. J. Physiol. (Lond.) (1981) [Pubmed]
  18. Resistance to apamin of the Ca2+-activated K+ permeability in pancreatic B-cells. Lebrun, P., Atwater, I., Claret, M., Malaisse, W.J., Herchuelz, A. FEBS Lett. (1983) [Pubmed]
  19. A comparative structural study of apamin and related bee venom peptides. Hider, R.C., Ragnarsson, U. Biochim. Biophys. Acta (1981) [Pubmed]
  20. Allergy to insect stings. II. Phospholipase A: the major allergen in honeybee venom. Sobotka, A.K., Franklin, R.M., Adkinson, N.F., Valentine, M., Baer, H., Lichtenstein, L.M. J. Allergy Clin. Immunol. (1976) [Pubmed]
  21. The actions of presynaptic snake toxins on membrane currents of mouse motor nerve terminals. Dreyer, F., Penner, R. J. Physiol. (Lond.) (1987) [Pubmed]
  22. The presence in pig brain of an endogenous equivalent of apamin, the bee venom peptide that specifically blocks Ca2+-dependent K+ channels. Fosset, M., Schmid-Antomarchi, H., Hugues, M., Romey, G., Lazdunski, M. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  23. Crystallization and preliminary X-ray diffraction data of the Fab fragment of a monoclonal antibody against apamin, a bee venom neurotoxin. Devaux, C., Defendini, M.L., Alzari, P.M., Abergel, C., Granier, C., Fontecilla-Camps, J.C., Alzar, P.M. FEBS Lett. (1991) [Pubmed]
  24. Synthesis of apamin, a neurotoxic peptide from bee venom. van Rietschoten, J., Granier, C., Rochat, H., Lissitzky, S., Miranda, F. Eur. J. Biochem. (1975) [Pubmed]
  25. Bicuculline methiodide potentiates NMDA-dependent burst firing in rat dopamine neurons by blocking apamin-sensitive Ca2+-activated K+ currents. Johnson, S.W., Seutin, V. Neurosci. Lett. (1997) [Pubmed]
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