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MeSH Review

Conus Snail

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Disease relevance of Conus Snail

  • The malformation was associated with bilateral conus, 1-transposition of the great arteries, and subpulmonary ventricular septal defect without significant pulmonary stenosis in situs solitus [1].
  • Frequently associated anomalies included ventricular septal defect (17 patients), atrioventricular valve malformations (17) subaortic conus (14) and pulmonary outflow tract stenosis or atresia (11) [2].
  • In the present case, an infant was discovered to have a lesion most closely resembling a capillary hemangioma involving the skin of the midline and right buttock, the deep soft tissues of the right buttock, the dura, and the conus medullaris [3].
  • Aortic regurgitation developed in two patients from possible trauma during the operation: Regurgitation was mild (causing symptoms) in one patient who had had poor surgical exposure with a subpulmonic ventricular septal defect and a well-developed subaortic conus; it was trivial (asymptomatic) in the other patient [4].
  • A 67-year-old man with non-insulin-dependent diabetes mellitus progressively developed, over a 2-year period, lower extremity sensory and motor defects associated with impaired bladder function and perineal and perianal sensation related to a disease of the conus medullaris extending from T12 to S5 [5].

High impact information on Conus Snail

  • Conus peptides targeted to specific nicotinic acetylcholine receptor subtypes [6].
  • The venom of the fish-eating marine mollusc, Conus geographus, contains several neurotoxic peptides having different targets [7].
  • One class targets alpha1-adrenoceptors (rho-TIA from the fish-hunting Conus tulipa), and the second class targets the neuronal noradrenaline transporter (chi-MrIA and chi-MrIB from the mollusk-hunting C. marmoreus). rho-TIA and chi-MrIA selectively modulate these important membrane-bound proteins [8].
  • Conotoxins are small cysteine rich peptides found in the venom of the predatory cone snails (Conus) which have prove to be useful high affinity ligands for various receptors and ion channels [9].
  • We demonstrate here that the correct folding of a Conus peptide is facilitated by a posttranslationally modified amino acid, gamma-carboxyglutamate [10].

Chemical compound and disease context of Conus Snail

  • Retrobulbar injection of 3 ml isotonic metrizamide in the muscular conus of rabbits causes slight and inconstant cellulitis, but a similar reaction can also be found after injection of the same amount of saline [11].
  • His MRI showed cord expansion at the tip of the conus medullaris; contrast enhancement with Gadolinium revealed a cystic lesion and histopathology confirmed the diagnosis of a dermoid cyst [12].

Biological context of Conus Snail

  • A novel post-translational modification involving bromination of tryptophan. Identification of the residue, L-6-bromotryptophan, in peptides from Conus imperialis and Conus radiatus venom [13].
  • Patterns of cladogenesis in the venomous marine gastropod genus Conus from the Cape Verde islands [14].
  • The alpha-CnIA inhibited the fixation of iodinated alpha-bungarotoxin to Torpedo nicotinic acetylcholine receptors with an IC50 of 0.19 microM which can be compared to the IC50 of 0.31 microM found for the previously characterized alpha-MI isolated from the piscivorous Conus magus [15].
  • We purified and characterized a peptide from the venom of Conus textile that makes normal mice assume the phenotype of a well-known mutant, the spasmodic mouse [16].
  • Urodynamic evaluation in 5 patients with a conus lesion showed a variety of detrusor responses ranging from hyperreflexia through areflexia with decreased compliance to areflexia with normal compliance [17].

Anatomical context of Conus Snail

  • These nicotinic antagonist peptides from Conus are broadly divided into two groups: those that act at the neuromuscular junction and those that act at subtypes of neuronal nicotinic acetylcholine receptors [6].
  • This inward current could be distinguished from the native barium current of control oocytes by its high sensitivity to blockade by cadmium ions and its inhibition by omega-conotoxin, a peptide neurotoxin from Conus geographicus [18].
  • Two polypeptide toxins which modulate the uptake of 45Ca2+ in bovine chromaffin cells were isolated from the venom of the marine snail Conus distans [19].
  • We studied the protein expression of GAP-43 within the conus medullaris portion of the spinal cord in adult male rats [20].
  • Magnetic resonance imaging of the spine demonstrated intense gadolinium enhancement of the cauda equina, whereas the conus medullaris appeared normal [21].

Associations of Conus Snail with chemical compounds

  • The release of SP, as measured by radioimmunoassay (RIA), was characterized in terms of its dependence on extracellular calcium ion, its stimulus-response relationship, its sensitivity to the calcium-channel blocker omega conus toxin (omega-CgTx), and its modulation by the DHPs Bay K 8644 and nifedipine [22].
  • This observation suggests that like conantokin-G (a homologous Conus peptide with recently identified NMDA antagonist activity) conantokin-T has NMDA antagonist activity [23].
  • Here, we report a new family of Conus peptides, which have a novel cysteine motif [24].
  • This small island chain located in the Central Atlantic hosts 10% of the worldwide species diversity of Conus [14].
  • We have purified contulakin-G, a 16-amino acid O-linked glycopeptide (pGlu-Ser-Glu-Glu-Gly-Gly-Ser-Asn-Ala-Thr-Lys-Lys-Pro-Tyr-Ile-Leu-OH, pGlu is pyroglutamate) from Conus geographus venom [25].

Gene context of Conus Snail

  • Conantokins are small peptides (17-27 amino acids) found in the venoms of cone snails (Conus sp.) that inhibit the activity of N-methyl-D-aspartate (NMDA) receptors [26].
  • In vitro and in vivo characterization of conantokin-R, a selective NMDA receptor antagonist isolated from the venom of the fish-hunting snail Conus radiatus [27].
  • We synthesized and characterized new chimera peptides by inserting an epitope of the mucin 1 glycoprotein (MUC1) as a 'guest' sequence in the 'host' structure of alpha-conotoxin GI, a 13-residue peptide (ECCNPACGRHYSC) isolated from the venom of Conus geographus [28].
  • Given the functional similarity of mammalian vitamin K-dependent carboxylases and the vitamin K-dependent carboxylase from Conus textile, a marine invertebrate, we hypothesized that structurally conserved regions would identify sequences critical to this common functionality [29].
  • CGX-1007, a 17-amino acid polypeptide isolated from the venom of Conus geographus, is a novel NMDA receptor antagonist that is selective for the NR2B subunit [30].

Analytical, diagnostic and therapeutic context of Conus Snail


  1. Successful repair of double-outlet right ventricle with bilateral conus, 1-transposition of great arteries (S,D,L), and subpulmonary ventricular septal defect. Yamaguchi, M., Horikoshi, K., Toriyama, A., Kimura, K., Mito, H. J. Thorac. Cardiovasc. Surg. (1976) [Pubmed]
  2. Echocardiographic and angiographic findings in superior-inferior cardiac ventricles. Héry, E., Jimenez, M., Didier, D., van Doesburg, N.H., Guérin, R., Fouron, J.C., Davignon, A. Am. J. Cardiol. (1989) [Pubmed]
  3. Metameric capillary hemangioma producing complete myelographic block in an infant. Case report. Mawk, J.R., Leibrock, L.G., McComb, R.D., Trembath, E.J. J. Neurosurg. (1987) [Pubmed]
  4. Transaortic closure of ventricular septal defect in atrioventricular discordance with pulmonary stenosis or atresia. Results in five patients. Matsuda, H., Kawashima, Y., Hirose, H., Nakano, S., Shirakura, R., Shimazaki, Y., Nagai, I. J. Thorac. Cardiovasc. Surg. (1984) [Pubmed]
  5. Progressive necrosis of the conus medullaris: magnetic resonance imaging and surgical findings. de Toffol, B., Cotty, P., Gaymard, B., Velut, S. Neurosurgery (1990) [Pubmed]
  6. Conus peptides targeted to specific nicotinic acetylcholine receptor subtypes. McIntosh, J.M., Santos, A.D., Olivera, B.M. Annu. Rev. Biochem. (1999) [Pubmed]
  7. A venom peptide with a novel presynaptic blocking action. Kerr, L.M., Yoshikami, D. Nature (1984) [Pubmed]
  8. Two new classes of conopeptides inhibit the alpha1-adrenoceptor and noradrenaline transporter. Sharpe, I.A., Gehrmann, J., Loughnan, M.L., Thomas, L., Adams, D.A., Atkins, A., Palant, E., Craik, D.J., Adams, D.J., Alewood, P.F., Lewis, R.J. Nat. Neurosci. (2001) [Pubmed]
  9. Constant and hypervariable regions in conotoxin propeptides. Woodward, S.R., Cruz, L.J., Olivera, B.M., Hillyard, D.R. EMBO J. (1990) [Pubmed]
  10. Efficient oxidative folding of conotoxins and the radiation of venomous cone snails. Bulaj, G., Buczek, O., Goodsell, I., Jimenez, E.C., Kranski, J., Nielsen, J.S., Garrett, J.E., Olivera, B.M. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  11. Orbitography with a new non-ionizing water-soluble contrast medium. Evensen, A., Johansen, J.G., Udnaes, I., Arnesen, K. Acta ophthalmologica. (1976) [Pubmed]
  12. Dermoid of the conus medullaris. Krishna, K.K., Agarwal, P.A., Agarwal, S.I., Jain, M.M. Journal of clinical neuroscience : official journal of the Neurosurgical Society of Australasia. (2004) [Pubmed]
  13. A novel post-translational modification involving bromination of tryptophan. Identification of the residue, L-6-bromotryptophan, in peptides from Conus imperialis and Conus radiatus venom. Craig, A.G., Jimenez, E.C., Dykert, J., Nielsen, D.B., Gulyas, J., Abogadie, F.C., Porter, J., Rivier, J.E., Cruz, L.J., Olivera, B.M., McIntosh, J.M. J. Biol. Chem. (1997) [Pubmed]
  14. Patterns of cladogenesis in the venomous marine gastropod genus Conus from the Cape Verde islands. Cunha, R.L., Castilho, R., Rüber, L., Zardoya, R. Syst. Biol. (2005) [Pubmed]
  15. Biochemical characterization and nuclear magnetic resonance structure of novel alpha-conotoxins isolated from the venom of Conus consors. Favreau, P., Krimm, I., Le Gall, F., Bobenrieth, M.J., Lamthanh, H., Bouet, F., Servent, D., Molgo, J., Ménez, A., Letourneux, Y., Lancelin, J.M. Biochemistry (1999) [Pubmed]
  16. The spasmodic peptide defines a new conotoxin superfamily. Lirazan, M.B., Hooper, D., Corpuz, G.P., Ramilo, C.A., Bandyopadhyay, P., Cruz, L.J., Olivera, B.M. Biochemistry (2000) [Pubmed]
  17. Detrusor function with lesions of the conus medullaris. Beric, A., Light, J.K. J. Urol. (1992) [Pubmed]
  18. Expression of an omega-conotoxin-sensitive calcium channel in Xenopus oocytes injected with mRNA from Torpedo electric lobe. Umbach, J.A., Gundersen, C.B. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  19. Two polypeptide toxins with opposite effects on calcium uptake in bovine chromaffin cells: isolation from the venom of the marine snail Conus distans. Partoens, P., Wang, J.M., Coen, E.P., Vauquelin, G., De Potter, W.P. Neurochem. Int. (1996) [Pubmed]
  20. Differential distribution of growth associated protein (GAP-43) in the motor nuclei of the adult rat conus medullaris. Warner, E.A., Deyoung, D.Z., Hoang, T.X., Franchini, B.T., Westerlund, U., Havton, L.A. Experimental brain research. Experimentelle Hirnforschung. Expérimentation cérébrale. (2005) [Pubmed]
  21. Cauda equina syndrome complicating pneumococcal meningitis. Kikuchi, M., Nagao, K., Muraosa, Y., Ohnuma, S., Hoshino, H. Pediatric neurology. (1999) [Pubmed]
  22. Characterization of the electrically evoked release of substance P from dorsal root ganglion neurons: methods and dihydropyridine sensitivity. Holz, G.G., Dunlap, K., Kream, R.M. J. Neurosci. (1988) [Pubmed]
  23. Conantokin-T. A gamma-carboxyglutamate containing peptide with N-methyl-d-aspartate antagonist activity. Haack, J.A., Rivier, J., Parks, T.N., Mena, E.E., Cruz, L.J., Olivera, B.M. J. Biol. Chem. (1990) [Pubmed]
  24. lambda-conotoxins, a new family of conotoxins with unique disulfide pattern and protein folding. Isolation and characterization from the venom of Conus marmoreus. Balaji, R.A., Ohtake, A., Sato, K., Gopalakrishnakone, P., Kini, R.M., Seow, K.T., Bay, B.H. J. Biol. Chem. (2000) [Pubmed]
  25. Contulakin-G, an O-glycosylated invertebrate neurotensin. Craig, A.G., Norberg, T., Griffin, D., Hoeger, C., Akhtar, M., Schmidt, K., Low, W., Dykert, J., Richelson, E., Navarro, V., Mazella, J., Watkins, M., Hillyard, D., Imperial, J., Cruz, L.J., Olivera, B.M. J. Biol. Chem. (1999) [Pubmed]
  26. Conantokins: peptide antagonists of NMDA receptors. Layer, R.T., Wagstaff, J.D., White, H.S. Current medicinal chemistry. (2004) [Pubmed]
  27. In vitro and in vivo characterization of conantokin-R, a selective NMDA receptor antagonist isolated from the venom of the fish-hunting snail Conus radiatus. White, H.S., McCabe, R.T., Armstrong, H., Donevan, S.D., Cruz, L.J., Abogadie, F.C., Torres, J., Rivier, J.E., Paarmann, I., Hollmann, M., Olivera, B.M. J. Pharmacol. Exp. Ther. (2000) [Pubmed]
  28. Synthesis and antibody recognition of mucin 1 (MUC1)-alpha-conotoxin chimera. Drakopoulou, E., Uray, K., Mezö, G., Price, M.R., Vita, C., Hudecz, F. J. Pept. Sci. (2000) [Pubmed]
  29. A conserved motif within the vitamin K-dependent carboxylase gene is widely distributed across animal phyla. Begley, G.S., Furie, B.C., Czerwiec, E., Taylor, K.L., Furie, G.L., Bronstein, L., Stenflo, J., Furie, B. J. Biol. Chem. (2000) [Pubmed]
  30. The effect of CGX-1007 and CI-1041, novel NMDA receptor antagonists, on kindling acquisition and expression. Barton, M.E., White, H.S. Epilepsy Res. (2004) [Pubmed]
  31. Supine metrizamide myelography: a technique for achieving excellent visualization of the thoracic cord and conus medullaris. Russell, E.J., Pinto, R., Kricheff, I.L. Radiology. (1980) [Pubmed]
  32. Longitudinal study on occlusal force distribution in lower distal-extension removable partial dentures with conus crown telescopic system. Ogata, K., Ishii, A., Shimizu, K., Watanabe, N. Journal of oral rehabilitation. (1993) [Pubmed]
  33. Electrical stimulation of the conus medullaris to control the bladder in the paraplegic patient. A 10-year review. Nashold, B.S., Friedman, H., Grimes, J. Applied neurophysiology. (1981) [Pubmed]
  34. Thoracolumbar intradural extramedullary bronchiogenic cyst. Baumann, C.R., Könü, D., Glatzel, M., Siegel, A.M. Acta neurochirurgica. (2005) [Pubmed]
  35. Vasoactive peptides in the heart of Champsocephalus gunnari. Masini, M.A., Sturla, M., Uva, B.M. Comp. Biochem. Physiol. A Physiol. (1997) [Pubmed]
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