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MeSH Review

Cephalopoda

 
 
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Disease relevance of Cephalopoda

  • The ability of octopus GST to bind with free Cu(II) may have important biological implications to enable cephalopods to avoid copper-induced cellular toxicity [1].
 

High impact information on Cephalopoda

  • Because homologous genes are present in vertebrates, ascidians, insects, cephalopods, and nemerteans, ey may function as a master control gene throughout the metazoa [2].
  • The sole crystallin of the scallop eye lens was found to be homologous to Omega-crystallin, a minor crystallin in cephalopods related to aldehyde dehydrogenase (ALDH) class 1/2 [3].
  • Arginine kinases were isolated from the cephalopods Nautilus pompilius, Octopus vulgaris, and Sepioteuthis lessoniana, and the cDNA-derived amino acid sequences have been determined [4].
  • Squid glutathione S-transferase. Relationships with other glutathione S-transferases and S-crystallins of cephalopods [5].
  • Three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods [6].
 

Biological context of Cephalopoda

 

Anatomical context of Cephalopoda

  • In addition progesterone may play a role in the pre-activation of spermatozoa stored in the female tract, further supporting the hypothesized parallelism between cephalopods and vertebrates [8].
  • In the framework of a wide monitoring programme on the presence of heavy metals in marine organisms caught in the South Adriatic Sea, cadmium and total mercury concentrations were determined in flesh and hepatopancreas of 512 specimens of two species of cephalopods [9].
 

Associations of Cephalopoda with chemical compounds

  • One such enzyme, aldehyde dehydrogenase (ALDH), has been recruited as a lens crystallin in certain mammals (Wistow, G., and Kim, H. (1991) J. Mol. Evol. 32, 262-269) and cephalopods (Tomarev, S., Zinovieva, R., and Piatigorsky, J. (1991) J. Biol. Chem. 266, 24226-24231) [10].
  • The oxygen carrier molecule in the cephalopods' blood is the copper-containing hemocyanin, which during turnover will release Cu(II) [1].
  • Cephalopods not previously recorded from the North Atlantic are Onychoteuthis boreali-japonicus, and Histioteuthis bonnellii corpuscula [11].
  • The absence of other alcohol dehydrogenases in cephalopods is compatible with the emergence of the ethanol-active class I type at a later stage, in lineages leading to vertebrates [12].
  • Acetylcholinesterase in tentacles of Octopus vulgaris (Cephalopoda). Histochemical localization and characterization of a specific high salt-soluble and heparin-soluble fraction of globular forms [13].
 

Gene context of Cephalopoda

  • The l-rRNA ranges in size from a minimum mol wt of 1.28 X 10(6) to a maximum weight of 1.60--1.66 X 10(6) (of warm-blooded vertebrates, Cephalopoda and Diptera); several intermediate values have been found in lower organisms and Protozoa [14].
  • Glutathione S-transferase and S-crystallins of cephalopods: evolution from active enzyme to lens-refractive proteins [15].
  • These results demonstrate that calbindin, although not identical in vertebrates and cephalopods, may be phylogenetically conserved in structure [16].
  • Occasionally, anti-RALBP antibodies were seen to react weakly with "IRBP" in some cephalopods [17].
  • Cephalopods also have at least two taxon-specific crystallins: omega-crystallin, related to aldehyde dehydrogenase, and omega-crystallin, related to a superfamily of lipid-binding proteins [18].
 

Analytical, diagnostic and therapeutic context of Cephalopoda

  • Using the cuttlefish Sepia officinalis (Cephalopoda) as a model, the cells and pathways of one of the brain nerves were labeled with paramagnetic cobalt(II) ions by conventional centripetal cobalt iontophoresis [19].
  • SDS polyacrylamide gel electrophoresis and immunoblotting were used to examine soluble proteins from the eyes of six species of cephalopods i.e. Lolliguncula brevis, Sepia officinalis, Octopus maya, Octopus bimaculoides, Rossia pacifica and Loligo opalescens [17].

References

  1. Metal-catalyzed oxidation and cleavage of octopus glutathione transferase by the Cu(II)-ascorbate system. Tang, S.S., Lin, C.C., Chang, G.G. Free Radic. Biol. Med. (1996) [Pubmed]
  2. Induction of ectopic eyes by targeted expression of the eyeless gene in Drosophila. Halder, G., Callaerts, P., Gehring, W.J. Science (1995) [Pubmed]
  3. Omega -crystallin of the scallop lens. A dimeric aldehyde dehydrogenase class 1/2 enzyme-crystallin. Piatigorsky, J., Kozmik, Z., Horwitz, J., Ding, L., Carosa, E., Robison, W.G., Steinbach, P.J., Tamm, E.R. J. Biol. Chem. (2000) [Pubmed]
  4. Arginine kinase from Nautilus pompilius, a living fossil. Site-directed mutagenesis studies on the role of amino acid residues in the Guanidino specificity region. Suzuki, T., Fukuta, H., Nagato, H., Umekawa, M. J. Biol. Chem. (2000) [Pubmed]
  5. Squid glutathione S-transferase. Relationships with other glutathione S-transferases and S-crystallins of cephalopods. Tomarev, S.I., Zinovieva, R.D., Guo, K., Piatigorsky, J. J. Biol. Chem. (1993) [Pubmed]
  6. Three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods. Ji, X., von Rosenvinge, E.C., Johnson, W.W., Tomarev, S.I., Piatigorsky, J., Armstrong, R.N., Gilliland, G.L. Biochemistry (1995) [Pubmed]
  7. Phylogenetic relationships among major species of japanese coleoid cephalopods (Mollusca: Cephalopoda) using three mitochondrial DNA sequences. Takumiya, M., Kobayashi, M., Tsuneki, K., Furuya, H. Zool. Sci. (2005) [Pubmed]
  8. Progesterone induces activation in Octopus vulgaris spermatozoa. Tosti, E., Di Cosmo, A., Cuomo, A., Di Cristo, C., Gragnaniello, G. Mol. Reprod. Dev. (2001) [Pubmed]
  9. Cadmium and total mercury in some cephalopods from the South Adriatic Sea (Italy). Storelli, M.M., Marcotrigiano, G.O. Food additives and contaminants. (1999) [Pubmed]
  10. The muscle-derived lens of a squid bioluminescent organ is biochemically convergent with the ocular lens. Evidence for recruitment of aldehyde dehydrogenase as a predominant structural protein. Montgomery, M.K., McFall-Ngai, M.J. J. Biol. Chem. (1992) [Pubmed]
  11. The diet of sperm whales (Physeter macrocephalus Linnaeus 1758) off the Azores. Clarke, M.R., Martins, H.R., Pascoe, P. Philos. Trans. R. Soc. Lond., B, Biol. Sci. (1993) [Pubmed]
  12. Cephalopod alcohol dehydrogenase: purification and enzymatic characterization. Rosario Fernández, M., Jörnvall, H., Moreno, A., Kaiser, R., Parés, X. FEBS Lett. (1993) [Pubmed]
  13. Acetylcholinesterase in tentacles of Octopus vulgaris (Cephalopoda). Histochemical localization and characterization of a specific high salt-soluble and heparin-soluble fraction of globular forms. Talesa, V., Grauso, M., Giovannini, E., Rosi, G., Toutant, J.P. Neurochem. Int. (1995) [Pubmed]
  14. Discontinuity of the large ribosomal subunit RNA and rRNA molecular weights in eukaryote evolution. Cammarano, P., Pons, S., Londei, P. Acta Biol. Med. Ger. (1975) [Pubmed]
  15. Glutathione S-transferase and S-crystallins of cephalopods: evolution from active enzyme to lens-refractive proteins. Tomarev, S.I., Chung, S., Piatigorsky, J. J. Mol. Evol. (1995) [Pubmed]
  16. Calcium binding protein in squid brain: biochemical similarity to the 28,000-Mr vitamin D-dependent calcium binding protein (calbindin-D28k). Christakos, S., Malkowitz, L., Sori, A., Sperduto, A., Feldman, S.C. J. Neurochem. (1987) [Pubmed]
  17. IRBP-like proteins in the eyes of six cephalopod species--immunochemical relationship to vertebrate interstitial retinol-binding protein (IRBP) and cephalopod retinal-binding protein. Fong, S.L., Lee, P.G., Ozaki, K., Hara, R., Hara, T., Bridges, C.D. Vision Res. (1988) [Pubmed]
  18. Lens crystallins of invertebrates--diversity and recruitment from detoxification enzymes and novel proteins. Tomarev, S.I., Piatigorsky, J. Eur. J. Biochem. (1996) [Pubmed]
  19. MR microscopy of cobalt-labeled nerve cells and pathways in an invertebrate brain (Sepia officinalis, Cephalopoda). Quast, M.J., Neumeister, H., Ezell, E.L., Budelmann, B.U. Magnetic resonance in medicine : official journal of the Society of Magnetic Resonance in Medicine / Society of Magnetic Resonance in Medicine. (2001) [Pubmed]
 
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