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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
MeSH Review

Suberites

 
 
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High impact information on Suberites

  • Stimulation of protein (collagen) synthesis in sponge cells by a cardiac myotrophin-related molecule from Suberites domuncula [1].
  • The steady-state level of expression of the Suberites lectin rises in primmorphs in response to lipopolysaccharide, an effect that was prevented by co-incubation with D-GlcNAc [2].
  • This study demonstrates that sponge cells (here the demosponge Suberites domuncula has been used), which have assembled to primmorphs, react to 5 microM ethylene with a significant up-regulation of intracellular Ca(2+) concentration and with a reduction of starvation-induced apoptosis [3].
  • Matrix-mediated canal formation in primmorphs from the sponge Suberites domuncula involves the expression of a CD36 receptor-ligand system [4].
  • We show that after the transfer of primmorphs from the demosponge Suberites domuncula to a homologous matrix (galectin), canal-like structures are formed in these 3D-cell aggregates [4].
 

Biological context of Suberites

  • In the marine sponge Suberites domuncula, genes encoding p38 and JNK kinases contain nine and twelve introns, respectively [5].
  • Increased gene expression of a cytokine-related molecule and profilin after activation of Suberites domuncula cells with xenogeneic sponge molecule(s) [6].
  • A homolog of the putative tumor suppressor QM in the sponge Suberites domuncula: downregulation during the transition from immortal to mortal (apoptotic) cells [7].
  • Ef lectin, a marker for the cell type involved in innate immunity, shares 59% to 65% identity with the marine sponge Suberites domuncula galactose-binding protein (Sd GBP) and horseshoe crab Tachypleus tridentatus tachylectin1/lectinL6 [8].
 

Anatomical context of Suberites

 

Associations of Suberites with chemical compounds

  • The primmorph system was used to demonstrate that in the demosponge Suberites domuncula the synthesis of the siliceous spicules starts intracellularly and is dependent on the concentration of silicic acid [11].
  • Bruton tyrosine kinase-like protein, BtkSD, is present in the marine sponge Suberites domuncula [12].
  • We show that retinoic acid causes tissue regression in intact individuals of the demosponge Suberites domuncula and in primmorphs, special three-dimensional cell aggregates [13].
  • We studied the effects of temperature, ammonium, and the fungicide amphotericin B on the viability of a primary-cell culture from the marine sponge Suberites domuncula using the aforementioned flow-cytometric assay [14].
  • Here we demonstrate, for the demosponge Suberites domuncula (Porifera, Demospongiae, Hadromerida), a cell surface receptor that recognizes (1-->3)-beta-D-glucans, e.g. curdlan or laminarin [15].
 

Gene context of Suberites

  • Therefore, a cDNA from the marine sponge Suberites domuncula encoding the MAPK was isolated and analyzed [16].
  • In this report we describe the isolation and genomic characterization of two T-box genes from the siliceous sponge Suberites domuncula [17].
  • In a previous report, we described the isolation and genomic characterization of two T-box genes from the siliceous sponge Suberites domuncula: a Brachyury homologue, Sd-Bra, and a Tbx2 homologue, Sd-Tbx2 [18].
  • Expression pattern of the Brachyury and Tbx2 homologues from the sponge Suberites domuncula [18].
  • Induction of DNA strand breaks and expression of HSP70 and GRP78 homolog by cadmium in the marine sponge Suberites domuncula [19].

References

  1. Stimulation of protein (collagen) synthesis in sponge cells by a cardiac myotrophin-related molecule from Suberites domuncula. Schröder, H.C., Krasko, A., Batel, R., Skorokhod, A., Pahler, S., Kruse, M., Müller, I.M., Müller, W.E. FASEB J. (2000) [Pubmed]
  2. Emergence and disappearance of an immune molecule, an antimicrobial lectin, in basal metazoa. A tachylectin-related protein in the sponge Suberites domuncula. Schröder, H.C., Ushijima, H., Krasko, A., Gamulin, V., Thakur, N.L., Diehl-Seifert, B., Müller, I.M., Müller, W.E. J. Biol. Chem. (2003) [Pubmed]
  3. Ethylene modulates gene expression in cells of the marine sponge Suberites domuncula and reduces the degree of apoptosis. Krasko, A., Schröder, H.C., Perovic, S., Steffen, R., Kruse, M., Reichert, W., Müller, I.M., Müller, W.E. J. Biol. Chem. (1999) [Pubmed]
  4. Matrix-mediated canal formation in primmorphs from the sponge Suberites domuncula involves the expression of a CD36 receptor-ligand system. Müller, W.E., Thakur, N.L., Ushijima, H., Thakur, A.N., Krasko, A., Le Pennec, G., Indap, M.M., Perovic-Ottstadt, S., Schröder, H.C., Lang, G., Bringmann, G. J. Cell. Sci. (2004) [Pubmed]
  5. Conservation of the positions of metazoan introns from sponges to humans. Müller, W.E., Böhm, M., Grebenjuk, V.A., Skorokhod, A., Müller, I.M., Gamulin, V. Gene (2002) [Pubmed]
  6. Increased gene expression of a cytokine-related molecule and profilin after activation of Suberites domuncula cells with xenogeneic sponge molecule(s). Müller, W.E., Perovic, S., Wilkesman, J., Kruse, M., Müller, I.M., Batel, R. DNA Cell Biol. (1999) [Pubmed]
  7. A homolog of the putative tumor suppressor QM in the sponge Suberites domuncula: downregulation during the transition from immortal to mortal (apoptotic) cells. Wiens, M., Koziol, C., Hassanein, H.M., Müller, I.M., Müller, W.E. Tissue & cell. (1999) [Pubmed]
  8. Isolation of Ef silicatein and Ef lectin as molecular markers for sclerocytes and cells involved in innate immunity in the freshwater sponge Ephydatia fluviatilis. Funayama, N., Nakatsukasa, M., Kuraku, S., Takechi, K., Dohi, M., Iwabe, N., Miyata, T., Agata, K. Zool. Sci. (2005) [Pubmed]
  9. Evolution of metazoan cell junction proteins: the scaffold protein MAGI and the transmembrane receptor tetraspanin in the demosponge Suberites domuncula. Adell, T., Gamulin, V., Perović-Ottstadt, S., Wiens, M., Korzhev, M., Müller, I.M., Müller, W.E. J. Mol. Evol. (2004) [Pubmed]
  10. Polarity factor 'Frizzled' in the demosponge Suberites domuncula: identification, expression and localization of the receptor in the epithelium/pinacoderm(1). Adell, T., Nefkens, I., Müller, W.E. FEBS Lett. (2003) [Pubmed]
  11. Biosilica formation in spicules of the sponge Suberites domuncula: synchronous expression of a gene cluster. Schröder, H.C., Perovic-Ottstadt, S., Grebenjuk, V.A., Engel, S., Müller, I.M., Müller, W.E. Genomics (2005) [Pubmed]
  12. Bruton tyrosine kinase-like protein, BtkSD, is present in the marine sponge Suberites domuncula. Cetkovic, H., Müller, W.E., Gamulin, V. Genomics (2004) [Pubmed]
  13. Retinoid X receptor and retinoic acid response in the marine sponge Suberites domuncula. Wiens, M., Batel, R., Korzhev, M., Müller, W.E. J. Exp. Biol. (2003) [Pubmed]
  14. The life and death of sponge cells. Sipkema, D., Snijders, A.P., Schroën, C.G., Osinga, R., Wijffels, R.H. Biotechnol. Bioeng. (2004) [Pubmed]
  15. A (1-->3)-beta-D-glucan recognition protein from the sponge Suberites domuncula. Mediated activation of fibrinogen-like protein and epidermal growth factor gene expression. Perović-Ottstadt, S., Adell, T., Proksch, P., Wiens, M., Korzhev, M., Gamulin, V., Müller, I.M., Müller, W.E. Eur. J. Biochem. (2004) [Pubmed]
  16. The mitogen-activated protein kinase p38 pathway is conserved in metazoans: cloning and activation of p38 of the SAPK2 subfamily from the sponge Suberites domuncula. Böhm, M., Schröder, H.C., Müller, I.M., Müller, W.E., Gamulin, V. Biol. Cell (2000) [Pubmed]
  17. Isolation and characterization of two T-box genes from sponges, the phylogenetically oldest metazoan taxon. Adell, T., Grebenjuk, V.A., Wiens, M., Müller, W.E. Dev. Genes Evol. (2003) [Pubmed]
  18. Expression pattern of the Brachyury and Tbx2 homologues from the sponge Suberites domuncula. Adell, T., Müller, W.E. Biol. Cell (2005) [Pubmed]
  19. Induction of DNA strand breaks and expression of HSP70 and GRP78 homolog by cadmium in the marine sponge Suberites domuncula. Schröder, H.C., Hassanein, H.M., Lauenroth, S., Koziol, C., Mohamed, T.A., Lacorn, M., Steinhart, H., Batel, R., Müller, W.E. Arch. Environ. Contam. Toxicol. (1999) [Pubmed]
 
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