title: Ethylene modulates gene expression in cells of the marine sponge Suberites domuncula and reduces the degree of apoptosis.
abstract: Sponges (phylum Porifera) live in an aqueous milieu that contains dissolved organic carbon. This is degraded photochemically by ultraviolet radiation to alkenes, particularly to ethylene. 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. In primmorphs from S. domuncula the expression of two genes is up-regulated after exposure to ethylene. The cDNA of the first gene (SDERR) isolated from S. domuncula encodes a potential ethylene-responsive protein, termed ERR_SUBDO; its putative M(r) is 32,704. Data bank search revealed that the sponge polypeptide shares high similarity (82% on amino acid level) with the corresponding plant molecule, the ethylene-inducible protein from Hevea brasiliensis. Until now no other metazoan ethylene-responsive proteins have been identified. The second gene, whose expression is up-regulated in response to ethylene is a Ca(2+)/calmodulin-dependent protein kinase II. Its cDNA, SDCCdPK, encodes a M(r) 54,863 putative kinase that shares 69% similarity with the corresponding enzyme from Drosophila melanogaster. The expression of both genes in primmorphs from S. domuncula is increased by approximately 5-fold after a 3-day incubation period with ethylene. It is concluded that also metazoan cells, with sponge cells as a model, may react to ethylene with an activation of cell metabolism including gene induction.
authors.affiliation: Institut für Physiologische Chemie, Abteilung Angewandte Molekularbiologie, Universität, Duesbergweg 6, D-55099 Mainz, Germany.
authors.forename: A
authors.initials: A
authors.lastname: Krasko
authors.forename: H C
authors.initials: HC
authors.lastname: Schröder
authors.forename: S
authors.initials: S
authors.lastname: Perovic
authors.forename: R
authors.initials: R
authors.lastname: Steffen
authors.forename: M
authors.initials: M
authors.lastname: Kruse
authors.forename: W
authors.initials: W
authors.lastname: Reichert
authors.forename: I M
authors.initials: IM
authors.lastname: Müller
authors.forename: W E
authors.initials: WE
authors.lastname: Müller
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D017209:Apoptosis; D054732:Calcium-Calmodulin-Dependent Protein Kinase Type 2; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000096:biosynthesis / Q000235:genetics; D003001:Cloning, Molecular; D005030:Ethylenes / Q000494:pharmacology*; D019143:Evolution, Molecular; D005508:Food Deprivation / Q000502:physiology; D005786:Gene Expression Regulation; D008386:Marine Biology; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000235:genetics; D011161:Porifera / Q000187:drug effects*; D014176:Protein Biosynthesis; D011506:Proteins / Q000235:genetics; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction; D015533:Transcriptional Activation
chemical_list: D005030:Ethylenes; C096319:HEVER protein, Hevea brasiliensis; D010940:Plant Proteins; D011506:Proteins; C400528:SDERR protein, Suberites domuncula; C036216:ethylene; D054732:Calcium-Calmodulin-Dependent Protein Kinase Type 2; D017871:Calcium-Calmodulin-Dependent Protein Kinases