Abstract:Species belonging to the lowest metazoan phylum, the sponges (Porifera), exhibit a surprisingly complex and multifaceted Bauplan (body plan). Recently, key molecules have been isolated from sponges which demonstrate that the cells of these animals are provided with characteristic metazoan adhesion and signal transduction molecules, allowing tissue formation. In order to understand which factors control the spatial organization of these cells in the sponge body plan, we screened for a cDNA encoding a soluble mo… Show more
“…10 In line with these studies it could be clarified, mainly from results with the marine sponges Suberites domuncula and Geodia cydonium, that Porifera have molecules similar to those known from the mammalian innate immune system, such as molecules containing scavenger receptor cysteine-rich domains, 11,12 cytokine-like molecules 13 or members of the (2'-5')oligoadenylate pathway. 14 ± 16 Furthermore, it could also be shown that`precursors' of the second type of immune response in mammals, the adaptive immune system, are present in sponges.…”
Sponges (Porifera) are a classical model to study the events during tissue transplantation. Applying the`insertion technique' autografts from the marine sponge Geodia cydonium fuse within 5 days. In contrast, allografts are rejected and destroyed. Here we show that during allograft rejection the cells in the grafts undergo apoptosis; 5 days after transplantation 46% of the cells show signs of apoptosis. In a previous study it was shown that during this process a tumor necrosis factor-like molecule is induced in allo-and xenografts. Molecules grouped to the superfamily of tumor necrosis factor receptors and a series of associated adapter molecules contain the characteristic death domain. Therefore, we screened for a cDNA encoding such a domain. Here we report on the first invertebrate molecule from Geodia cydonium comprising a death domain. The potential proapoptotic molecule DD2, with a calculated M r of 24 970, possesses in contrast to all known mammalian death domaincontaining proteins two such domains with highest similarity to the death domain present in human Fas/APO-1. The expression of this gene is not detectable in control tissue but strongly upregulated in allografts; only very low expression is seen in autografts. Parallel with the increase of the expression of the potential proapoptotic molecule DD2 in allografts the level of LTB 4 drastically increases from 2.5 pg/mg of protein (controls) to 389 pg LTB 4 /mg during a period of 5 days after transplantation; the level of LTB 4 in autografts does not change. Very likely in response to inflammatory reactions the LTB 4 metabolizing enzyme LTB 4 12-hydroxy-dehydrogenase is expressed both in auto-and allografts. These results demonstrate that sponges are provided with apoptotic pathways, similar to those present in deuterostomes and apparently absent in protostomes, which are composed of molecules comprising a death domain. In addition, it is suggested that in sponges LTB 4 is one metabolite which is involved in the initiation of apoptosis. It is postulated that the potential proapoptotic effect of LTB 4 is prevented in autografts by the expression of the LTB 4 12-hydroxy-dehydrogenase. Cell Death and Differentiation (2000) 7, 461 ± 469.
“…10 In line with these studies it could be clarified, mainly from results with the marine sponges Suberites domuncula and Geodia cydonium, that Porifera have molecules similar to those known from the mammalian innate immune system, such as molecules containing scavenger receptor cysteine-rich domains, 11,12 cytokine-like molecules 13 or members of the (2'-5')oligoadenylate pathway. 14 ± 16 Furthermore, it could also be shown that`precursors' of the second type of immune response in mammals, the adaptive immune system, are present in sponges.…”
Sponges (Porifera) are a classical model to study the events during tissue transplantation. Applying the`insertion technique' autografts from the marine sponge Geodia cydonium fuse within 5 days. In contrast, allografts are rejected and destroyed. Here we show that during allograft rejection the cells in the grafts undergo apoptosis; 5 days after transplantation 46% of the cells show signs of apoptosis. In a previous study it was shown that during this process a tumor necrosis factor-like molecule is induced in allo-and xenografts. Molecules grouped to the superfamily of tumor necrosis factor receptors and a series of associated adapter molecules contain the characteristic death domain. Therefore, we screened for a cDNA encoding such a domain. Here we report on the first invertebrate molecule from Geodia cydonium comprising a death domain. The potential proapoptotic molecule DD2, with a calculated M r of 24 970, possesses in contrast to all known mammalian death domaincontaining proteins two such domains with highest similarity to the death domain present in human Fas/APO-1. The expression of this gene is not detectable in control tissue but strongly upregulated in allografts; only very low expression is seen in autografts. Parallel with the increase of the expression of the potential proapoptotic molecule DD2 in allografts the level of LTB 4 drastically increases from 2.5 pg/mg of protein (controls) to 389 pg LTB 4 /mg during a period of 5 days after transplantation; the level of LTB 4 in autografts does not change. Very likely in response to inflammatory reactions the LTB 4 metabolizing enzyme LTB 4 12-hydroxy-dehydrogenase is expressed both in auto-and allografts. These results demonstrate that sponges are provided with apoptotic pathways, similar to those present in deuterostomes and apparently absent in protostomes, which are composed of molecules comprising a death domain. In addition, it is suggested that in sponges LTB 4 is one metabolite which is involved in the initiation of apoptosis. It is postulated that the potential proapoptotic effect of LTB 4 is prevented in autografts by the expression of the LTB 4 12-hydroxy-dehydrogenase. Cell Death and Differentiation (2000) 7, 461 ± 469.
“…Their expression is upregulated during fusion and rejection reactions. Among them are the allograft inflammatory factor, the (2Ј-5Ј)oligoadenylate synthetase , and a potential morphogen (Pahler et al 1998a).…”
Cells from metazoan organisms are eliminated in a variety of physiological and pathophysiological processes by apoptosis. In this report, we describe the cloning and characterization of molecules from the marine sponges Geodia cydonium and Suberites domuncula, whose domains show a high similarity to those that are found in molecules of the vertebrate Bcl-2 superfamily and of the death receptors. The Bcl-2 proteins contain up to four Bcl-2 homology regions (BH). Two Bcl-2-related molecules have been identified from sponges that are provided with two of those regions, BH1 and BH2, and are termed Bcl-2 homology proteins (BHP). The G. cydonium molecule, BHP1_GC, has a putative size of 28,164, while the related sequence from S. domuncula, BHP1_SD, has a M(r) of 24,187. Phylogenetic analyses of the entire two sponge BHPs revealed a high similarity to members of the mammalian Bcl-2 superfamilies and to the Caenorhabditis elegans Ced-9. When the two domains, BH1 and BH2, are analyzed separately, again the highest similarity was found to the members of the Bcl-2 superfamily, but a clearly lower relationship to the C. elegans BH1 and BH2 domains in Ced-9. In unrooted phylogenetic trees the sponge BH1 and BH2 are grouped among the mammalian sequences and are only distantly related to the C. elegans BH domains. The analysis of the gene structure of the G. cydonium BHP showed that the single intron present is located within the BH2 domain at the same position as in C. elegans and rat Bcl-x(L). In addition, a sponge molecule comprising two death domains has been characterized from G. cydonium. The two death domains of the potential proapoptotic molecule GC_DD2, M(r) 24,970, share a high similarity with the Fas-FADD/MORT1 domains. A death domain-containing molecule has not been identified in the C. elegans genome. The phylogenetic analysis revealed that the sponge domain originated from an ankyrin building block from which the mammalian Fas-FADD/MORT1 evolved. It is suggested that the apoptotic pathways that involve members of the Bcl-2 superfamily and of the death receptors are already present in the lowest metazoan phylum, the Porifera.
“…At present it can be postulated that the an (2′-5′)A system is involved in a cytokine-mediated pathway and/or in the protection system against viruses, present in the marine environment. The existence of cytokines or related molecules has been shown in sponges [14] and the presence of viruses in the marine milieu is well documented [56]. Studies are in progress to identify further components of the (2′-5′)A system in sponges and to elucidate the structure of the sponge (2′-5′)A synthetase gene(s).…”
Section: Discussionmentioning
confidence: 99%
“…integrin receptor [2], collagen [3] or galectin [4,5]), cell-surface receptors (tyrosine kinase receptor [6]), elements of the sensory system (crystallin [7], metabotropic glutamate receptor [8]) and homologs/modules of an immune system (immunoglobulin-like domains [9], scavenger receptor cysteine-rich domains and short consensus repeats [10], Rh-like protein [11]). These molecules were found to display high similarity to sequences from members of higher metazoan phyla [12].Recently a cDNA encoding a putative cytokine, the endothelial monocyte-activating polypeptide [13], was identified in G. cydonium [14]. The physiological role of this factor in sponges is not known.…”
mentioning
confidence: 99%
“…Recently a cDNA encoding a putative cytokine, the endothelial monocyte-activating polypeptide [13], was identified in G. cydonium [14]. The physiological role of this factor in sponges is not known.…”
Previously we reported on the presence of a high (2′-5′)oligoadenylate synthetase activity in the marine sponge Geodia cydonium [Kuusksalu, A., Pihlak, A., Müller, W. E. G. & Kelve, M. (1995) Eur. J. Biochem. 232, 351Ϫ357]. The presence of (2′-5′)oligoadenylates [(2′-5′)A] in crude sponge extract was shown by radioimmunoassay and by their HPLC comigration with authentic (2′-5′)A oligomers. In addition, the sponge (2′-5′)oligoadenylates displayed biological activity, as determined by inhibition studies of protein biosynthesis in rabbit reticulocyte lysate. In the present study individual (2′-5′)oligoadenylates synthesized by sponge enzyme were separated by HPLC. The exact composition of every oligonucleotide peak eluted was determined by matrix-assisted laser-desorption-ionization mass spectrometry (MALDI-MS) analysis. The 2′-5′ phosphodiester bond in oligoadenylates was verified by NMR analysis. Based on the high concentration of (2′-5′)A oligomers in G. cydonium and their similarity with those found in mammals we propose that the (2′-5′)A system is involved in a cytokine-mediated pathway and/ or in a protection system against viruses, present in the marine environment.Keywords : (2′-5′)oligoadenylate; Geodia cydonium ; matrix-assisted laser-desorption-ionization MS; NMR.Sponges (Porifera) are the simplest multicellular animals, which have existed since the Proteozoic period [1]. In the past few years several cDNA/gene sequences have been isolated and characterized from sponges, especially from the marine demosponge Geodia cydonium. Analyses revealed that sponges contain proteins of the extracellular matrix/basal lamina (e.g. integrin receptor [2], collagen [3] or galectin [4,5]), cell-surface receptors (tyrosine kinase receptor [6]), elements of the sensory system (crystallin [7], metabotropic glutamate receptor [8]) and homologs/modules of an immune system (immunoglobulin-like domains [9], scavenger receptor cysteine-rich domains and short consensus repeats [10], Rh-like protein [11]). These molecules were found to display high similarity to sequences from members of higher metazoan phyla [12].Recently a cDNA encoding a putative cytokine, the endothelial monocyte-activating polypeptide [13], was identified in G. cydonium [14]. The physiological role of this factor in sponges is not known. One pathway in mammalian organisms which is controlled by cytokine(s) is the (2′-5′)oligoadenylate [2′-5′(A)] system. It regulates the RNA degradation pathway and is inCorrespondence to M. Kelve,
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