Putative multiadhesive protein from the marine sponge Geodia cydonium: Cloning of the cDNA encoding a fibronectin‐, an SRCR‐, and a complement control protein module
Abstract:Sponges (Porifera) representing the simplest metazoan phylum so far have been thought to possess no basal lamina tissue structures. One major extracellular matrix protein that is also a constitutive glycoprotein of the basal lamina is fibronectin. It was the aim of the present study to identify the native protein from the marine sponge Geodia cydonium and to isolate the corresponding cDNA. In crude extracts from this sponge protein(s) of M(r) of approximately 230 and approximately 210 kDa could be visualized b… 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.
“…Sponges constitute the oldest and lowest metazoan phylum; within them, Geodia cydonium, from the family Geodiidae, represents the oldest living group (Mü ller et al, 1999). Several alternatively spliced forms of an SRCR group A protein and a group B protein have been identified in G. cydonium (Pancer et al, 1997;Pahler et al, 1998). The group A protein has both membrane-bound and soluble forms, whereas the SRCR domain of MAP_GEOCY, the group B protein, displays high homology with those of CD5 and CD6.…”
“…The molecules identified, cloned, and expressed from sponges, mainly from Geodia cydonium and Suberites domuncula, are cell membrane receptors that are not found in fungi, plants, or Protozoa, e.g., the receptor tyrosine kinase (Müller and Schäcke 1996;Wimmer et al 1999a), integrin (Pancer et al 1997a;Wimmer et al 1999b), receptors comprising scavenger receptor cysteine-rich repeats (Pancer et al 1997b;Blumbach et al 1998), a putative multiadhesive basal lamina protein (Pahler et al 1998b), a neuronal-like metabotropic glutamate-like receptor (Perovic et al 1999), and the sponge adhesion molecules with two immunoglobulin-like domains in the extracellular part that display sequence similarity to the human inhibitory receptor Kir or to the T-cell receptor (Blumbach et al 1999;Müller et al 1999b). Furthermore, immune molecules, cytokine-like as well as immune modulatory molecules, identified in sponges, have also not yet been found in nonmetazoan organisms.…”
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.
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