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  • 1
    Electronic Resource
    Electronic Resource
    Origins of immunity: transcription factors and homologues of effector genes of the vertebrate immune system expressed in sea urchin coelomocytes (1999)
    Springer
    Immunogenetics 49 (1999), S. 773-786 
    Details
    ISSN: 1432-1211
    Keywords: Key words NFKB ; GATA ; Runt ; HS1 ; SRCR
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Echinoderms share common ancestry with the chordates within the deuterostome clade. Molecular features that are shared between their immune systems and that of mammals thus illuminate the basal genetic framework on which these immune systems have been constructed during evolution. The immune effector cells of sea urchins are the coelomocytes, whose primary function is protection against invasive marine pathogens; here we identify six genes expressed in coelomocytes, homologues of which are also expressed in cells of the mammalian immune system. Three coelomocyte genes reported here encode transcription factors. These are an NFKB homologue (SpNFKB); a GATA-2/3 homologue (SpGATAc); and a runt domain factor (SpRunt-1). All three of these coelomocyte genes respond sharply to bacterial challenge: SpNFKB and SpRunt-1 genes are rapidly up-regulated, while transcripts of SpGATAc factor disappear within hours of injection of bacteria. Sham injection also activates SpNFKB and SpRunt, though with slower kinetics, but does not affect SpGATAc levels. Another gene, SpHS, encodes a protein related to the signal transduction intermediate HS1 of lymphoid cells. Two other newly discovered genes, SpSRCR1 and SpSRCR5, encode proteins featuring SRCR repeats. These genes are members of a complex family of SRCR genes all expressed specifically in coelomocytes. The SRCR repeats most closely resemble those of mammalian macrophage scavenger receptors. Remarkably, each individual sea urchin expresses a specific pattern of SRCR genes. Our results imply some shared immune functions and more generally, a shared regulatory architecture which underlies immune system gene expression in all deuterostomes. We conclude that the vertebrate immune system has evolved by inserting new genes into old gene regulatory networks dedicated to immunity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002510050551
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  • 2
    Electronic Resource
    Electronic Resource
    Molecular evolution of the Metazoan protein kinase C multigene family (1996)
    Springer
    Journal of molecular evolution 43 (1996), S. 374-383 
    Details
    ISSN: 1432-1432
    Keywords: Sponges ; Geodia cydonium ; Serine/threonine kinases ; Phylogeny ; Molecular systematics ; Molecular evolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Protein kinases C (PKCs) comprise closely related Ser/Thr kinases, ubiquitously present in animal tissues; they respond to second messengers, e.g., Ca2+ and/or diacylglycerol, to express their activities. Two PKCs have been sequenced fromGeodia cydonium, a member of the lowest multicellular animals, the sponges (Porifera). One spongeG. cydonium PKC, GCPKC1, belongs to the “novel” (Ca2+-independent) PKC (nPKC) subfamily while the second one, GCPKC2, has the hallmarks of the “conventional” (Ca2+-dependent) PKC (cPKC) subfamily. The alignment of the Ser/Thr catalytic kinase domains, of the predicted as sequences for these cDNAs with respective segments from previously reported sequences, revealed highest homology to PKCs from animals but also distant relationships to Ser/Thr kinases from protozoa, plants, and bacteria. However, a comparison of the complete structures of the sponge PKCs, which are-already-identical to those of nPKCs and cPKCs from higher metazoa, with the structures of protozoan, plant, and bacterial Ser/Thr kinases indicates that the metazoan PKCs have to be distinguished from the nonmetazoan enzymes. These data indicate that metazoan PKCs have a universal common ancestor which they share with the nonmetazoan Ser/Thr kinases with respect to the kinase domain, but they differ from them in overall structural composition.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02339011
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  • 3
    Electronic Resource
    Electronic Resource
    Molecular Evolution of the Metazoan Protein Kinase C Multigene Family (1996)
    Springer
    Journal of molecular evolution 43 (1996), S. 374-383 
    Details
    ISSN: 1432-1432
    Keywords: Key words: Sponges —Geodia cydonium— Serine/threonine kinases — Phylogeny — Molecular systematics — Molecular evolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. Protein kinases C (PKCs) comprise closely related Ser/Thr kinases, ubiquitously present in animal tissues; they respond to second messengers, e.g., Ca2+ and/or diacylglycerol, to express their activities. Two PKCs have been sequenced from Geodia cydonium, a member of the lowest multicellular animals, the sponges (Porifera). One sponge G. cydonium PKC, GCPKC1, belongs to the ``novel'' (Ca2+-independent) PKC (nPKC) subfamily while the second one, GCPKC2, has the hallmarks of the ``conventional'' (Ca2+-dependent) PKC (cPKC) subfamily. The alignment of the Ser/Thr catalytic kinase domains, of the predicted aa sequences for these cDNAs with respective segments from previously reported sequences, revealed highest homology to PKCs from animals but also distant relationships to Ser/Thr kinases from protozoa, plants, and bacteria. However, a comparison of the complete structures of the sponge PKCs, which are—already—identical to those of nPKCs and cPKCs from higher metazoa, with the structures of protozoan, plant, and bacterial Ser/Thr kinases indicates that the metazoan PKCs have to be distinguished from the nonmetazoan enzymes. These data indicate that metazoan PKCs have a universal common ancestor which they share with the nonmetazoan Ser/Thr kinases with respect to the kinase domain, but they differ from them in overall structural composition.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00006096
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Somatic diversification of variable lymphocyte receptors in the agnathan sea lamprey (2004)
    [s.l.] : Macmillian Magazines Ltd.
    Nature 430 (2004), S. 174-180 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Although jawless vertebrates are apparently capable of adaptive immune responses, they have not been found to possess the recombinatorial antigen receptors shared by all jawed vertebrates. Our search for the phylogenetic roots of adaptive immunity in the lamprey has instead identified a new type of ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature02740
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  • 5
    Electronic Resource
    Electronic Resource
    Molecular cloning and primary structure of a Rhesus (Rh)-like protein from the marine sponge Geodia cydonium (1997)
    Springer
    Immunogenetics 46 (1997), S. 493-498 
    Details
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  In humans, the 30 000 M r Rhesus (Rh) polypeptide D (RhD) is a dominant antigen (Ag) of the Rh blood group system. To date, an Rh-like protein has been found in chimpanzees, gorillas, gibbons, and rhesus monkeys. Related to the 30 000 M r Rh Ag protein are two polypeptides of 50 000 M r , the human 50 000 M r Rh Ag and the RhD-like protein from Caenorhabditis elegans. The function of all these proteins is not sufficiently known. Here we characterize a cDNA clone (GCRH) encoding a putative 57 000 M r polypeptide from the marine sponge Geodia cydonium, which shares sequence similarity both to the RhD Ag and the Rh50 glycoprotein. The sponge Rh-like protein comprises 523 aa residues; hydropathy analysis hints at the presence of ten transmembrane domains. An N-terminal hydrophobic cleavage signal sequence is missing, suggesting that the first membrane-spanning domain of the sponge Rh-like protein acts as a signal-anchor sequence. The sponge Rh-like protein, like the human Rh50, lacks the CLP motif which is characteristic of the 30 000 M r RhD. In addition, the hydropathy profile of the sponge Rh-like protein is of a similar size and shape as that of human Rh50. This data indicates that the RhD and its structurally related Rh50 glycoprotein, which are highly immunogenic in humans, share a common ancestral molecule with the G. cydonium Rh-like protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002510050310
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  • 6
    Electronic Resource
    Electronic Resource
    A tunicate (Botryllus schlosseri) cDNA reveals similarity to vertebrate antigen receptors (1996)
    Springer
    Immunogenetics 45 (1996), S. 69-72 
    Details
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002510050169
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