| 1. |
- Cerenius, Lage, et al.
(författare)
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Proteolytic cascades and their involvement in invertebrate immunity
- 2010
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Ingår i: TIBS -Trends in Biochemical Sciences. Regular ed.. - : Elsevier BV. - 0968-0004 .- 1362-4326. ; 35:10, s. 575-583
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Forskningsöversikt (refereegranskat)abstract
- Bacteria and other potential pathogens are cleared rapidly from the body fluids of invertebrates by the immediate response of the innate immune system. Proteolytic cascades, following their initiation by pattern recognition proteins, control several such reactions, notably coagulation, melanisation, activation of the Toll receptor and complement-like reactions. However, there is considerable variation among invertebrates and these cascades, although widespread, are not present in all phyla. In recent years, significant progress has been made in identifying and characterizing these cascades in insects. Notably, recent work has identified several connections and shared principles among the different pathways, suggesting that cross-talk between them may be common.
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| 2. |
- Hara, Yuko, et al.
(författare)
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Expression patterns of Hox genes in larvae of the sea lily Metacrinus rotundus
- 2006
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Ingår i: Development Genes and Evolution. ; 216, s. 797-809
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Tidskriftsartikel (refereegranskat)abstract
- We cloned eight Hox genes (MrHox1, MrHox2, MrHox4, MrHox5, MrHox7, MrHox8, MrHox9/10, and MrHox11/13c) from the sea lily Metacrinus rotundus, a member of the most basal group of the extant echinoderms. At the auricularia stage, before the formation of the pentaradial rudiment, four MrHox genes were expressed sequentially along the anteroposterior (AP) axis in the straightened mesodermal somatocoels in the order MrHox5, MrHox7, MrHox8, and MrHox9/10. The expression of MrHox7 and MrHox8 was detected as early as the hatching stage in the presumptive somatocoel region of the archenteral sac. MrHox5 was expressed in the anteriormost region of the somatocoels, where a stalk-related structure (the chambered organ) forms later. In addition to the mesodermal somatocoels, MrHox7 was expressed in the oral hood ectoderm, which gives rise to the adhesive pit. The expression of four other MrHox genes (MrHox1, MrHox2, MrHox4, and MrHox11/13c) was not detected in any of the larval stages we examined. In comparison with the mesodermal sea urchin Hox genes, the MrHox genes are expressed more posteriorly along the AP (oral–anal) axis than the sea urchin orthologs, implying that the evolution of the eleutherozoans was accompanied by a posteriorization of the larval body. Our study illuminates the possible body plan and Hox expression patterns of the ancestral echinoderm and sheds light on the larval body plan of the last common ancestor of the echinoderms and chordates.
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| 3. |
- Holland, Linda Z, et al.
(författare)
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The amphioxus genome illuminates vertebrate origins and cephalochordate biology
- 2008
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Ingår i: Genome Research. - : Cold Spring Harbor Laboratory. - 1088-9051 .- 1549-5469. ; 18:7, s. 1100-1111
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Tidskriftsartikel (refereegranskat)abstract
- Cephalochordates, urochordates, and vertebrates evolved from a common ancestor over 520 million years ago. To improve our understanding of chordate evolution and the origin of vertebrates, we intensively searched for particular genes, gene families, and conserved noncoding elements in the sequenced genome of the cephalochordate Branchiostoma floridae, commonly called amphioxus or lancelets. Special attention was given to homeobox genes, opsin genes, genes involved in neural crest development, nuclear receptor genes, genes encoding components of the endocrine and immune systems, and conserved cis-regulatory enhancers. The amphioxus genome contains a basic set of chordate genes involved in development and cell signaling, including a fifteenth Hox gene. This set includes many genes that were co-opted in vertebrates for new roles in neural crest development and adaptive immunity. However, where amphioxus has a single gene, vertebrates often have two, three, or four paralogs derived from two whole-genome duplication events. In addition, several transcriptional enhancers are conserved between amphioxus and vertebrates--a very wide phylogenetic distance. In contrast, urochordate genomes have lost many genes, including a diversity of homeobox families and genes involved in steroid hormone function. The amphioxus genome also exhibits derived features, including duplications of opsins and genes proposed to function in innate immunity and endocrine systems. Our results indicate that the amphioxus genome is elemental to an understanding of the biology and evolution of nonchordate deuterostomes, invertebrate chordates, and vertebrates.
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| 4. |
- Kim, Chan-Hee, et al.
(författare)
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A three-step proteolytic cascade mediates the activation of the peptidoglycan-induced toll pathway in an insect
- 2008
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Ingår i: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 283:12, s. 7599-7607
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Tidskriftsartikel (refereegranskat)abstract
- The recognition of lysine-type peptidoglycans (PG) by the PG recognition complex has been suggested to cause activation of the serine protease cascade leading to the processing of Spätzle and subsequent activation of the Toll signaling pathway. So far, two serine proteases involved in the lysine-type PG Toll signaling pathway have been identified. One is a modular serine protease functioning as an initial enzyme to be recruited into the lysine-type PG recognition complex. The other is the Drosophila Spätzle processing enzyme (SPE), a terminal enzyme that converts Spätzle pro-protein to its processed form capable of binding to the Toll receptor. However, it remains unclear how the initial PG recognition signal is transferred to Spätzle resulting in Toll pathway activation. Also, the biochemical characteristics and mechanism of action of a serine protease linking the modular serine protease and SPE have not been investigated. Here, we purified and cloned a novel upstream serine protease of SPE that we named SAE, SPE-activating enzyme, from the hemolymph of a large beetle, Tenebrio molitor larvae. This enzyme was activated by Tenebrio modular serine protease and in turn activated the Tenebrio SPE. The biochemical ordered functions of these three serine proteases were determined in vitro, suggesting that the activation of a three-step proteolytic cascade is necessary and sufficient for lysine-type PG recognition signaling. The processed Spätzle by this cascade induced antibacterial activity in vivo. These results demonstrate that the three-step proteolytic cascade linking the PG recognition complex and Spätzle processing is essential for the PG-dependent Toll signaling pathway.
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