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dc.contributor.authorHosp, Juliaeng
dc.contributor.authorSagane, Yoshimasaeng
dc.contributor.authorDanks, Gemmaeng
dc.contributor.authorThompson, Eric M.eng
dc.date.accessioned2013-04-08T13:46:55Z
dc.date.available2013-04-08T13:46:55Z
dc.date.issued2012-07-05eng
dc.PublishedPLoS ONE 7(7): e40172eng
dc.identifier.issn1932-6203en_US
dc.identifier.urihttp://hdl.handle.net/1956/6491
dc.description.abstractExtracellular matrices regulate biological processes at the level of cells, tissues, and in some cases, entire multicellular organisms. The subphylum Urochordata exemplifies the latter case, where animals are partially or completely enclosed in “houses” or “tunics”. Despite this common strategy, we show that the house proteome of the appendicularian, Oikopleura, has very little in common with the proteome of the sister class, ascidian, Ciona. Of 80 identified house proteins (oikosins), ~half lack domain modules or similarity to known proteins, suggesting de novo appearance in appendicularians. Gene duplication has been important in generating almost 1/3 of the current oikosin complement, with serial duplications up to 8 paralogs in one family. Expression pattern analyses revealed that individual oikosins are produced from specific fields of cells within the secretory epithelium, but in some cases, migrate up to at least 20 cell diameters in extracellular space to combine in defined house structures. Interestingly, peroxidasin and secretory phospholipase A2 domains, implicated in innate immune defence are secreted from the anlage associated with the food-concentrating filter, suggesting that this extra-organismal structure may play, in part, such a role in Oikopleura. We also show that sulfation of proteoglycans is required for the hydration and inflation of pre-house rudiments into functional houses. Though correct proportioning in the production of oikosins would seem important in repetitive assembly of the complex house structure, the genomic organization of oikosin loci appears incompatible with common enhancers or locus control regions exerting such a coordinate regulatory role. Thus, though all tunicates employ extracellular matrices based on a cellulose scaffold as a defining feature of the subphylum, they have evolved radically different protein compositions associated with this common underlying structural theme.en_US
dc.language.isoengeng
dc.publisherPublic Library of Scienceen_US
dc.rightsAttribution CC BYeng
dc.rights.urihttp://creativecommons.org/licenses/by/2.5/eng
dc.titleThe Evolving Proteome of a Complex Extracellular Matrix, the Oikopleura Houseen_US
dc.typePeer reviewed
dc.typeJournal article
dc.description.versionpublishedVersion
dc.rights.holderCopyright 2012 Hosp et al.en_US
dc.identifier.doihttps://doi.org/10.1371/journal.pone.0040172
dc.identifier.cristin966373


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