the evolving proteome of a complex extracellular matrix, the oikopleura house进化的一个复杂的细胞外基质蛋白质组,oikopleura房子.pdfVIP

the evolving proteome of a complex extracellular matrix, the oikopleura house进化的一个复杂的细胞外基质蛋白质组,oikopleura房子.pdf

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the evolving proteome of a complex extracellular matrix, the oikopleura house进化的一个复杂的细胞外基质蛋白质组,oikopleura房子

The Evolving Proteome of a Complex Extracellular Matrix, the Oikopleura House 1 1 1,2 1,3 Julia Hosp , Yoshimasa Sagane , Gemma Danks , Eric M. Thompson * 1 Sars International Centre for Marine Molecular Biology, University of Bergen, Bergen, Norway, 2 Computational Biology Unit, University of Bergen, Bergen, Norway, 3 Department of Biology, University of Bergen, Bergen, Norway Abstract Extracellular 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

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