Please use this identifier to cite or link to this item: http://www.repositorio.ufop.br/handle/123456789/4650
Title: The proteasome-ubiquitin pathway in the Schistosoma mansoni egg has development - and morphology - specific characteristics.
Authors: Mathieson, William
Borges, William de Castro
Wilson, R. Alan
Keywords: Hatch fluid
Miracidium
Vitelline cells
Vitellaria
Issue Date: 2011
Citation: MATHIESON, W.; BORGES, W. de C.; WILSON, R. A. The proteasome - ubiquitin pathway in the Schistosoma mansoni egg has development - and morphology - specific characteristics. Molecular and Biochemical Parasitology, v. 175, p. 118-125, 2011. Disponível em: <http://www.sciencedirect.com/science/article/pii/S0166685110002574>. Acesso em: 08 nov. 2014.
Abstract: Schistosoma mansoni eggs, consisting of an ovum surrounded by nutritive vitelline cells packaged in a tanned protein shell, are produced by paired worms residing in the mesenteric veins of the human host. The vitelline cells are degraded as the larval miracidium matures, the fully developed egg either crossing the gut wall to escape the host or becoming lodged in the host’s tissues where it dies and disintegrates, inducing a potentially pathological immune response. Thus, the egg is central to both the transmission of the parasite and the aetiology of the disease. Herewepresent the first study investigating protein turnover in the egg. We establish that the ubiquitin-proteasome pathway (UPP) changes with egg development and furthermore, that the morphological components of the fully developed egg (the miracidium and the subshell envelope) also exhibit different proteasome subunit expression profiles. We conclude that the UPP is responsible not only for degrading the vitelline cells but is also more highly developed in the envelope than in the miracidium. The envelope is involved in the defence of the miracidium and produces the proteins that the egg secretes, presumably to facilitate its escape from the host, so the UPP probably has a multi-faceted role in the egg’s biology.
URI: http://www.repositorio.ufop.br/handle/123456789/4650
metadata.dc.identifier.doi: https://doi.org/10.1016/j.molbiopara.2010.10.005
ISSN: 0166-6851
metadata.dc.rights.license: O periódico Molecular and Biochemical Parasitology concede permissão para depósito deste artigo no Repositório Institucional da UFOP. Número da licença: 3550930750265.
Appears in Collections:DECBI - Artigos publicados em periódicos

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