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Evidence for a protective response by the gill proteome of rainbow trout exposed to X‐ray induced bystander signals
Author(s) -
Smith Richard W.,
Wang Jiaxi,
Bucking Carol P.,
Mothersill Carmel E.,
Seymour Colin B.
Publication year - 2007
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200700573
Subject(s) - bystander effect , gill , rainbow trout , microbiology and biotechnology , biology , lactate dehydrogenase , trout , intracellular , proteome , chemistry , biochemistry , immunology , enzyme , fishery , fish <actinopterygii>
The bystander effect occurs when cells which are not directly exposed to radiation, but which receive signals from irradiated cells, respond as though they were irradiated. An X‐ray induced bystander effect has been demonstrated in rainbow trout gills. Therefore, a proteomic comparison was made of gills from X‐ray treated trout and trout exposed to X‐ray induced bystander signals. 2‐D gel analysis revealed X‐ray exposure increased the expression of the cancer related protein annexin II. The proteomic changes associated with the bystander effect differed from those associated with direct radiation exposure. Expression of a hemopexin‐like protein, Rho GDP dissociation inhibitor (RhoGDI) and pyruvate dehydrogenase (PDH) were increased. These proteins possess protective properties against reactive oxygen damage (a component of the bystander signal), regulate epithelial polarity and prevent lactate acidosis, respectively. There was also evidence for an increase in chromosome 1 SR‐like CTD‐associated factor (SCAF) protein turnover, which could suggest the protective response is transcriptionally regulated. The freshwater fish gill is a polarised barrier, separating against an external hypotonic environment. Since the maintenance of epithelial polarity is vital to gill function, these bystander effect proteomic changes could collectively protect the structural, functional and intracellular integrity of gill epithelia.