PMC:4502368 / 32543-34002 JSONTXT

{"project":"2_test","denotations":[{"id":"25911227-7923371-43383327","span":{"begin":337,"end":341},"obj":"7923371"},{"id":"25911227-9857172-43383328","span":{"begin":355,"end":359},"obj":"9857172"},{"id":"25911227-10329681-43383329","span":{"begin":813,"end":817},"obj":"10329681"},{"id":"25911227-10438909-43383330","span":{"begin":836,"end":840},"obj":"10438909"},{"id":"25911227-17580304-43383331","span":{"begin":1117,"end":1121},"obj":"17580304"},{"id":"25911227-18434552-43383332","span":{"begin":1138,"end":1142},"obj":"18434552"},{"id":"25911227-21923101-43383333","span":{"begin":1158,"end":1162},"obj":"21923101"},{"id":"25911227-21722280-43383334","span":{"begin":1182,"end":1186},"obj":"21722280"},{"id":"25911227-23477725-43383335","span":{"begin":1199,"end":1203},"obj":"23477725"}],"text":"The ubiquitin/proteasome pathway is the other major destination for unfolded or damaged proteins that are not salvaged through chaperone stabilization or refolding. Proteins are marked for removal by the covalent attachment of multiple ubiquitin molecules and are subsequently degraded by the 26S proteasome or the lysosome (Ciechanover 1994; Ciechanover 1998). Multiple genes involved in the attachment of ubiquitin to target proteins were upregulated in juvenile Chinook salmon at 25°, including the ubiquitin ligases RNF19B and RNF8 and the ubiquitin conjugating enzyme UBE2B, which attach ubiquitin molecules to target proteins. RNF19B and the ubiquitin carrying protein type E2 are both associated with inflammatory and immune activation by cytotoxic t-cells or the NF-κB pathway, respectively (Gonen et al. 1999; Kozlowski et al. 1999). Genes (SQSMT1, ZFAND5, PTPN23) associated with the formation of polyubiquitinated bodies and the endosomal sorting machinery that processes targeted proteins for lysosomal degradation were also upregulated in individuals exposed to the 21° and 25° treatments (Pankiv et al. 2007; Doyotte et al. 2008; Garner et al. 2011; Shields and Piper 2011; Ali et al. 2013). The ubiquitin/proteosome pathway is likely strongly active in the experimental fish, especially in the higher temperature groups, indicating that the need for disposal of denatured proteins begins very early in the thermal stress response in these fish."}