Pitfalls in invertebrate proteasome assays

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2013
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Götze, Sandra
Abele, Doris
Sokolova, Inna M.
Saborowski, Reinhard
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The ubiquitin-proteasome system controls a variety of essential intracellular processes through directed protein turnover. The invertebrate proteasome has recently gained increasing interest with respect to central physiological processes and pathways in different taxa. A pitfall in proteasome activity assays, represented by the trypsin-like, chymotrypsin-like or caspase-like site, lies in the fact that most commonly used experimental substrates are susceptible to degradation by non-proteasomal proteolytic enzymes, which can lead to erroneous interpretation of activity data obtained. Through the use of a proteasome-specific inhibitor, epoxomicin, we showed that the shares of proteasomal and non-proteasomal activities in the degradation of a model polypeptide substrate for chymotrypsin-like activity vary considerably between invertebrate taxa. Crustacean muscle tissue and hemocytes showed almost exclusively proteasomal activity. In yeast, approximately 90% of total proteolytic activity can be attributed to the proteasome. In contrast, proteasomal activity comprises only 20-60% of the total proteolytic activity in bivalve tissues. These results reveal that, without verification of the shares of proteasomal and non-proteasomal activities in crude extracts through the use of highly specific inhibitors, common proteasomal enzyme assays should be used and interpreted with caution.

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ISO 690GÖTZE, Sandra, Aneesh P. H. BOSE, Doris ABELE, Inna M. SOKOLOVA, Reinhard SABOROWSKI, 2013. Pitfalls in invertebrate proteasome assays. In: The Journal of Experimental Biology. Company of Biologists. 2013, 216(8), pp. 1351-1354. ISSN 0022-0949. eISSN 1477-9145. Available under: doi: 10.1242/jeb.082792
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@article{Gotze2013-04-15Pitfa-50116,
  year={2013},
  doi={10.1242/jeb.082792},
  title={Pitfalls in invertebrate proteasome assays},
  number={8},
  volume={216},
  issn={0022-0949},
  journal={The Journal of Experimental Biology},
  pages={1351--1354},
  author={Götze, Sandra and Bose, Aneesh P. H. and Abele, Doris and Sokolova, Inna M. and Saborowski, Reinhard}
}
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