Abstract.
The anti-heat shock protein (Hsp)-90 monoclonal antibody AC-16 reacts on blots with Hsp90 and a 50 kDa protein (prot-50) from infective-stage (L1) larvae of the nematode Trichinella spiralis. We examined Hsp90 and prot-50 levels by densitometric analysis of immunoblots of T. spiralis larval extracts prepared before (time 0, 37°C) and after oxidative [hydrogen peroxide (H2O2)] stress, or cold shock at 4°C. Extracts from H2O2-exposed L1 were obtained after 2 h; the others at 2, 4, and 8 h after the temperature shift. After H2O2 shock, the constitutive Hsp90 and prot-50 were both significantly induced and appeared as slower migrating inducible isoforms. However, whereas Hsp90 levels decreased after cold shock, prot-50 levels immediately and persistently increased after shock at 4°C. These data present compelling evidence that the prot-50 described here functions as a Hsp and a cold shock protein.
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Martinez, .J., Perez-Serrano, .J., Bernadina, .W. et al. Oxidative and cold shock cause enhanced induction of a 50 kDa stress protein in Trichinella spiralis . Parasitol Res 88, 427–430 (2002). https://doi.org/10.1007/s00436-002-0608-5
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DOI: https://doi.org/10.1007/s00436-002-0608-5