Related Experiment Video
Updated: Aug 1, 2026

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
Published on: January 8, 2015
An influence of stress protein CSP 310 and antiserum against this protein on lipid peroxidation in cereal
A V Kolesnichenko1, O I Grabelnych, V V Tourchaninova
1Siberian Institute of Plant Physiology and Biochemistry, Siberian Division of Russian Academy of Sciences, Irkutsk.
Abstract:
It is determined that an addition of an anti-CSP 310 antiserum to isolated winter wheat and maize mitochondria caused more significant increasing of spontaneous lipid peroxidation than the addition of stress protein CSP 310. It is shown that, at function of different mitochondrial respiratory chain complexes, the lipid peroxidation in winter wheat and maize mitochondria take place with different intensities. Under the functioning of mitochondrial respiratory chain complex IV, the maximum output of lipid peroxidation products, dienic conjugates is detected. The presence of antiserum against CSP 310 in incubation media induces lipid peroxidation more than the presence of CSP 310 in mitochondria isolated from stressed plants under these conditions. Based on data obtained, it is possible to conclude that in vivo endogenous CSP 310, during a cold stress, has an antioxidant activity the same as other known uncoupling proteins.
Related Concept Videos
Responses to Heat and Cold Stress
The Unfolded Protein Response
Regulation of the Unfolded Protein Response

