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Updated: Aug 14, 2026
Prevention of Heat Stress Adverse Effects in Rats by Bacillus subtilis Strain
Published on: July 11, 2016
Expression and localization of heat shock proteins in rat basophilic leukemia cells: differential modulation by
M Bachelet1, F Marchand, E Souil
1Laboratoire de Physiologie Respiratoire et de Biologie Cellulair, UFR Cochin Port-Royal, 24, rue de Faubourg Saint-Jacques, 75014 Paris, France.
Background:
Rat basophilic leukemia (RBL-2H3) cells are well characterized in terms of morphological and biochemical changes upon activation, and have been extensively used as a model system for studying the mechanisms of the immediate hypersensitivity reaction. To investigate whether overexpression of heat shock/stress proteins (HSP) is involved in the mast cell-dependent reactivity, we examined the adaptive responses of RBL-2H3 cells to classical stress conditions such as heat shock or oxidative injury produced by an aqueous extract of tobacco smoke.
Methods:
HSP were determined by flow cytometry and immunocytochemistry. Degranulation was confirmed as the release of beta-hexosaminidase, determined spectrophotometrically, and by electron microscopy experiments.
Results:
We found that RBL-2H3 cells respond to heat shock or oxidative injury by the synthesis of both the inducible 72 kDa HSP (Hsp70), and the oxidation-specific 32 kDa heme oxygenase (HO)-1. Heat shock induced mainly Hsp70 in a cell growth-dependent manner, whereas oxidative stress induced mainly HO-1 in a cell growth-independent manner. However, heat shock or oxidative stress had no significant effects on degranulation.
Conclusion:
Stress-mediated synthesis of HSP was not associated with RBL-2H3 degranulation and likewise, degranulation did not induce HSP.
