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Expression and localization of heat shock proteins in rat basophilic leukemia cells: differential modulation by degranulation, thermal or oxidative stress.

AbstractBACKGROUND:
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.
AuthorsM Bachelet, F Marchand, E Souil, D François, E Mariéthoz, A Weyer, B S Polla
JournalAllergy (Allergy) Vol. 57 Issue 9 Pg. 791-7 (Sep 2002) ISSN: 0105-4538 [Print] Denmark
PMID12169174 (Publication Type: Journal Article)
Chemical References
  • HSP70 Heat-Shock Proteins
  • Ionophores
  • Calcimycin
  • Heme Oxygenase (Decyclizing)
  • Heme Oxygenase-1
  • beta-N-Acetylhexosaminidases
Topics
  • Animals
  • Calcimycin (pharmacology)
  • Cell Degranulation
  • Cell Division
  • Flow Cytometry
  • HSP70 Heat-Shock Proteins (biosynthesis)
  • Heme Oxygenase (Decyclizing) (biosynthesis)
  • Heme Oxygenase-1
  • Hot Temperature
  • Hypersensitivity (metabolism)
  • Immunohistochemistry
  • Ionophores (pharmacology)
  • Leukemia, Basophilic, Acute (metabolism)
  • Oxidative Stress
  • Rats
  • Tobacco
  • Tumor Cells, Cultured
  • beta-N-Acetylhexosaminidases (metabolism)

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