title: A subset of histamine receptor ligands improve thermotolerance of the yeast Saccharomyces cerevisiae.
abstract: OBJECTIVE
  Histamine interacts with the stress response in eukaryotes. This study investigated the effects of antihistamines on the heat shock (HS) response in yeast, thereby exploring their functions in a well-established histamine receptor (H(x) R)-free model.
  
  
  RESULTS
  Stress response was evaluated by determining growth and viability of postlogarithmic phase grown yeast cultures after HS at 53°C for 30 min. The effects of H(x) R ligands were investigated following short- and long-term administration. The H(1) R antagonist dimethindene exerted dose-related antifungal actions, whereas the H(2) R antagonist ranitidine failed to elicit any effect. In contrast, the H(3/4) R and H(4) R ligands, thioperamide and JNJ7777120, respectively, induced the thermotolerant phenotype. The circumvention of thermotolerance by cycloheximide and the induction of Hsp70 and Hsp104 expression indicated the contribution of de novo protein synthesis in the adaptive process, likely directed towards alterations in Hsp expression.
  
  
  CONCLUSIONS
  The data provide evidence for the differential function of H(x) R ligands in thermotolerance induction in yeast.
  
  
  CONCLUSIONS
  First demonstration of the action of antihistamines in the HS response in yeast. The work supports the potential H(x) R-independent functions of histaminergic compounds in fungal adaptation and stimulates research on the prospect of their exploitation in eukaryotic (patho)physiology.
authors.affiliation: Department of Pharmacology, Medical School, University of Athens, Athens, Greece.
authors.forename: K
authors.initials: K
authors.lastname: Papamichael
authors.forename: B
authors.initials: B
authors.lastname: Delitheos
authors.forename: E
authors.initials: E
authors.lastname: Tiligada
mesh_terms: D000222:Adaptation, Physiological / Q000187:drug effects / Q000235:genetics; D003513:Cycloheximide / Q000494:pharmacology; D018840:HSP70 Heat-Shock Proteins / Q000096:biosynthesis; D006360:Heat-Shock Proteins / Q000096:biosynthesis; D018869:Heat-Shock Response / Q000187:drug effects / Q000235:genetics; D006633:Histamine Antagonists / Q000494:pharmacology*; D007211:Indoles / Q000494:pharmacology; D008024:Ligands; D050296:Microbial Viability; D010879:Piperazines / Q000494:pharmacology; D014176:Protein Biosynthesis / Q000187:drug effects; D012441:Saccharomyces cerevisiae / Q000187:drug effects* / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000096:biosynthesis
chemical_list: D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D006633:Histamine Antagonists; D007211:Indoles; D008024:Ligands; D010879:Piperazines; D029701:Saccharomyces cerevisiae Proteins; C070972:HsP104 protein, S cerevisiae; C484309:1-((5-chloro-1H-indol-2-yl)carbonyl)-4-methylpiperazine; D003513:Cycloheximide