title: Effect of ischemia--reperfusion on heat shock protein 70 and 90 gene expression in rat liver: relation to nutritional status.
abstract: Heat shock proteins are intracellular proteins associated with a generalized response of cells to stress. The purpose of this study was to assess RNA levels of heat shock protein 70 and 90 in fed or fasted rat livers during ischemia-reperfusion. Northern blot analysis of heat shock proteins was performed. Adenosine triphosphate and glutathione were assessed. In baseline conditions, livers of fasted rats showed a twofold increase in mRNA for both heat shock proteins and 38% and 43% reductions in adenosine triphosphate and glutathione, respectively, when compared with organs from fed rats. After ischemia, livers of fasted rats presented a twofold decrease in heat shock protein mRNA, while no changes were observed in livers of fed rats; reduced glutathione and adenosine triphosphate decreased 55% and 50% in fasted livers and 25% and 20% in fed organs, respectively. After 120 min of reperfusion, heat shock protein mRNA rose threefold in fasted livers, while a slight decrease was observed in the fed group; reduced glutathione and adenosine triphosphate returned to 65% and 70% of baseline values in fasted livers and 85% and 90% in fed organs, respectively. In conclusion, the nutritional status affects heat shock protein expression determined by reperfusion. The reduced antioxidant status leading to increased oxidative stress could be the mechanism underlying the phenomenon.
authors.affiliation: Internal Medicine Department, Catholic University of Rome, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Gasbarrini
authors.forename: S D
authors.initials: SD
authors.lastname: Esposti
authors.forename: C
authors.initials: C
authors.lastname: Di Campli
authors.forename: S
authors.initials: S
authors.lastname: De Notariis
authors.forename: S
authors.initials: S
authors.lastname: Loffredo
authors.forename: A
authors.initials: A
authors.lastname: Abraham
authors.forename: M
authors.initials: M
authors.lastname: Simoncini
authors.forename: R
authors.initials: R
authors.lastname: Pola
authors.forename: A
authors.initials: A
authors.lastname: Colantoni
authors.forename: F
authors.initials: F
authors.lastname: Trevisani
authors.forename: M
authors.initials: M
authors.lastname: Bernardi
authors.forename: G
authors.initials: G
authors.lastname: Gasbarrini
mesh_terms: D000255:Adenosine Triphosphate / Q000032:analysis; D000818:Animals; D015152:Blotting, Northern; D015870:Gene Expression; D005978:Glutathione / Q000032:analysis; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D008297:Male; D009752:Nutritional Status; D012333:RNA, Messenger / Q000032:analysis; D051381:Rats; D017207:Rats, Sprague-Dawley; D015427:Reperfusion Injury / Q000378:metabolism*
chemical_list: D018840:HSP70 Heat-Shock Proteins; D018841:HSP90 Heat-Shock Proteins; D012333:RNA, Messenger; D000255:Adenosine Triphosphate; D005978:Glutathione