title: Leptin is the modulator of HSP60 gene expression in AR42J cells.
abstract: Leptin, circulating protein involved in the control of body weight and energy expenditure received attention as a modulator of immune response of the organism. Leptin receptors have been detected in the pancreas and experimental studies have shown that leptin protects the pancreas against the damage induced by caerulein overstimulation. Heat shock proteins (HSP) are endogenous proteins produced by various cells exposed to high temperature or to the noxious agents. HSP protect the cells against various environmental and endogenous stressors. The implication of HSP60 in the leptin-induced pancreatic protection has not been examined yet. The aim of this study was: to investigate the changes of HSP60 mRNA signal in the pancreatic AR42J cells subjected to caerulein and leptin. AR42J cells were incubated in standart medium at 37 degrees C for: 0, 1, 3, 5, 12 or 24 h, under basal conditions. Incubation time of 3 h was selected for the next experiments. AR42J cells were incubated in presence of caerulein (10(-11), 10(-9) or 10(-7) M), leptin (10(-8) or 10(-6) M), or combination of above. Gene expression for HSP60 was determined by RT-PCR. The mRNA signal for HSP60 has been observed in AR42J pancreatic cells under basal conditions. Incubation of AR42J cells in presence of leptin (10(-8) or 10(-6) M) resulted in the significant increase of gene expression for HSP60 in both groups of AR42J cells. Caerulein stimulation reduced mRNA signal for HSP60. The strongest mRNA signal for HSP60 has been observed after the exposition of AR42J cells to combination of leptin and caerulein. We conclude that: 1. Gene expression for HSP60 has been detected in pancreatic AR42J cells under basal conditions. 2. HSP60 gene expression was significantly increased in pancreatic AR42J cells stimulated by leptin whereas caerulein reduced this signal. 3. The strongest gene expression for HSP60 has been detected in the cells incubated with combination of caerulein and leptin.
authors.affiliation: Department of Medical Physiology, Health Care Faculty, Jagiellonian University Medical College, Cracow, Poland. jabonior@gazeta.pl
authors.forename: J
authors.initials: J
authors.lastname: Bonior
authors.forename: J
authors.initials: J
authors.lastname: Jaworek
authors.forename: S J
authors.initials: SJ
authors.lastname: Konturek
authors.forename: W W
authors.initials: WW
authors.lastname: Pawlik
mesh_terms: D000199:Actins / Q000378:metabolism; D000818:Animals; D002460:Cell Line; D002108:Ceruletide / Q000494:pharmacology; D018834:Chaperonin 60 / Q000096:biosynthesis / Q000235:genetics*; D004305:Dose-Response Relationship, Drug; D015870:Gene Expression / Q000187:drug effects; D020738:Leptin / Q000494:pharmacology*; D010179:Pancreas / Q000187:drug effects / Q000378:metabolism / Q000502:physiology; D012333:RNA, Messenger / Q000096:biosynthesis / Q000235:genetics; D051381:Rats
chemical_list: D000199:Actins; D018834:Chaperonin 60; D020738:Leptin; D012333:RNA, Messenger; D002108:Ceruletide