Insulin modulates rat liver glucocorticoid receptor
Апстракт
This investigation used cytosol fraction of rat liver to examine the effects of insulin ( INS) on functional properties of glucocorticoid receptor ( GR). Male Wistar rats ( 220 - 250 g b.wt.) were injected with INS ( 50 mu g/200 g b.wt, i.p.) and 18 h after INS administration used for experiments. INS-stimulated dissociation of G-R complexes was significantly increased by 133% compared to control level. However, INS treatment significantly stimulated stability of GR protein by 138% above control value. Furthermore, results show that INS stimulated activation of formed cytosol [ H-3] TA-R complexes by 143% in respect to control. [ H-3] TA-R complexes from INS treated animals could be activated and accumulated at higher rate in cell nuclei of control animals. The physiological relevance of the data was confirmed by INS-related stimulation of Tryptophan oxigenase ( TO) activity. It was observed that INS stimulated TO activity while INS injected to adrenalectomized rats, exhibited less eff...ects compared to control. The results indicate that a glucocorticoid hormone ( CORT) enhances INS induced stimulation of TO activity, as evidenced by enhanced enzyme activity. Presented data suggest: that INS treatment leads to modifications of the GR protein and the nuclear components and that INS activates the rat liver CORT signaling pathway which mediates, in part, the activity of TO.
Кључне речи:
glucocorticoid receptor / activation of receptor / hormon-receptor complex / insulin / tryptophan oxigenaseИзвор:
Acta Biologica Hungarica, 2006, 57, 1, 37-48
DOI: 10.1556/ABiol.57.2006.1.4
ISSN: 0236-5383
PubMed: 16646523
WoS: 000235657200004
Scopus: 2-s2.0-33746005268
Колекције
Институција/група
VinčaTY - JOUR AU - Isenović, Esma R. AU - Žakula, Zorica AU - Korićanac, Goran AU - Ribarac-Stepić, Nevena B. PY - 2006 UR - https://vinar.vin.bg.ac.rs/handle/123456789/2982 AB - This investigation used cytosol fraction of rat liver to examine the effects of insulin ( INS) on functional properties of glucocorticoid receptor ( GR). Male Wistar rats ( 220 - 250 g b.wt.) were injected with INS ( 50 mu g/200 g b.wt, i.p.) and 18 h after INS administration used for experiments. INS-stimulated dissociation of G-R complexes was significantly increased by 133% compared to control level. However, INS treatment significantly stimulated stability of GR protein by 138% above control value. Furthermore, results show that INS stimulated activation of formed cytosol [ H-3] TA-R complexes by 143% in respect to control. [ H-3] TA-R complexes from INS treated animals could be activated and accumulated at higher rate in cell nuclei of control animals. The physiological relevance of the data was confirmed by INS-related stimulation of Tryptophan oxigenase ( TO) activity. It was observed that INS stimulated TO activity while INS injected to adrenalectomized rats, exhibited less effects compared to control. The results indicate that a glucocorticoid hormone ( CORT) enhances INS induced stimulation of TO activity, as evidenced by enhanced enzyme activity. Presented data suggest: that INS treatment leads to modifications of the GR protein and the nuclear components and that INS activates the rat liver CORT signaling pathway which mediates, in part, the activity of TO. T2 - Acta Biologica Hungarica T1 - Insulin modulates rat liver glucocorticoid receptor VL - 57 IS - 1 SP - 37 EP - 48 DO - 10.1556/ABiol.57.2006.1.4 ER -
@article{ author = "Isenović, Esma R. and Žakula, Zorica and Korićanac, Goran and Ribarac-Stepić, Nevena B.", year = "2006", abstract = "This investigation used cytosol fraction of rat liver to examine the effects of insulin ( INS) on functional properties of glucocorticoid receptor ( GR). Male Wistar rats ( 220 - 250 g b.wt.) were injected with INS ( 50 mu g/200 g b.wt, i.p.) and 18 h after INS administration used for experiments. INS-stimulated dissociation of G-R complexes was significantly increased by 133% compared to control level. However, INS treatment significantly stimulated stability of GR protein by 138% above control value. Furthermore, results show that INS stimulated activation of formed cytosol [ H-3] TA-R complexes by 143% in respect to control. [ H-3] TA-R complexes from INS treated animals could be activated and accumulated at higher rate in cell nuclei of control animals. The physiological relevance of the data was confirmed by INS-related stimulation of Tryptophan oxigenase ( TO) activity. It was observed that INS stimulated TO activity while INS injected to adrenalectomized rats, exhibited less effects compared to control. The results indicate that a glucocorticoid hormone ( CORT) enhances INS induced stimulation of TO activity, as evidenced by enhanced enzyme activity. Presented data suggest: that INS treatment leads to modifications of the GR protein and the nuclear components and that INS activates the rat liver CORT signaling pathway which mediates, in part, the activity of TO.", journal = "Acta Biologica Hungarica", title = "Insulin modulates rat liver glucocorticoid receptor", volume = "57", number = "1", pages = "37-48", doi = "10.1556/ABiol.57.2006.1.4" }
Isenović, E. R., Žakula, Z., Korićanac, G.,& Ribarac-Stepić, N. B.. (2006). Insulin modulates rat liver glucocorticoid receptor. in Acta Biologica Hungarica, 57(1), 37-48. https://doi.org/10.1556/ABiol.57.2006.1.4
Isenović ER, Žakula Z, Korićanac G, Ribarac-Stepić NB. Insulin modulates rat liver glucocorticoid receptor. in Acta Biologica Hungarica. 2006;57(1):37-48. doi:10.1556/ABiol.57.2006.1.4 .
Isenović, Esma R., Žakula, Zorica, Korićanac, Goran, Ribarac-Stepić, Nevena B., "Insulin modulates rat liver glucocorticoid receptor" in Acta Biologica Hungarica, 57, no. 1 (2006):37-48, https://doi.org/10.1556/ABiol.57.2006.1.4 . .