Impact of estradiol on insulin signaling in the rat heart
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2009
Authors
Koricanac, G.Milosavljević, T.
Stojiljković, Mojca
Zakula, Z.
Tepavcević, S.
Ribarac-Stepić, N.
Isenović, E.R.
Article (Published version)
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It is well known that variation in the concentration of estrogens affects insulin action. In this study we examine the impact of estradiol (E2) on insulin signaling in the rat heart. Ovariectomized female rats were treated with E2 6 h prior to analysis of basal protein and mRNA content of insulin signaling molecules, and additionally with insulin 30 min before the experiment to delineate E2 effects on phosphorylations and molecular associations relevant for insulin signaling. The results show that E2 decreased insulin receptor (IR) tyrosine phosphorylation, while it did not alter IR protein and mRNA content. E2 administration did not change IR substrate 1 (IRS-1) protein content and tyrosine phosphorylation, while decreased mRNA content and increased its association with the p85 subunit of phosphatidylinositol 3-kinase (PI3K). E2 decreased protein and mRNA content of IR substrate 2 (IRS-2), while did not change IRS-2 tyrosine phosphorylation and IRS-2 association with p85. The increase... of IRS-1/p85 is accompanied by increase of p85 protein and mRNA levels, and by stimulation of protein kinase B (Akt) Ser473 phosphorylation. In contrast, Akt protein and mRNA content were not changed. In summary, although in some aspects cardiac insulin signaling is obviously improved by E2 treatment (increase of p85 mRNA and protein levels, enhancement of IRS-1/p85 association and Ser473 Akt phosphorylation), the observed decrease of IR tyrosine phosphorylation, IRS-2 protein content, and IRSs mRNA contents, suggest very complex interplay of beneficial and suppressive effects of E2, both genomic and non-genomic, in regulation of heart insulin signaling. Copyright
Keywords:
PI3 kinase / Insulin signaling / Insulin receptor / Heart / Akt / 17-estradiolSource:
Cell Biochemistry and Function, 2009, 27, 2, 102-110Funding / projects:
- Molekularni mehanizmi transdukcije hormonskih signala: Biološki markeri modifikacije i integracije signalnih puteva u fiziološkim i patofiziološkim stanjima (RS-MESTD-MPN2006-2010-143030)
DOI: 10.1002/cbf.1542
ISSN: 0263-6484
PubMed: 19226537
WoS: 000264118100007
Scopus: 2-s2.0-63149148931
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Institut za molekularnu genetiku i genetičko inženjerstvoTY - JOUR AU - Koricanac, G. AU - Milosavljević, T. AU - Stojiljković, Mojca AU - Zakula, Z. AU - Tepavcević, S. AU - Ribarac-Stepić, N. AU - Isenović, E.R. PY - 2009 UR - https://imagine.imgge.bg.ac.rs/handle/123456789/376 AB - It is well known that variation in the concentration of estrogens affects insulin action. In this study we examine the impact of estradiol (E2) on insulin signaling in the rat heart. Ovariectomized female rats were treated with E2 6 h prior to analysis of basal protein and mRNA content of insulin signaling molecules, and additionally with insulin 30 min before the experiment to delineate E2 effects on phosphorylations and molecular associations relevant for insulin signaling. The results show that E2 decreased insulin receptor (IR) tyrosine phosphorylation, while it did not alter IR protein and mRNA content. E2 administration did not change IR substrate 1 (IRS-1) protein content and tyrosine phosphorylation, while decreased mRNA content and increased its association with the p85 subunit of phosphatidylinositol 3-kinase (PI3K). E2 decreased protein and mRNA content of IR substrate 2 (IRS-2), while did not change IRS-2 tyrosine phosphorylation and IRS-2 association with p85. The increase of IRS-1/p85 is accompanied by increase of p85 protein and mRNA levels, and by stimulation of protein kinase B (Akt) Ser473 phosphorylation. In contrast, Akt protein and mRNA content were not changed. In summary, although in some aspects cardiac insulin signaling is obviously improved by E2 treatment (increase of p85 mRNA and protein levels, enhancement of IRS-1/p85 association and Ser473 Akt phosphorylation), the observed decrease of IR tyrosine phosphorylation, IRS-2 protein content, and IRSs mRNA contents, suggest very complex interplay of beneficial and suppressive effects of E2, both genomic and non-genomic, in regulation of heart insulin signaling. Copyright T2 - Cell Biochemistry and Function T1 - Impact of estradiol on insulin signaling in the rat heart EP - 110 IS - 2 SP - 102 VL - 27 DO - 10.1002/cbf.1542 ER -
@article{ author = "Koricanac, G. and Milosavljević, T. and Stojiljković, Mojca and Zakula, Z. and Tepavcević, S. and Ribarac-Stepić, N. and Isenović, E.R.", year = "2009", abstract = "It is well known that variation in the concentration of estrogens affects insulin action. In this study we examine the impact of estradiol (E2) on insulin signaling in the rat heart. Ovariectomized female rats were treated with E2 6 h prior to analysis of basal protein and mRNA content of insulin signaling molecules, and additionally with insulin 30 min before the experiment to delineate E2 effects on phosphorylations and molecular associations relevant for insulin signaling. The results show that E2 decreased insulin receptor (IR) tyrosine phosphorylation, while it did not alter IR protein and mRNA content. E2 administration did not change IR substrate 1 (IRS-1) protein content and tyrosine phosphorylation, while decreased mRNA content and increased its association with the p85 subunit of phosphatidylinositol 3-kinase (PI3K). E2 decreased protein and mRNA content of IR substrate 2 (IRS-2), while did not change IRS-2 tyrosine phosphorylation and IRS-2 association with p85. The increase of IRS-1/p85 is accompanied by increase of p85 protein and mRNA levels, and by stimulation of protein kinase B (Akt) Ser473 phosphorylation. In contrast, Akt protein and mRNA content were not changed. In summary, although in some aspects cardiac insulin signaling is obviously improved by E2 treatment (increase of p85 mRNA and protein levels, enhancement of IRS-1/p85 association and Ser473 Akt phosphorylation), the observed decrease of IR tyrosine phosphorylation, IRS-2 protein content, and IRSs mRNA contents, suggest very complex interplay of beneficial and suppressive effects of E2, both genomic and non-genomic, in regulation of heart insulin signaling. Copyright", journal = "Cell Biochemistry and Function", title = "Impact of estradiol on insulin signaling in the rat heart", pages = "110-102", number = "2", volume = "27", doi = "10.1002/cbf.1542" }
Koricanac, G., Milosavljević, T., Stojiljković, M., Zakula, Z., Tepavcević, S., Ribarac-Stepić, N.,& Isenović, E.R.. (2009). Impact of estradiol on insulin signaling in the rat heart. in Cell Biochemistry and Function, 27(2), 102-110. https://doi.org/10.1002/cbf.1542
Koricanac G, Milosavljević T, Stojiljković M, Zakula Z, Tepavcević S, Ribarac-Stepić N, Isenović E. Impact of estradiol on insulin signaling in the rat heart. in Cell Biochemistry and Function. 2009;27(2):102-110. doi:10.1002/cbf.1542 .
Koricanac, G., Milosavljević, T., Stojiljković, Mojca, Zakula, Z., Tepavcević, S., Ribarac-Stepić, N., Isenović, E.R., "Impact of estradiol on insulin signaling in the rat heart" in Cell Biochemistry and Function, 27, no. 2 (2009):102-110, https://doi.org/10.1002/cbf.1542 . .