Ministry of Science, Republic of Serbia [143030B]

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Ministry of Science, Republic of Serbia [143030B]

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Publications

Impact of estradiol on insulin signaling in the rat heart

Korićanac, Goran; Milosavljević, Tijana; Stojiljković, Mojca D.; Žakula, Zorica; Tepavčević, Snežana; Ribarac-Stepić, Nevena B.; Isenović, Esma R.

(2009)

TY  - JOUR
AU  - Korićanac, Goran
AU  - Milosavljević, Tijana
AU  - Stojiljković, Mojca D.
AU  - Žakula, Zorica
AU  - Tepavčević, Snežana
AU  - Ribarac-Stepić, Nevena B.
AU  - Isenović, Esma R.
PY  - 2009
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3648
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 chance 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) Ser(473) 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 Ser(473) 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 (C) 2009 John Wiley and Sons, Ltd.
T2  - Cell Biochemistry and Function
T1  - Impact of estradiol on insulin signaling in the rat heart
VL  - 27
IS  - 2
SP  - 102
EP  - 110
DO  - 10.1002/cbf.1542
ER  - 
@article{
author = "Korićanac, Goran and Milosavljević, Tijana and Stojiljković, Mojca D. and Žakula, Zorica and Tepavčević, Snežana and Ribarac-Stepić, Nevena B. and Isenović, Esma 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 chance 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) Ser(473) 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 Ser(473) 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 (C) 2009 John Wiley and Sons, Ltd.",
journal = "Cell Biochemistry and Function",
title = "Impact of estradiol on insulin signaling in the rat heart",
volume = "27",
number = "2",
pages = "102-110",
doi = "10.1002/cbf.1542"
}
Korićanac, G., Milosavljević, T., Stojiljković, M. D., Žakula, Z., Tepavčević, S., Ribarac-Stepić, N. B.,& 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
Korićanac G, Milosavljević T, Stojiljković MD, Žakula Z, Tepavčević S, Ribarac-Stepić NB, Isenović ER. 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 .
Korićanac, Goran, Milosavljević, Tijana, Stojiljković, Mojca D., Žakula, Zorica, Tepavčević, Snežana, Ribarac-Stepić, Nevena B., Isenović, Esma 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 . .
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