The Circadian Rhythms of STAT3 in the Rat Pineal Gland and Its Involvement in Arylalkylamine-N-Acetyltransferase Regulation

0549779 - FGÚ 2022 RIV CH eng J - Článek v odborném periodiku
Moravcová, S. - Filipovská, E. - Spišská, V. - Svobodová, Irena - Novotný, J. - Bendová, Z.
The Circadian Rhythms of STAT3 in the Rat Pineal Gland and Its Involvement in Arylalkylamine-N-Acetyltransferase Regulation.
Life. Roč. 11, č. 10 (2021), č. článku 1105. E-ISSN 2075-1729
Grant CEP: GA MZd(CZ) EF16_025/0007444
Institucionální podpora: RVO:67985823
Klíčová slova: STAT3 * arylalkylamine-N-acetyltransferase * pineal gland * circadian rhythms * lipopolysaccharide * rat
Obor OECD: Physiology (including cytology)
Impakt faktor: 3.253, rok: 2021
Způsob publikování: Open access
https://www.mdpi.com/2075-1729/11/10/1105

In rodents, the melatonin production by the pineal gland is controlled through adrenergic signaling from the suprachiasmatic nuclei and regulation of the principal enzyme in its synthesis, arylalkylamine-N-acetyltransferase (AANAT). In the present study, we identified increased isoprenaline-induced aa-nat expression and nocturnal AANAT activity in the pineal glands in response to the silencing of the signal transducer and activator of transcription 3 (STAT3) with siRNA or STAT3 inhibitors WP1066 and AZD1480. This AANAT activity enhancement in vivo did not interfere with light-induced AANAT suppression. Systemic or in vitro lipopolysaccharide (LPS) administration markedly increased Stat3 expression and STAT3 phosphorylation, but it did not significantly affect AANAT expression or activity. Simultaneous LPS administration and Stat3 silencing enhanced the aa-nat transcription and AANAT activity to a similar extent as Stat3 inhibition without LPS co-administration. Furthermore, we describe the circadian rhythmicity in Stat3 expression and the phosphorylated form of STAT3 protein in the rat pineal gland. Our data suggest that the higher nocturnal endogenous level of STAT3 in the pineal gland decelerates or hampers the process of NA-induced AANAT activation or affects the AANAT enzyme stability.
Trvalý link: http://hdl.handle.net/11104/0325688