Characterization of prolactin-releasing peptide: Binding, signaling and hormone secretion in rodent pituitary cell lines endogenously expressing its receptor

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F11%3A00359843" target="_blank" >RIV/61388963:_____/11:00359843 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11150/11:10105705

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.peptides.2010.12.011" target="_blank" >http://dx.doi.org/10.1016/j.peptides.2010.12.011</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.peptides.2010.12.011" target="_blank" >10.1016/j.peptides.2010.12.011</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Characterization of prolactin-releasing peptide: Binding, signaling and hormone secretion in rodent pituitary cell lines endogenously expressing its receptor

Popis výsledku v původním jazyce

The recently discovered prolactin-releasing peptide (PrRP) binds to the PrRP receptor and is involved in endocrine regulation and energy metabolism. However, its main physiological role is currently unknown. Two biologically active isoforms of PrRP exist: the 31 (PrRP31) and the 20 (PrRP20) amino acid forms, which both contain a C-terminal Phe amide sequence. In the present study, the PrRP receptor was immunodetected in three rodent tumor pituitary cell lines: GH3, AtT20 and RC-4B/C cells. Food intake after intracerebroventricular administration of PrRP analogs in fasted mice was followed. Both PrRP31 and PrRP20 decreased food intake, but PrRP13 did not show significant effect.

Název v anglickém jazyce

Characterization of prolactin-releasing peptide: Binding, signaling and hormone secretion in rodent pituitary cell lines endogenously expressing its receptor

Popis výsledku anglicky

The recently discovered prolactin-releasing peptide (PrRP) binds to the PrRP receptor and is involved in endocrine regulation and energy metabolism. However, its main physiological role is currently unknown. Two biologically active isoforms of PrRP exist: the 31 (PrRP31) and the 20 (PrRP20) amino acid forms, which both contain a C-terminal Phe amide sequence. In the present study, the PrRP receptor was immunodetected in three rodent tumor pituitary cell lines: GH3, AtT20 and RC-4B/C cells. Food intake after intracerebroventricular administration of PrRP analogs in fasted mice was followed. Both PrRP31 and PrRP20 decreased food intake, but PrRP13 did not show significant effect.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CC - Organická chemie

OECD FORD obor

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Projekt

<a href="/cs/project/GAP303%2F10%2F1368" target="_blank" >GAP303/10/1368: Nové farmakologické intervence ovlivňující energetickou rovnováhu a vývoj inzulínové rezistence/diabetu mellitu 2. typu</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Peptides

ISSN

0196-9781

e-ISSN

—

Svazek periodika

32

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

7

Strana od-do

811-817

Kód UT WoS článku

000289707300026

EID výsledku v databázi Scopus

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