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Titolo:
NEUROPEPTIDE-Y-3-36 IS AN ENDOGENOUS LIGAND SELECTIVE FOR Y2 RECEPTORS
Autore:
GRANDT D; SCHIMICZEK M; RASCHER W; FETH F; SHIVELY J; LEE TD; DAVIS MT; REEVE JR; MICHEL MC;
Indirizzi:
UNIV ESSEN GESAMTHSCH,DEPT MED,DIV GASTROENTEROL & NEPHROL,HUFELANDSTR 55 D-45122 ESSEN GERMANY UNIV GIESSEN,DEPT PEDIAT GIESSEN GERMANY CITY HOPE NATL MED CTR,BECKMAN RES INST,DIV IMMUNOL DUARTE CA 91010 UNIV CALIF LOS ANGELES,CTR DIGEST DIS,CURE LOS ANGELES CA 90073 VET ADM WADSWORTH MED CTR LOS ANGELES CA 90073
Titolo Testata:
Regulatory peptides
fascicolo: 1, volume: 67, anno: 1996,
pagine: 33 - 37
SICI:
0167-0115(1996)67:1<33:NIAELS>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
DIPEPTIDYL PEPTIDASE-IV; STRUCTURAL CHARACTERIZATION; BRAIN PEPTIDE; PYY; HORMONE; SUBTYPES; CELLS;
Keywords:
NEUROPEPTIDE Y; NEUROTRANSMITTER; RECEPTOR; MOLECULAR HETEROGENEITY; PIG; BRAIN; HPLC; RADIOIMMUNOASSAY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
23
Recensione:
Indirizzi per estratti:
Citazione:
D. Grandt et al., "NEUROPEPTIDE-Y-3-36 IS AN ENDOGENOUS LIGAND SELECTIVE FOR Y2 RECEPTORS", Regulatory peptides, 67(1), 1996, pp. 33-37

Abstract

Neuropeptide Y (NPY 1-36) binds to Y1 and Y2 receptors with similar affinity. No endogenous molecular form of NPY with selectivity for Y1 or Y2 receptors has been described so far. We report the presence of anendogenous fragment of NPY in porcine brain, NPY 3-36, which lacks the amino-terminal dipeptide Tyr-Pro of NPY 1-36. NPY 3-36 accounts for 35% of NPY-like immunoreactivity in porcine brain. We have compared binding of NPY 3-36 and NPY 1-36 in model systems of Y1-like (SK-N-MC cells) and Y2-like receptors (CHP234 cells). NPY 3-36 and NPY 1-36 had similarly high affinity for Y2-like receptors on CHP234 cells, but NPY 3-36 had a 1000-fold lower affinity than NPY 1-36 for Y1-like receptors on SK-N-MC cells. Thus amino-terminal cleavage of NPY 1-36 generating NPY 3-36 converts an unselective Y1/Y2 receptor ligand into a highlyY2 selective ligand. This may be a means of fine tuning NPY biological actions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 05:29:08