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Physiological role of ghrelin as revealed by the ghrelin and GOAT knockout mice.
Kang, Kihwa; Zmuda, Erik; Sleeman, Mark W.
Afiliación
  • Kang K; Regeneron Pharmaceuticals, Inc, 777 Old Saw Mill River Road, Tarrytown, NY 10591, USA.
Peptides ; 32(11): 2236-41, 2011 Nov.
Article en En | MEDLINE | ID: mdl-21600256
Ghrelin is a gastric hormone that has been shown to regulate food intake and energy metabolism. One unique feature of ghrelin is that its activity is regulated post transcriptionally by ghrelin O-acyltransferase (GOAT) through the addition of fatty acid to the serine residue in the N terminal region. Despite much biochemical characterization, to date no other proteins have been shown to be specifically octonylated by GOAT, suggesting a unique matching of the acyl transferase for a single ligand, ghrelin. If this is indeed correct, then genetic deletion of ghrelin or GOAT should produce near identical phenotypes and there should be extensive overlap in expression patterns. This review summarizes the similarities and differences in the phenotypes with the genetic deletion of ghrelin and GOAT in the various knockout mouse lines reported to date. While there is considerable overlap in expression pattern between ghrelin and GOAT, the latter does exhibit some unique tissue expression that could suggest that additional peptides may be acylated and await discovery and characterization.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Aciltransferasas / Ingestión de Alimentos / Metabolismo Energético / Ghrelina / Estudios de Asociación Genética / Glucosa Límite: Animals / Humans Idioma: En Revista: Peptides Año: 2011 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Aciltransferasas / Ingestión de Alimentos / Metabolismo Energético / Ghrelina / Estudios de Asociación Genética / Glucosa Límite: Animals / Humans Idioma: En Revista: Peptides Año: 2011 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos