Document Detail

Purification and properties of ghrelin from the intestine of the goldfish, Carassius auratus.
MedLine Citation:
PMID:  19150635     Owner:  NLM     Status:  MEDLINE    
In goldfish, intraperitoneal (IP) or intracerebroventricular (ICV) administration of synthetic ghrelin consisting of 12- or 19-amino-acid residues, deduced from its precursor cDNA, with an octanoic acid modification at the third N-terminal serine residue (Ser(3)), stimulates growth hormone release and food intake. However, native ghrelin generated from its precursor has not yet been identified in this species. Therefore, we purified ghrelin from the goldfish intestine using acid extraction, cation-exchange and reverse-phase high-performance liquid chromatography combined with immune-affinity purification. In order to confirm ghrelin activity in the fractions at each purification step, we examined the effect of each fraction on intracellular Ca(2+) mobilization in rat growth hormone secretagogue-receptor (GHS-R)-expressing cells. We characterized the goldfish ghrelin as 11 molecular forms consisting of 14-, 17-, 18- and 19-amino-acid residues with acylation at Ser(3), and the 17-residue form was predominant. We then synthesized 17-residue forms with octanoic acid modification (octanoyl ghrelin17) and without acylation (des-acyl ghrelin17) at Ser(3), and examined their biological activity. Octanoyl ghrelin17, but not des-acyl ghrelin17, increased the intracellular Ca(2+) concentration in rat GHS-R-expressing cells with a potency similar to those of synthetic ghrelin consisting of 12 residues (octanoyl ghrelin12) and octanoyl rat ghrelin. IP and ICV administration of octanoyl ghrelin17 and octanoyl ghrelin12, but not des-acyl ghrelin17, increased food intake in goldfish. The present findings indicate that native goldfish ghrelin consists of 11 molecular variants, the major form being a 17-residue peptide. This dominant form with acylation is implicated in the regulation of food intake in goldfish.
Tohru Miura; Keisuke Maruyama; Hiroyuki Kaiya; Mikiya Miyazato; Kenji Kangawa; Minoru Uchiyama; Seiji Shioda; Kouhei Matsuda
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-12-27
Journal Detail:
Title:  Peptides     Volume:  30     ISSN:  1873-5169     ISO Abbreviation:  Peptides     Publication Date:  2009 Apr 
Date Detail:
Created Date:  2009-03-30     Completed Date:  2009-08-05     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8008690     Medline TA:  Peptides     Country:  United States    
Other Details:
Languages:  eng     Pagination:  758-65     Citation Subset:  IM    
University of Toyama, Gofuku, Japan.
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MeSH Terms
Chromatography, Affinity
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Feeding Behavior / drug effects
Ghrelin / administration & dosage,  genetics,  isolation & purification*,  pharmacology
Injections, Intraperitoneal
Injections, Intraventricular
Intestines / chemistry*
RNA, Messenger / genetics
Reg. No./Substance:
0/Ghrelin; 0/RNA, Messenger

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