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J. Biol. Chem., Vol. 276, Issue 44, 40441-40448, November 2, 2001
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From the We have identified the amphibian ghrelin
from the stomach of the bullfrog. We also examined growth hormone
(GH)-releasing activity of this novel peptide in both the rat and
bullfrog. The three forms of ghrelin identified, each comprised of 27 or 28 amino acids, possessed 29% sequence identity to the mammalian ghrelins. A unique threonine at amino acid position 3 (Thr3) in bullfrog ghrelin differs from the serine
present in the mammalian ghrelins; this Thr3 is acylated by
either n-octanoic or n-decanoic acid. The
frog ghrelin-28 has a complete structure of GLT
(O-n-octanoyl)FLSPADMQKIAERQSQNKLRHGNM; the
structure of frog ghrelin-27 was determined to be
GLT(O-n-octanoyl)FLSPADMQKIAERQSQNKLRHGN; frog
ghelin-27-C10 possessed a structure of
GLT(O-n-decanoyl)FLSPADMQKIAERQSQNKLRHGN. Northern blot analysis demonstrated that ghrelin mRNA is
predominantly expressed in the stomach. Low levels of gene expression
were observed in the heart, lung, small intestine, gall bladder,
pancreas, and testes, as revealed by reverse transcription polymerase
chain reaction analysis. Bullfrog ghrelin stimulated the
secretion of both GH and prolactin in dispersed bullfrog pituitary
cells with potency 2-3 orders of magnitude greater than that of rat
ghrelin. Bullfrog ghrelin, however, was only minimally effective in
elevating plasma GH levels following intravenous injection into rats.
These results indicate that although the regulatory mechanism of
ghrelin to induce GH secretion is evolutionary conserved, the
structural changes in the different ghrelins result in species-specific
receptor binding.
The nucleotide sequence(s) reported in this paper has been submitted to the DDBJ/GenBankTM/EBI Data Bank with accession number(s) AB058510.
Bullfrog Ghrelin Is Modified by n-Octanoic Acid at
Its Third Threonine Residue*
§,,,
,,,
Department of Biochemistry, National
Cardiovascular Center Research Institute, 5-7-1 Fujishirodai, Suita,
Osaka 565-8565, Japan, the ¶ Department of Biology, School of
Education, Waseda University, 1-6-1 Nishiwaseda, Shinjuku-ku Tokyo
169-8050, Japan, and the Suntory Institute for Medicinal
Research and Development, 2716-1 Kurakake, Akaiwa, Chiyoda-machi,
Ora-gun, Gunma 370-0503, Japan
*
This work was supported in part by a grant-in-aid for
Scientific Research from the Ministry of Education, Science and Culture of Japan, a grant-in-aid for Scientific Research from the Science and
Technology Agency of Japan, and a grant-in-aid for the Promotion of
Fundamental Studies in Health Science from the Organization for
Pharmaceutical Safety and Research (OPSR) of Japan.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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