Purification and characterization of feline ghrelin and its possible role

Ghrelin, a novel 28-amino acid peptide with an n-octanoyl modification at Ser 3, has been isolated from rat and human stomach as an endogenous ligand for the growth hormone secretagogue receptor. Here, we purified feline ghrelin and examined its possible physiological role in cats. The major active...

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Published in	Domestic animal endocrinology Vol. 32; no. 2; pp. 93 - 105
Main Authors	Ida, Takanori, Miyazato, Mikiya, Naganobu, Kiyokazu, Nakahara, Keiko, Sato, Miho, Lin, Xing-Zi, Kaiya, Hiroyuki, Doi, Kentaro, Noda, Soushi, Kubo, Ayako, Murakami, Noboru, Kangawa, Kenji
Format	Journal Article
Language	English
Published	United States Elsevier Inc 01.02.2007
Subjects	Amino Acid Sequence amino acid sequences Animals Base Sequence blood Cat Cats chemical structure chemistry Chromatography, High Pressure Liquid Cloning, Molecular complementary DNA DNA, Complementary DNA, Complementary - chemistry DNA, Complementary - genetics Enzyme-Linked Immunosorbent Assay Fasting fatty acids feed deprivation Feeding behavior genetics Ghrelin Growth Hormone Growth Hormone - blood hormonal regulation hormone secretion isolation & purification Kinetics Molecular Sequence Data nucleotide sequences Peptide Hormones Peptide Hormones - chemistry Peptide Hormones - genetics Peptide Hormones - isolation & purification Peptide Hormones - physiology physiology purification somatotropin Feeding behavior Growth hormone Ghrelin Cat
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ISSN	0739-7240 1879-0054
DOI	10.1016/j.domaniend.2006.01.002

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Abstract	Ghrelin, a novel 28-amino acid peptide with an n-octanoyl modification at Ser 3, has been isolated from rat and human stomach as an endogenous ligand for the growth hormone secretagogue receptor. Here, we purified feline ghrelin and examined its possible physiological role in cats. The major active form of feline ghrelin is a 28-amino acid peptide octanoylated (C8:0) at Ser 3; except for one amino acid residue replacement, this structure is identical to those of rat and human ghrelins. However, much structural divergence in peptide length and fatty acid modification was observed in feline ghrelin: peptides consisting of 27 or 26 amino acids lacking Gln 14 and/or Arg 28 were found, and the third serine residue was modified by octanoic acid (C8:0), decanoic acid (10:0), or unsaturated fatty acids (C8:1, C10:1 and C10:2). In agreement with the structural divergence, two kinds of cDNA with different lengths were isolated. Administration of synthetic rat ghrelin increased plasma growth hormone levels in cats, with a potency similar to that in rat or human. Plasma levels of ghrelin in cats increased approximately 2.5-fold after fasting. The present study indicates the existence of structural divergence in feline ghrelin and suggests that, as in other animals, ghrelin may play important roles in GH release and feeding in cats.
AbstractList	Ghrelin, a novel 28-amino acid peptide with an n-octanoyl modification at Ser 3, has been isolated from rat and human stomach as an endogenous ligand for the growth hormone secretagogue receptor. Here, we purified feline ghrelin and examined its possible physiological role in cats. The major active form of feline ghrelin is a 28-amino acid peptide octanoylated (C8:0) at Ser 3; except for one amino acid residue replacement, this structure is identical to those of rat and human ghrelins. However, much structural divergence in peptide length and fatty acid modification was observed in feline ghrelin: peptides consisting of 27 or 26 amino acids lacking Gln 14 and/or Arg 28 were found, and the third serine residue was modified by octanoic acid (C8:0), decanoic acid (10:0), or unsaturated fatty acids (C8:1, C10:1 and C10:2). In agreement with the structural divergence, two kinds of cDNA with different lengths were isolated. Administration of synthetic rat ghrelin increased plasma growth hormone levels in cats, with a potency similar to that in rat or human. Plasma levels of ghrelin in cats increased approximately 2.5-fold after fasting. The present study indicates the existence of structural divergence in feline ghrelin and suggests that, as in other animals, ghrelin may play important roles in GH release and feeding in cats. Ghrelin, a novel 28-amino acid peptide with an n-octanoyl modification at Ser3, has been isolated from rat and human stomach as an endogenous ligand for the growth hormone secretagogue receptor. Here, we purified feline ghrelin and examined its possible physiological role in cats. The major active form of feline ghrelin is a 28-amino acid peptide octanoylated (C8:0) at Ser3; except for one amino acid residue replacement, this structure is identical to those of rat and human ghrelins. However, much structural divergence in peptide length and fatty acid modification was observed in feline ghrelin: peptides consisting of 27 or 26 amino acids lacking Gln14 and/or Arg28 were found, and the third serine residue was modified by octanoic acid (C8:0), decanoic acid (10:0), or unsaturated fatty acids (C8:1, C10:1 and C10:2). In agreement with the structural divergence, two kinds of cDNA with different lengths were isolated. Administration of synthetic rat ghrelin increased plasma growth hormone levels in cats, with a potency similar to that in rat or human. Plasma levels of ghrelin in cats increased approximately 2.5-fold after fasting. The present study indicates the existence of structural divergence in feline ghrelin and suggests that, as in other animals, ghrelin may play important roles in GH release and feeding in cats. Ghrelin, a novel 28-amino acid peptide with an n-octanoyl modification at Ser3, has been isolated from rat and human stomach as an endogenous ligand for the growth hormone secretagogue receptor. Here, we purified feline ghrelin and examined its possible physiological role in cats. The major active form of feline ghrelin is a 28-amino acid peptide octanoylated (C8:0) at Ser3; except for one amino acid residue replacement, this structure is identical to those of rat and human ghrelins. However, much structural divergence in peptide length and fatty acid modification was observed in feline ghrelin: peptides consisting of 27 or 26 amino acids lacking Gln14 and/or Arg28 were found, and the third serine residue was modified by octanoic acid (C8:0), decanoic acid (10:0), or unsaturated fatty acids (C8:1, C10:1 and C10:2). In agreement with the structural divergence, two kinds of cDNA with different lengths were isolated. Administration of synthetic rat ghrelin increased plasma growth hormone levels in cats, with a potency similar to that in rat or human. Plasma levels of ghrelin in cats increased approximately 2.5-fold after fasting. The present study indicates the existence of structural divergence in feline ghrelin and suggests that, as in other animals, ghrelin may play important roles in GH release and feeding in cats.Ghrelin, a novel 28-amino acid peptide with an n-octanoyl modification at Ser3, has been isolated from rat and human stomach as an endogenous ligand for the growth hormone secretagogue receptor. Here, we purified feline ghrelin and examined its possible physiological role in cats. The major active form of feline ghrelin is a 28-amino acid peptide octanoylated (C8:0) at Ser3; except for one amino acid residue replacement, this structure is identical to those of rat and human ghrelins. However, much structural divergence in peptide length and fatty acid modification was observed in feline ghrelin: peptides consisting of 27 or 26 amino acids lacking Gln14 and/or Arg28 were found, and the third serine residue was modified by octanoic acid (C8:0), decanoic acid (10:0), or unsaturated fatty acids (C8:1, C10:1 and C10:2). In agreement with the structural divergence, two kinds of cDNA with different lengths were isolated. Administration of synthetic rat ghrelin increased plasma growth hormone levels in cats, with a potency similar to that in rat or human. Plasma levels of ghrelin in cats increased approximately 2.5-fold after fasting. The present study indicates the existence of structural divergence in feline ghrelin and suggests that, as in other animals, ghrelin may play important roles in GH release and feeding in cats.
Author	Murakami, Noboru Nakahara, Keiko Ida, Takanori Noda, Soushi Sato, Miho Kangawa, Kenji Naganobu, Kiyokazu Miyazato, Mikiya Kaiya, Hiroyuki Lin, Xing-Zi Kubo, Ayako Doi, Kentaro
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Snippet	Ghrelin, a novel 28-amino acid peptide with an n-octanoyl modification at Ser 3, has been isolated from rat and human stomach as an endogenous ligand for the... Ghrelin, a novel 28-amino acid peptide with an n-octanoyl modification at Ser3, has been isolated from rat and human stomach as an endogenous ligand for the...
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SubjectTerms	Amino Acid Sequence amino acid sequences Animals Base Sequence blood Cat Cats chemical structure chemistry Chromatography, High Pressure Liquid Cloning, Molecular complementary DNA DNA, Complementary DNA, Complementary - chemistry DNA, Complementary - genetics Enzyme-Linked Immunosorbent Assay Fasting fatty acids feed deprivation Feeding behavior genetics Ghrelin Growth Hormone Growth Hormone - blood hormonal regulation hormone secretion isolation & purification Kinetics Molecular Sequence Data nucleotide sequences Peptide Hormones Peptide Hormones - chemistry Peptide Hormones - genetics Peptide Hormones - isolation & purification Peptide Hormones - physiology physiology purification somatotropin
Title	Purification and characterization of feline ghrelin and its possible role
URI	https://dx.doi.org/10.1016/j.domaniend.2006.01.002 https://www.ncbi.nlm.nih.gov/pubmed/16466902 https://www.proquest.com/docview/47313211 https://www.proquest.com/docview/68969161
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