Purification and Characterization of Caprine Ghrelin and Its Effect on Growth Hormone Release
Abstract Ghrelin, a novel peptide modified by n-octanoic acid at the third serine residue ($ Ser^{3} $), serves as an endogenous ligand for the growth hormone secretagogue receptor (GHS-R) 1a. The octanoyl modification at $ Ser^{3} $ is essential for receptor binding or growth hormone release. Here,...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Ida, Takanori [verfasserIn] Miyazato, Mikiya [verfasserIn] Lin, Xing-Zi [verfasserIn] Kaiya, Hiroyuki [verfasserIn] Sato, Takahiro [verfasserIn] Nakahara, Keiko [verfasserIn] Murakami, Noboru [verfasserIn] Kangawa, Kenji [verfasserIn] Kojima, Masayasu [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2010 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Journal of molecular neuroscience - New York, NY : Springer, 1998, 42(2010), 1 vom: 02. Mai, Seite 99-105 |
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| Übergeordnetes Werk: |
volume:42 ; year:2010 ; number:1 ; day:02 ; month:05 ; pages:99-105 |
| Links: |
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| DOI / URN: |
10.1007/s12031-010-9379-0 |
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| Katalog-ID: |
SPR023840846 |
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| 245 | 1 | 0 | |a Purification and Characterization of Caprine Ghrelin and Its Effect on Growth Hormone Release |
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| 520 | |a Abstract Ghrelin, a novel peptide modified by n-octanoic acid at the third serine residue ($ Ser^{3} $), serves as an endogenous ligand for the growth hormone secretagogue receptor (GHS-R) 1a. The octanoyl modification at $ Ser^{3} $ is essential for receptor binding or growth hormone release. Here, we report the purification of caprine ghrelin and its physiological role in goats. The major form of caprine ghrelin is a 27 amino acid peptide that is octanoylated (C8:0) at $ Ser^{3} $ and lacks $ Gln^{14} $, which is present in rat and human ghrelin. Additionally, we identified various acyl modifications in caprine ghrelin: nonanoic (C9:0), decanoic (10:0), unsaturated octanoic acids (C8:1), and an unidentified fatty acid modification. We observed that differences in acyl modifications affected GHS-R1a activation. In addition, administration of synthetic bovine ghrelin increased plasma growth hormone (GH) levels in goats. Thus, the present study indicates a structural divergence in caprine ghrelin and suggests that ghrelin is involved in GH release in ruminants. | ||
| 650 | 4 | |a Ghrelin |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Goat |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Growth hormone |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Fatty acid modification |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Miyazato, Mikiya |e verfasserin |4 aut | |
| 700 | 1 | |a Lin, Xing-Zi |e verfasserin |4 aut | |
| 700 | 1 | |a Kaiya, Hiroyuki |e verfasserin |4 aut | |
| 700 | 1 | |a Sato, Takahiro |e verfasserin |4 aut | |
| 700 | 1 | |a Nakahara, Keiko |e verfasserin |4 aut | |
| 700 | 1 | |a Murakami, Noboru |e verfasserin |4 aut | |
| 700 | 1 | |a Kangawa, Kenji |e verfasserin |4 aut | |
| 700 | 1 | |a Kojima, Masayasu |e verfasserin |4 aut | |
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| 912 | |a GBV_ILN_2061 | ||
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| 912 | |a GBV_ILN_2106 | ||
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10.1007/s12031-010-9379-0 doi (DE-627)SPR023840846 (SPR)s12031-010-9379-0-e DE-627 ger DE-627 rakwb eng 610 ASE 44.90 bkl Ida, Takanori verfasserin aut Purification and Characterization of Caprine Ghrelin and Its Effect on Growth Hormone Release 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Ghrelin, a novel peptide modified by n-octanoic acid at the third serine residue ($ Ser^{3} $), serves as an endogenous ligand for the growth hormone secretagogue receptor (GHS-R) 1a. The octanoyl modification at $ Ser^{3} $ is essential for receptor binding or growth hormone release. Here, we report the purification of caprine ghrelin and its physiological role in goats. The major form of caprine ghrelin is a 27 amino acid peptide that is octanoylated (C8:0) at $ Ser^{3} $ and lacks $ Gln^{14} $, which is present in rat and human ghrelin. Additionally, we identified various acyl modifications in caprine ghrelin: nonanoic (C9:0), decanoic (10:0), unsaturated octanoic acids (C8:1), and an unidentified fatty acid modification. We observed that differences in acyl modifications affected GHS-R1a activation. In addition, administration of synthetic bovine ghrelin increased plasma growth hormone (GH) levels in goats. Thus, the present study indicates a structural divergence in caprine ghrelin and suggests that ghrelin is involved in GH release in ruminants. Ghrelin (dpeaa)DE-He213 Goat (dpeaa)DE-He213 Growth hormone (dpeaa)DE-He213 Fatty acid modification (dpeaa)DE-He213 Miyazato, Mikiya verfasserin aut Lin, Xing-Zi verfasserin aut Kaiya, Hiroyuki verfasserin aut Sato, Takahiro verfasserin aut Nakahara, Keiko verfasserin aut Murakami, Noboru verfasserin aut Kangawa, Kenji verfasserin aut Kojima, Masayasu verfasserin aut Enthalten in Journal of molecular neuroscience New York, NY : Springer, 1998 42(2010), 1 vom: 02. Mai, Seite 99-105 (DE-627)342319477 (DE-600)2071508-0 1559-1166 nnns volume:42 year:2010 number:1 day:02 month:05 pages:99-105 https://dx.doi.org/10.1007/s12031-010-9379-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 44.90 ASE AR 42 2010 1 02 05 99-105 |
| spelling |
10.1007/s12031-010-9379-0 doi (DE-627)SPR023840846 (SPR)s12031-010-9379-0-e DE-627 ger DE-627 rakwb eng 610 ASE 44.90 bkl Ida, Takanori verfasserin aut Purification and Characterization of Caprine Ghrelin and Its Effect on Growth Hormone Release 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Ghrelin, a novel peptide modified by n-octanoic acid at the third serine residue ($ Ser^{3} $), serves as an endogenous ligand for the growth hormone secretagogue receptor (GHS-R) 1a. The octanoyl modification at $ Ser^{3} $ is essential for receptor binding or growth hormone release. Here, we report the purification of caprine ghrelin and its physiological role in goats. The major form of caprine ghrelin is a 27 amino acid peptide that is octanoylated (C8:0) at $ Ser^{3} $ and lacks $ Gln^{14} $, which is present in rat and human ghrelin. Additionally, we identified various acyl modifications in caprine ghrelin: nonanoic (C9:0), decanoic (10:0), unsaturated octanoic acids (C8:1), and an unidentified fatty acid modification. We observed that differences in acyl modifications affected GHS-R1a activation. In addition, administration of synthetic bovine ghrelin increased plasma growth hormone (GH) levels in goats. Thus, the present study indicates a structural divergence in caprine ghrelin and suggests that ghrelin is involved in GH release in ruminants. Ghrelin (dpeaa)DE-He213 Goat (dpeaa)DE-He213 Growth hormone (dpeaa)DE-He213 Fatty acid modification (dpeaa)DE-He213 Miyazato, Mikiya verfasserin aut Lin, Xing-Zi verfasserin aut Kaiya, Hiroyuki verfasserin aut Sato, Takahiro verfasserin aut Nakahara, Keiko verfasserin aut Murakami, Noboru verfasserin aut Kangawa, Kenji verfasserin aut Kojima, Masayasu verfasserin aut Enthalten in Journal of molecular neuroscience New York, NY : Springer, 1998 42(2010), 1 vom: 02. Mai, Seite 99-105 (DE-627)342319477 (DE-600)2071508-0 1559-1166 nnns volume:42 year:2010 number:1 day:02 month:05 pages:99-105 https://dx.doi.org/10.1007/s12031-010-9379-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 44.90 ASE AR 42 2010 1 02 05 99-105 |
| allfields_unstemmed |
10.1007/s12031-010-9379-0 doi (DE-627)SPR023840846 (SPR)s12031-010-9379-0-e DE-627 ger DE-627 rakwb eng 610 ASE 44.90 bkl Ida, Takanori verfasserin aut Purification and Characterization of Caprine Ghrelin and Its Effect on Growth Hormone Release 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Ghrelin, a novel peptide modified by n-octanoic acid at the third serine residue ($ Ser^{3} $), serves as an endogenous ligand for the growth hormone secretagogue receptor (GHS-R) 1a. The octanoyl modification at $ Ser^{3} $ is essential for receptor binding or growth hormone release. Here, we report the purification of caprine ghrelin and its physiological role in goats. The major form of caprine ghrelin is a 27 amino acid peptide that is octanoylated (C8:0) at $ Ser^{3} $ and lacks $ Gln^{14} $, which is present in rat and human ghrelin. Additionally, we identified various acyl modifications in caprine ghrelin: nonanoic (C9:0), decanoic (10:0), unsaturated octanoic acids (C8:1), and an unidentified fatty acid modification. We observed that differences in acyl modifications affected GHS-R1a activation. In addition, administration of synthetic bovine ghrelin increased plasma growth hormone (GH) levels in goats. Thus, the present study indicates a structural divergence in caprine ghrelin and suggests that ghrelin is involved in GH release in ruminants. Ghrelin (dpeaa)DE-He213 Goat (dpeaa)DE-He213 Growth hormone (dpeaa)DE-He213 Fatty acid modification (dpeaa)DE-He213 Miyazato, Mikiya verfasserin aut Lin, Xing-Zi verfasserin aut Kaiya, Hiroyuki verfasserin aut Sato, Takahiro verfasserin aut Nakahara, Keiko verfasserin aut Murakami, Noboru verfasserin aut Kangawa, Kenji verfasserin aut Kojima, Masayasu verfasserin aut Enthalten in Journal of molecular neuroscience New York, NY : Springer, 1998 42(2010), 1 vom: 02. Mai, Seite 99-105 (DE-627)342319477 (DE-600)2071508-0 1559-1166 nnns volume:42 year:2010 number:1 day:02 month:05 pages:99-105 https://dx.doi.org/10.1007/s12031-010-9379-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 44.90 ASE AR 42 2010 1 02 05 99-105 |
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10.1007/s12031-010-9379-0 doi (DE-627)SPR023840846 (SPR)s12031-010-9379-0-e DE-627 ger DE-627 rakwb eng 610 ASE 44.90 bkl Ida, Takanori verfasserin aut Purification and Characterization of Caprine Ghrelin and Its Effect on Growth Hormone Release 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Ghrelin, a novel peptide modified by n-octanoic acid at the third serine residue ($ Ser^{3} $), serves as an endogenous ligand for the growth hormone secretagogue receptor (GHS-R) 1a. The octanoyl modification at $ Ser^{3} $ is essential for receptor binding or growth hormone release. Here, we report the purification of caprine ghrelin and its physiological role in goats. The major form of caprine ghrelin is a 27 amino acid peptide that is octanoylated (C8:0) at $ Ser^{3} $ and lacks $ Gln^{14} $, which is present in rat and human ghrelin. Additionally, we identified various acyl modifications in caprine ghrelin: nonanoic (C9:0), decanoic (10:0), unsaturated octanoic acids (C8:1), and an unidentified fatty acid modification. We observed that differences in acyl modifications affected GHS-R1a activation. In addition, administration of synthetic bovine ghrelin increased plasma growth hormone (GH) levels in goats. Thus, the present study indicates a structural divergence in caprine ghrelin and suggests that ghrelin is involved in GH release in ruminants. Ghrelin (dpeaa)DE-He213 Goat (dpeaa)DE-He213 Growth hormone (dpeaa)DE-He213 Fatty acid modification (dpeaa)DE-He213 Miyazato, Mikiya verfasserin aut Lin, Xing-Zi verfasserin aut Kaiya, Hiroyuki verfasserin aut Sato, Takahiro verfasserin aut Nakahara, Keiko verfasserin aut Murakami, Noboru verfasserin aut Kangawa, Kenji verfasserin aut Kojima, Masayasu verfasserin aut Enthalten in Journal of molecular neuroscience New York, NY : Springer, 1998 42(2010), 1 vom: 02. Mai, Seite 99-105 (DE-627)342319477 (DE-600)2071508-0 1559-1166 nnns volume:42 year:2010 number:1 day:02 month:05 pages:99-105 https://dx.doi.org/10.1007/s12031-010-9379-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 44.90 ASE AR 42 2010 1 02 05 99-105 |
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10.1007/s12031-010-9379-0 doi (DE-627)SPR023840846 (SPR)s12031-010-9379-0-e DE-627 ger DE-627 rakwb eng 610 ASE 44.90 bkl Ida, Takanori verfasserin aut Purification and Characterization of Caprine Ghrelin and Its Effect on Growth Hormone Release 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Ghrelin, a novel peptide modified by n-octanoic acid at the third serine residue ($ Ser^{3} $), serves as an endogenous ligand for the growth hormone secretagogue receptor (GHS-R) 1a. The octanoyl modification at $ Ser^{3} $ is essential for receptor binding or growth hormone release. Here, we report the purification of caprine ghrelin and its physiological role in goats. The major form of caprine ghrelin is a 27 amino acid peptide that is octanoylated (C8:0) at $ Ser^{3} $ and lacks $ Gln^{14} $, which is present in rat and human ghrelin. Additionally, we identified various acyl modifications in caprine ghrelin: nonanoic (C9:0), decanoic (10:0), unsaturated octanoic acids (C8:1), and an unidentified fatty acid modification. We observed that differences in acyl modifications affected GHS-R1a activation. In addition, administration of synthetic bovine ghrelin increased plasma growth hormone (GH) levels in goats. Thus, the present study indicates a structural divergence in caprine ghrelin and suggests that ghrelin is involved in GH release in ruminants. Ghrelin (dpeaa)DE-He213 Goat (dpeaa)DE-He213 Growth hormone (dpeaa)DE-He213 Fatty acid modification (dpeaa)DE-He213 Miyazato, Mikiya verfasserin aut Lin, Xing-Zi verfasserin aut Kaiya, Hiroyuki verfasserin aut Sato, Takahiro verfasserin aut Nakahara, Keiko verfasserin aut Murakami, Noboru verfasserin aut Kangawa, Kenji verfasserin aut Kojima, Masayasu verfasserin aut Enthalten in Journal of molecular neuroscience New York, NY : Springer, 1998 42(2010), 1 vom: 02. Mai, Seite 99-105 (DE-627)342319477 (DE-600)2071508-0 1559-1166 nnns volume:42 year:2010 number:1 day:02 month:05 pages:99-105 https://dx.doi.org/10.1007/s12031-010-9379-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 44.90 ASE AR 42 2010 1 02 05 99-105 |
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Enthalten in Journal of molecular neuroscience 42(2010), 1 vom: 02. Mai, Seite 99-105 volume:42 year:2010 number:1 day:02 month:05 pages:99-105 |
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Enthalten in Journal of molecular neuroscience 42(2010), 1 vom: 02. Mai, Seite 99-105 volume:42 year:2010 number:1 day:02 month:05 pages:99-105 |
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Ghrelin Goat Growth hormone Fatty acid modification |
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Ida, Takanori @@aut@@ Miyazato, Mikiya @@aut@@ Lin, Xing-Zi @@aut@@ Kaiya, Hiroyuki @@aut@@ Sato, Takahiro @@aut@@ Nakahara, Keiko @@aut@@ Murakami, Noboru @@aut@@ Kangawa, Kenji @@aut@@ Kojima, Masayasu @@aut@@ |
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The octanoyl modification at $ Ser^{3} $ is essential for receptor binding or growth hormone release. Here, we report the purification of caprine ghrelin and its physiological role in goats. The major form of caprine ghrelin is a 27 amino acid peptide that is octanoylated (C8:0) at $ Ser^{3} $ and lacks $ Gln^{14} $, which is present in rat and human ghrelin. Additionally, we identified various acyl modifications in caprine ghrelin: nonanoic (C9:0), decanoic (10:0), unsaturated octanoic acids (C8:1), and an unidentified fatty acid modification. We observed that differences in acyl modifications affected GHS-R1a activation. In addition, administration of synthetic bovine ghrelin increased plasma growth hormone (GH) levels in goats. 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|
| author |
Ida, Takanori |
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Ida, Takanori ddc 610 bkl 44.90 misc Ghrelin misc Goat misc Growth hormone misc Fatty acid modification Purification and Characterization of Caprine Ghrelin and Its Effect on Growth Hormone Release |
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1559-1166 |
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610 ASE 44.90 bkl Purification and Characterization of Caprine Ghrelin and Its Effect on Growth Hormone Release Ghrelin (dpeaa)DE-He213 Goat (dpeaa)DE-He213 Growth hormone (dpeaa)DE-He213 Fatty acid modification (dpeaa)DE-He213 |
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ddc 610 bkl 44.90 misc Ghrelin misc Goat misc Growth hormone misc Fatty acid modification |
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ddc 610 bkl 44.90 misc Ghrelin misc Goat misc Growth hormone misc Fatty acid modification |
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ddc 610 bkl 44.90 misc Ghrelin misc Goat misc Growth hormone misc Fatty acid modification |
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Purification and Characterization of Caprine Ghrelin and Its Effect on Growth Hormone Release |
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Purification and Characterization of Caprine Ghrelin and Its Effect on Growth Hormone Release |
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Ida, Takanori |
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Journal of molecular neuroscience |
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Journal of molecular neuroscience |
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Ida, Takanori Miyazato, Mikiya Lin, Xing-Zi Kaiya, Hiroyuki Sato, Takahiro Nakahara, Keiko Murakami, Noboru Kangawa, Kenji Kojima, Masayasu |
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purification and characterization of caprine ghrelin and its effect on growth hormone release |
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Purification and Characterization of Caprine Ghrelin and Its Effect on Growth Hormone Release |
| abstract |
Abstract Ghrelin, a novel peptide modified by n-octanoic acid at the third serine residue ($ Ser^{3} $), serves as an endogenous ligand for the growth hormone secretagogue receptor (GHS-R) 1a. The octanoyl modification at $ Ser^{3} $ is essential for receptor binding or growth hormone release. Here, we report the purification of caprine ghrelin and its physiological role in goats. The major form of caprine ghrelin is a 27 amino acid peptide that is octanoylated (C8:0) at $ Ser^{3} $ and lacks $ Gln^{14} $, which is present in rat and human ghrelin. Additionally, we identified various acyl modifications in caprine ghrelin: nonanoic (C9:0), decanoic (10:0), unsaturated octanoic acids (C8:1), and an unidentified fatty acid modification. We observed that differences in acyl modifications affected GHS-R1a activation. In addition, administration of synthetic bovine ghrelin increased plasma growth hormone (GH) levels in goats. Thus, the present study indicates a structural divergence in caprine ghrelin and suggests that ghrelin is involved in GH release in ruminants. |
| abstractGer |
Abstract Ghrelin, a novel peptide modified by n-octanoic acid at the third serine residue ($ Ser^{3} $), serves as an endogenous ligand for the growth hormone secretagogue receptor (GHS-R) 1a. The octanoyl modification at $ Ser^{3} $ is essential for receptor binding or growth hormone release. Here, we report the purification of caprine ghrelin and its physiological role in goats. The major form of caprine ghrelin is a 27 amino acid peptide that is octanoylated (C8:0) at $ Ser^{3} $ and lacks $ Gln^{14} $, which is present in rat and human ghrelin. Additionally, we identified various acyl modifications in caprine ghrelin: nonanoic (C9:0), decanoic (10:0), unsaturated octanoic acids (C8:1), and an unidentified fatty acid modification. We observed that differences in acyl modifications affected GHS-R1a activation. In addition, administration of synthetic bovine ghrelin increased plasma growth hormone (GH) levels in goats. Thus, the present study indicates a structural divergence in caprine ghrelin and suggests that ghrelin is involved in GH release in ruminants. |
| abstract_unstemmed |
Abstract Ghrelin, a novel peptide modified by n-octanoic acid at the third serine residue ($ Ser^{3} $), serves as an endogenous ligand for the growth hormone secretagogue receptor (GHS-R) 1a. The octanoyl modification at $ Ser^{3} $ is essential for receptor binding or growth hormone release. Here, we report the purification of caprine ghrelin and its physiological role in goats. The major form of caprine ghrelin is a 27 amino acid peptide that is octanoylated (C8:0) at $ Ser^{3} $ and lacks $ Gln^{14} $, which is present in rat and human ghrelin. Additionally, we identified various acyl modifications in caprine ghrelin: nonanoic (C9:0), decanoic (10:0), unsaturated octanoic acids (C8:1), and an unidentified fatty acid modification. We observed that differences in acyl modifications affected GHS-R1a activation. In addition, administration of synthetic bovine ghrelin increased plasma growth hormone (GH) levels in goats. Thus, the present study indicates a structural divergence in caprine ghrelin and suggests that ghrelin is involved in GH release in ruminants. |
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Purification and Characterization of Caprine Ghrelin and Its Effect on Growth Hormone Release |
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Miyazato, Mikiya Lin, Xing-Zi Kaiya, Hiroyuki Sato, Takahiro Nakahara, Keiko Murakami, Noboru Kangawa, Kenji Kojima, Masayasu |
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| score |
7.398037 |