Acylation Type Determines Ghrelin's Effects on Energy Homeostasis in Rodents
Ghrelin is a gastrointestinal polypeptide that acts through the ghrelin receptor (GHSR) to promote food intake and increase adiposity. Activation of GHSR requires the presence of a fatty-acid (FA) side chain on amino acid residue serine 3 of the ghrelin molecule. However, little is known about the r...
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| Veröffentlicht in: | Endocrinology (Philadelphia) 2012-10, Vol.153 (10), p.4687-4695 |
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| creator | Heppner, Kristy M Chaudhary, Nilika Müller, Timo D Kirchner, Henriette Habegger, Kirk M Ottaway, Nickki Smiley, David L DiMarchi, Richard Hofmann, Susanna M Woods, Stephen C Sivertsen, Bjørn Holst, Birgitte Pfluger, Paul T Perez-Tilve, Diego Tschöp, Matthias H |
| description | Ghrelin is a gastrointestinal polypeptide that acts through the ghrelin receptor (GHSR) to promote food intake and increase adiposity. Activation of GHSR requires the presence of a fatty-acid (FA) side chain on amino acid residue serine 3 of the ghrelin molecule. However, little is known about the role that the type of FA used for acylation plays in the biological action of ghrelin. We therefore evaluated a series of differentially acylated peptides to determine whether alterations in length or stability of the FA side chain have an impact on the ability of ghrelin to activate GHSR in vitro or to differentially alter food intake, body weight, and body composition in vivo. Fatty acids principally available in the diet (such as palmitate C16) and therefore representing potential substrates for the ghrelin-activating enzyme ghrelin O-acyltransferase (GOAT) were used for dose-, time-, and administration/route-dependent effects of ghrelin on food intake, body weight, and body composition in rats and mice. Our data demonstrate that altering the length of the FA side chain of ghrelin results in the differential activation of GHSR. Additionally, we found that acylation of ghrelin with a long-chain FA (C16) delays the acute central stimulation of food intake. Lastly, we found that, depending on acylation length, systemic and central chronic actions of ghrelin on adiposity can be enhanced or reduced. Together our data suggest that modification of the FA side-chain length can be a novel approach to modulate the efficacy of pharmacologically administered ghrelin. |
| doi_str_mv | 10.1210/en.2012-1194 |
| format | Article |
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Activation of GHSR requires the presence of a fatty-acid (FA) side chain on amino acid residue serine 3 of the ghrelin molecule. However, little is known about the role that the type of FA used for acylation plays in the biological action of ghrelin. We therefore evaluated a series of differentially acylated peptides to determine whether alterations in length or stability of the FA side chain have an impact on the ability of ghrelin to activate GHSR in vitro or to differentially alter food intake, body weight, and body composition in vivo. Fatty acids principally available in the diet (such as palmitate C16) and therefore representing potential substrates for the ghrelin-activating enzyme ghrelin O-acyltransferase (GOAT) were used for dose-, time-, and administration/route-dependent effects of ghrelin on food intake, body weight, and body composition in rats and mice. Our data demonstrate that altering the length of the FA side chain of ghrelin results in the differential activation of GHSR. Additionally, we found that acylation of ghrelin with a long-chain FA (C16) delays the acute central stimulation of food intake. Lastly, we found that, depending on acylation length, systemic and central chronic actions of ghrelin on adiposity can be enhanced or reduced. Together our data suggest that modification of the FA side-chain length can be a novel approach to modulate the efficacy of pharmacologically administered ghrelin.</description><identifier>ISSN: 0013-7227</identifier><identifier>EISSN: 1945-7170</identifier><identifier>DOI: 10.1210/en.2012-1194</identifier><identifier>PMID: 22865372</identifier><identifier>CODEN: ENDOAO</identifier><language>eng</language><publisher>Chevy Chase, MD: Endocrine Society</publisher><subject>Acylation ; Adipose tissue ; Amino acid composition ; Amino acids ; Animals ; Biological and medical sciences ; Body composition ; Body Composition - drug effects ; Body weight ; Body Weight - drug effects ; Eating - drug effects ; Energy balance ; Energy Balance-Obesity ; Energy Metabolism - drug effects ; Fatty acids ; Food ; Food availability ; Food chains ; Food composition ; Food intake ; Fundamental and applied biological sciences. Psychology ; Ghrelin ; Ghrelin - metabolism ; Ghrelin - pharmacology ; Homeostasis ; Homeostasis - drug effects ; In vivo methods and tests ; Male ; Mice ; Mice, Inbred C57BL ; Palmitic acid ; Peptides ; Polypeptides ; Protein Isoforms - metabolism ; Protein Isoforms - pharmacology ; Rats ; Rats, Long-Evans ; Receptors, Ghrelin - genetics ; Receptors, Ghrelin - metabolism ; Vertebrates: endocrinology</subject><ispartof>Endocrinology (Philadelphia), 2012-10, Vol.153 (10), p.4687-4695</ispartof><rights>Copyright © 2012 by The Endocrine Society</rights><rights>Copyright © 2012 by The Endocrine Society 2012</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c622t-9e6008167cb4a3e1f8d43faf71d83accecc8e31e48cf10e4192b1f2c6bf420443</citedby><cites>FETCH-LOGICAL-c622t-9e6008167cb4a3e1f8d43faf71d83accecc8e31e48cf10e4192b1f2c6bf420443</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,550,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=26398912$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22865372$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttp://kipublications.ki.se/Default.aspx?queryparsed=id:125307451$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Heppner, Kristy M</creatorcontrib><creatorcontrib>Chaudhary, Nilika</creatorcontrib><creatorcontrib>Müller, Timo D</creatorcontrib><creatorcontrib>Kirchner, Henriette</creatorcontrib><creatorcontrib>Habegger, Kirk M</creatorcontrib><creatorcontrib>Ottaway, Nickki</creatorcontrib><creatorcontrib>Smiley, David L</creatorcontrib><creatorcontrib>DiMarchi, Richard</creatorcontrib><creatorcontrib>Hofmann, Susanna M</creatorcontrib><creatorcontrib>Woods, Stephen C</creatorcontrib><creatorcontrib>Sivertsen, Bjørn</creatorcontrib><creatorcontrib>Holst, Birgitte</creatorcontrib><creatorcontrib>Pfluger, Paul T</creatorcontrib><creatorcontrib>Perez-Tilve, Diego</creatorcontrib><creatorcontrib>Tschöp, Matthias H</creatorcontrib><title>Acylation Type Determines Ghrelin's Effects on Energy Homeostasis in Rodents</title><title>Endocrinology (Philadelphia)</title><addtitle>Endocrinology</addtitle><description>Ghrelin is a gastrointestinal polypeptide that acts through the ghrelin receptor (GHSR) to promote food intake and increase adiposity. Activation of GHSR requires the presence of a fatty-acid (FA) side chain on amino acid residue serine 3 of the ghrelin molecule. However, little is known about the role that the type of FA used for acylation plays in the biological action of ghrelin. We therefore evaluated a series of differentially acylated peptides to determine whether alterations in length or stability of the FA side chain have an impact on the ability of ghrelin to activate GHSR in vitro or to differentially alter food intake, body weight, and body composition in vivo. Fatty acids principally available in the diet (such as palmitate C16) and therefore representing potential substrates for the ghrelin-activating enzyme ghrelin O-acyltransferase (GOAT) were used for dose-, time-, and administration/route-dependent effects of ghrelin on food intake, body weight, and body composition in rats and mice. Our data demonstrate that altering the length of the FA side chain of ghrelin results in the differential activation of GHSR. Additionally, we found that acylation of ghrelin with a long-chain FA (C16) delays the acute central stimulation of food intake. Lastly, we found that, depending on acylation length, systemic and central chronic actions of ghrelin on adiposity can be enhanced or reduced. Together our data suggest that modification of the FA side-chain length can be a novel approach to modulate the efficacy of pharmacologically administered ghrelin.</description><subject>Acylation</subject><subject>Adipose tissue</subject><subject>Amino acid composition</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Body composition</subject><subject>Body Composition - drug effects</subject><subject>Body weight</subject><subject>Body Weight - drug effects</subject><subject>Eating - drug effects</subject><subject>Energy balance</subject><subject>Energy Balance-Obesity</subject><subject>Energy Metabolism - drug effects</subject><subject>Fatty acids</subject><subject>Food</subject><subject>Food availability</subject><subject>Food chains</subject><subject>Food composition</subject><subject>Food intake</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Ghrelin</subject><subject>Ghrelin - metabolism</subject><subject>Ghrelin - pharmacology</subject><subject>Homeostasis</subject><subject>Homeostasis - drug effects</subject><subject>In vivo methods and tests</subject><subject>Male</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Palmitic acid</subject><subject>Peptides</subject><subject>Polypeptides</subject><subject>Protein Isoforms - metabolism</subject><subject>Protein Isoforms - pharmacology</subject><subject>Rats</subject><subject>Rats, Long-Evans</subject><subject>Receptors, Ghrelin - genetics</subject><subject>Receptors, Ghrelin - metabolism</subject><subject>Vertebrates: endocrinology</subject><issn>0013-7227</issn><issn>1945-7170</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>D8T</sourceid><recordid>eNp1kk1v1DAQhiMEotvCjTOKhFA5kOKxnTi5IFVlaZFWQkLlbHmdceuS2Fs7Ae2_r6OEliK4-GsevzPj11n2CsgJUCAf0J1QArQAaPiTbJXGshAgyNNsRQiwQlAqDrLDGG_SlnPOnmcHlNZVyQRdZZtTve_UYL3LL_c7zD_hgKG3DmN-fh2ws-445mtjUA8xT9DaYbja5xe-Rx8HFW3Mrcu_-RbdEF9kz4zqIr5c5qPs--f15dlFsfl6_uXsdFPoitKhaLAipIZK6C1XDMHULWdGGQFtzZTWqHWNDJDX2gBBDg3dgqG62hpOSergKCtm3fgLd-NW7oLtVdhLr6xcjn6kFcqSlZzXif848ynSY6tTrUF1j649jjh7La_8T8lKoITSJPBuEQj-dsQ4yN5GjV2nHPoxSiCCi0rUYkLf_IXe-DG49BySASMVJUSQRL2fKR18jAHNfTFA5GSrRCcnW-Vka8Jf_9nAPfzbxwS8XQAVtepMUE7b-MBVrKkbmLjjmfPj7n8piyUlm0l0rdch_YhdwBgfuvlnoXc_Lcgc</recordid><startdate>20121001</startdate><enddate>20121001</enddate><creator>Heppner, Kristy M</creator><creator>Chaudhary, Nilika</creator><creator>Müller, Timo D</creator><creator>Kirchner, Henriette</creator><creator>Habegger, Kirk M</creator><creator>Ottaway, Nickki</creator><creator>Smiley, David L</creator><creator>DiMarchi, Richard</creator><creator>Hofmann, Susanna M</creator><creator>Woods, Stephen C</creator><creator>Sivertsen, Bjørn</creator><creator>Holst, Birgitte</creator><creator>Pfluger, Paul T</creator><creator>Perez-Tilve, Diego</creator><creator>Tschöp, Matthias H</creator><general>Endocrine Society</general><general>Oxford University Press</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TM</scope><scope>7TO</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope><scope>ADTPV</scope><scope>AOWAS</scope><scope>D8T</scope><scope>ZZAVC</scope></search><sort><creationdate>20121001</creationdate><title>Acylation Type Determines Ghrelin's Effects on Energy Homeostasis in Rodents</title><author>Heppner, Kristy M ; Chaudhary, Nilika ; Müller, Timo D ; Kirchner, Henriette ; Habegger, Kirk M ; Ottaway, Nickki ; Smiley, David L ; DiMarchi, Richard ; Hofmann, Susanna M ; Woods, Stephen C ; Sivertsen, Bjørn ; Holst, Birgitte ; Pfluger, Paul T ; Perez-Tilve, Diego ; Tschöp, Matthias H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c622t-9e6008167cb4a3e1f8d43faf71d83accecc8e31e48cf10e4192b1f2c6bf420443</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Acylation</topic><topic>Adipose tissue</topic><topic>Amino acid composition</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Body composition</topic><topic>Body Composition - drug effects</topic><topic>Body weight</topic><topic>Body Weight - drug effects</topic><topic>Eating - drug effects</topic><topic>Energy balance</topic><topic>Energy Balance-Obesity</topic><topic>Energy Metabolism - drug effects</topic><topic>Fatty acids</topic><topic>Food</topic><topic>Food availability</topic><topic>Food chains</topic><topic>Food composition</topic><topic>Food intake</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Ghrelin</topic><topic>Ghrelin - metabolism</topic><topic>Ghrelin - pharmacology</topic><topic>Homeostasis</topic><topic>Homeostasis - drug effects</topic><topic>In vivo methods and tests</topic><topic>Male</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Palmitic acid</topic><topic>Peptides</topic><topic>Polypeptides</topic><topic>Protein Isoforms - metabolism</topic><topic>Protein Isoforms - pharmacology</topic><topic>Rats</topic><topic>Rats, Long-Evans</topic><topic>Receptors, Ghrelin - genetics</topic><topic>Receptors, Ghrelin - metabolism</topic><topic>Vertebrates: endocrinology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Heppner, Kristy M</creatorcontrib><creatorcontrib>Chaudhary, Nilika</creatorcontrib><creatorcontrib>Müller, Timo D</creatorcontrib><creatorcontrib>Kirchner, Henriette</creatorcontrib><creatorcontrib>Habegger, Kirk M</creatorcontrib><creatorcontrib>Ottaway, Nickki</creatorcontrib><creatorcontrib>Smiley, David L</creatorcontrib><creatorcontrib>DiMarchi, Richard</creatorcontrib><creatorcontrib>Hofmann, Susanna M</creatorcontrib><creatorcontrib>Woods, Stephen C</creatorcontrib><creatorcontrib>Sivertsen, Bjørn</creatorcontrib><creatorcontrib>Holst, Birgitte</creatorcontrib><creatorcontrib>Pfluger, Paul T</creatorcontrib><creatorcontrib>Perez-Tilve, Diego</creatorcontrib><creatorcontrib>Tschöp, Matthias H</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>SwePub</collection><collection>SwePub Articles</collection><collection>SWEPUB Freely available online</collection><collection>SwePub Articles full text</collection><jtitle>Endocrinology (Philadelphia)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Heppner, Kristy M</au><au>Chaudhary, Nilika</au><au>Müller, Timo D</au><au>Kirchner, Henriette</au><au>Habegger, Kirk M</au><au>Ottaway, Nickki</au><au>Smiley, David L</au><au>DiMarchi, Richard</au><au>Hofmann, Susanna M</au><au>Woods, Stephen C</au><au>Sivertsen, Bjørn</au><au>Holst, Birgitte</au><au>Pfluger, Paul T</au><au>Perez-Tilve, Diego</au><au>Tschöp, Matthias H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Acylation Type Determines Ghrelin's Effects on Energy Homeostasis in Rodents</atitle><jtitle>Endocrinology (Philadelphia)</jtitle><addtitle>Endocrinology</addtitle><date>2012-10-01</date><risdate>2012</risdate><volume>153</volume><issue>10</issue><spage>4687</spage><epage>4695</epage><pages>4687-4695</pages><issn>0013-7227</issn><eissn>1945-7170</eissn><coden>ENDOAO</coden><abstract>Ghrelin is a gastrointestinal polypeptide that acts through the ghrelin receptor (GHSR) to promote food intake and increase adiposity. Activation of GHSR requires the presence of a fatty-acid (FA) side chain on amino acid residue serine 3 of the ghrelin molecule. However, little is known about the role that the type of FA used for acylation plays in the biological action of ghrelin. We therefore evaluated a series of differentially acylated peptides to determine whether alterations in length or stability of the FA side chain have an impact on the ability of ghrelin to activate GHSR in vitro or to differentially alter food intake, body weight, and body composition in vivo. Fatty acids principally available in the diet (such as palmitate C16) and therefore representing potential substrates for the ghrelin-activating enzyme ghrelin O-acyltransferase (GOAT) were used for dose-, time-, and administration/route-dependent effects of ghrelin on food intake, body weight, and body composition in rats and mice. Our data demonstrate that altering the length of the FA side chain of ghrelin results in the differential activation of GHSR. Additionally, we found that acylation of ghrelin with a long-chain FA (C16) delays the acute central stimulation of food intake. Lastly, we found that, depending on acylation length, systemic and central chronic actions of ghrelin on adiposity can be enhanced or reduced. Together our data suggest that modification of the FA side-chain length can be a novel approach to modulate the efficacy of pharmacologically administered ghrelin.</abstract><cop>Chevy Chase, MD</cop><pub>Endocrine Society</pub><pmid>22865372</pmid><doi>10.1210/en.2012-1194</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | Endocrinology (Philadelphia), 2012-10, Vol.153 (10), p.4687-4695 |
| issn | 0013-7227 1945-7170 |
| language | eng |
| recordid | cdi_swepub_primary_oai_swepub_ki_se_535448 |
| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection; SWEPUB Freely available online; Journals@Ovid Complete |
| subjects | Acylation Adipose tissue Amino acid composition Amino acids Animals Biological and medical sciences Body composition Body Composition - drug effects Body weight Body Weight - drug effects Eating - drug effects Energy balance Energy Balance-Obesity Energy Metabolism - drug effects Fatty acids Food Food availability Food chains Food composition Food intake Fundamental and applied biological sciences. Psychology Ghrelin Ghrelin - metabolism Ghrelin - pharmacology Homeostasis Homeostasis - drug effects In vivo methods and tests Male Mice Mice, Inbred C57BL Palmitic acid Peptides Polypeptides Protein Isoforms - metabolism Protein Isoforms - pharmacology Rats Rats, Long-Evans Receptors, Ghrelin - genetics Receptors, Ghrelin - metabolism Vertebrates: endocrinology |
| title | Acylation Type Determines Ghrelin's Effects on Energy Homeostasis in Rodents |
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