Ghrelin acylation and metabolic control
► Ghrelin acylation depends on the function of GOAT and the availability of substrates. ► GOAT plays a distinct role in the regulation of energy and glucose homeostasis. ► GOAT may function as a modifier for the adaptive response to feeding and fasting. ► GOAT inhibition is a promising therapeutic t...
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| Veröffentlicht in: | Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2011-11, Vol.32 (11), p.2301-2308 |
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| creator | Al Massadi, O. Tschöp, M.H. Tong, J. |
| description | ► Ghrelin acylation depends on the function of GOAT and the availability of substrates. ► GOAT plays a distinct role in the regulation of energy and glucose homeostasis. ► GOAT may function as a modifier for the adaptive response to feeding and fasting. ► GOAT inhibition is a promising therapeutic target for weight and glucose control.
Since its discovery, many physiologic functions have been ascribed to ghrelin, a gut derived hormone. The presence of a median fatty acid side chain on the ghrelin peptide is required for the binding and activation of the classical ghrelin receptor, the growth hormone secretagogue receptor (GHSR)-1a. Ghrelin O-acyl transferase (GOAT) was recently discovered as the enzyme responsible for this acylation process. GOAT is expressed in all tissues that have been found to express ghrelin and has demonstrated actions on several complex endocrine organ systems such as the hypothalamus–pituitary–gonadal, insular and adrenal axis as well as the gastrointestinal (GI) tract, bone and gustatory system. Ghrelin acylation is dependent on the function of GOAT and the availability of substrates such as proghrelin and short- to medium-chain fatty acids (MCFAs). This process is governed by GOAT activity and has been shown to be modified by dietary lipids. In this review, we provided evidence that support an important role of GOAT in the regulation of energy homeostasis and glucose metabolism by modulating acyl ghrelin (AG) production. The relevance of GOAT and AG during periods of starvation remains to be defined. In addition, we summarized the recent literature on the metabolic effects of GOAT specific inhibitors and shared our view on the potential of targeting GOAT for the treatment of metabolic disorders such as obesity and type 2 diabetes. |
| doi_str_mv | 10.1016/j.peptides.2011.08.020 |
| format | Article |
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Since its discovery, many physiologic functions have been ascribed to ghrelin, a gut derived hormone. The presence of a median fatty acid side chain on the ghrelin peptide is required for the binding and activation of the classical ghrelin receptor, the growth hormone secretagogue receptor (GHSR)-1a. Ghrelin O-acyl transferase (GOAT) was recently discovered as the enzyme responsible for this acylation process. GOAT is expressed in all tissues that have been found to express ghrelin and has demonstrated actions on several complex endocrine organ systems such as the hypothalamus–pituitary–gonadal, insular and adrenal axis as well as the gastrointestinal (GI) tract, bone and gustatory system. Ghrelin acylation is dependent on the function of GOAT and the availability of substrates such as proghrelin and short- to medium-chain fatty acids (MCFAs). This process is governed by GOAT activity and has been shown to be modified by dietary lipids. In this review, we provided evidence that support an important role of GOAT in the regulation of energy homeostasis and glucose metabolism by modulating acyl ghrelin (AG) production. The relevance of GOAT and AG during periods of starvation remains to be defined. In addition, we summarized the recent literature on the metabolic effects of GOAT specific inhibitors and shared our view on the potential of targeting GOAT for the treatment of metabolic disorders such as obesity and type 2 diabetes.</description><identifier>ISSN: 0196-9781</identifier><identifier>EISSN: 1873-5169</identifier><identifier>DOI: 10.1016/j.peptides.2011.08.020</identifier><identifier>PMID: 21893140</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Activation ; Acyl ghrelin ; Acylation ; Acyltransferases - antagonists & inhibitors ; Acyltransferases - metabolism ; Animals ; Appetite Regulation - drug effects ; Appetite Regulation - physiology ; Blood Glucose - metabolism ; Body Weight ; Diabetes Mellitus, Type 2 - drug therapy ; Diabetes Mellitus, Type 2 - metabolism ; dietary fat ; energy ; Energy Metabolism - drug effects ; Energy Metabolism - physiology ; Enzyme Inhibitors - pharmacology ; Enzyme Inhibitors - therapeutic use ; Enzymes ; Fatty acids ; Fatty Acids - metabolism ; gastrointestinal system ; Gene Expression ; ghrelin ; Ghrelin - genetics ; Ghrelin - metabolism ; ghrelin receptors ; glucose ; GOAT ; Goats ; homeostasis ; Humans ; Inhibitors ; Insulin-Like Growth Factor I - genetics ; Insulin-Like Growth Factor I - metabolism ; MCFAs ; medium chain fatty acids ; Metabolism ; Mice ; Mice, Knockout ; noninsulin-dependent diabetes mellitus ; obesity ; Obesity - drug therapy ; Obesity - metabolism ; Peptides ; Peptides - pharmacology ; Peptides - therapeutic use ; Receptors ; Receptors, Ghrelin - genetics ; Receptors, Ghrelin - metabolism ; Signal Transduction ; starvation ; Stomach - metabolism ; tissues</subject><ispartof>Peptides (New York, N.Y. : 1980), 2011-11, Vol.32 (11), p.2301-2308</ispartof><rights>2011 Elsevier Inc.</rights><rights>Copyright © 2011 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c456t-70be19e8ec34ad87d2017a0837127c632ae23a0eb3ee5ed275fbae47fd9341ce3</citedby><cites>FETCH-LOGICAL-c456t-70be19e8ec34ad87d2017a0837127c632ae23a0eb3ee5ed275fbae47fd9341ce3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.peptides.2011.08.020$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,778,782,3539,27913,27914,45984</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21893140$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Al Massadi, O.</creatorcontrib><creatorcontrib>Tschöp, M.H.</creatorcontrib><creatorcontrib>Tong, J.</creatorcontrib><title>Ghrelin acylation and metabolic control</title><title>Peptides (New York, N.Y. : 1980)</title><addtitle>Peptides</addtitle><description>► Ghrelin acylation depends on the function of GOAT and the availability of substrates. ► GOAT plays a distinct role in the regulation of energy and glucose homeostasis. ► GOAT may function as a modifier for the adaptive response to feeding and fasting. ► GOAT inhibition is a promising therapeutic target for weight and glucose control.
Since its discovery, many physiologic functions have been ascribed to ghrelin, a gut derived hormone. The presence of a median fatty acid side chain on the ghrelin peptide is required for the binding and activation of the classical ghrelin receptor, the growth hormone secretagogue receptor (GHSR)-1a. Ghrelin O-acyl transferase (GOAT) was recently discovered as the enzyme responsible for this acylation process. GOAT is expressed in all tissues that have been found to express ghrelin and has demonstrated actions on several complex endocrine organ systems such as the hypothalamus–pituitary–gonadal, insular and adrenal axis as well as the gastrointestinal (GI) tract, bone and gustatory system. Ghrelin acylation is dependent on the function of GOAT and the availability of substrates such as proghrelin and short- to medium-chain fatty acids (MCFAs). This process is governed by GOAT activity and has been shown to be modified by dietary lipids. In this review, we provided evidence that support an important role of GOAT in the regulation of energy homeostasis and glucose metabolism by modulating acyl ghrelin (AG) production. The relevance of GOAT and AG during periods of starvation remains to be defined. In addition, we summarized the recent literature on the metabolic effects of GOAT specific inhibitors and shared our view on the potential of targeting GOAT for the treatment of metabolic disorders such as obesity and type 2 diabetes.</description><subject>Activation</subject><subject>Acyl ghrelin</subject><subject>Acylation</subject><subject>Acyltransferases - antagonists & inhibitors</subject><subject>Acyltransferases - metabolism</subject><subject>Animals</subject><subject>Appetite Regulation - drug effects</subject><subject>Appetite Regulation - physiology</subject><subject>Blood Glucose - metabolism</subject><subject>Body Weight</subject><subject>Diabetes Mellitus, Type 2 - drug therapy</subject><subject>Diabetes Mellitus, Type 2 - metabolism</subject><subject>dietary fat</subject><subject>energy</subject><subject>Energy Metabolism - drug effects</subject><subject>Energy Metabolism - physiology</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Enzyme Inhibitors - therapeutic use</subject><subject>Enzymes</subject><subject>Fatty acids</subject><subject>Fatty Acids - metabolism</subject><subject>gastrointestinal system</subject><subject>Gene Expression</subject><subject>ghrelin</subject><subject>Ghrelin - genetics</subject><subject>Ghrelin - metabolism</subject><subject>ghrelin receptors</subject><subject>glucose</subject><subject>GOAT</subject><subject>Goats</subject><subject>homeostasis</subject><subject>Humans</subject><subject>Inhibitors</subject><subject>Insulin-Like Growth Factor I - genetics</subject><subject>Insulin-Like Growth Factor I - metabolism</subject><subject>MCFAs</subject><subject>medium chain fatty acids</subject><subject>Metabolism</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>noninsulin-dependent diabetes mellitus</subject><subject>obesity</subject><subject>Obesity - drug therapy</subject><subject>Obesity - metabolism</subject><subject>Peptides</subject><subject>Peptides - pharmacology</subject><subject>Peptides - therapeutic use</subject><subject>Receptors</subject><subject>Receptors, Ghrelin - genetics</subject><subject>Receptors, Ghrelin - metabolism</subject><subject>Signal Transduction</subject><subject>starvation</subject><subject>Stomach - metabolism</subject><subject>tissues</subject><issn>0196-9781</issn><issn>1873-5169</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1vFDEMhiMEotuWv1D2Vi4ztZOZfNxAFbRIlTjQnqNM4oGsZidLMovUf9-stuVIT_bhsf3qMWMXCC0CyqtNu6PdEgOVlgNiC7oFDm_YCrUSTY_SvGUrQCMbozSesNNSNgDQdUa_ZycctRHYwYpd3vzONMV57fzj5JaYajeH9ZYWN6Qp-rVP85LTdM7ejW4q9OG5nrGHb1_vr2-bux8336-_3DW-6-XSKBgIDWnyonNBq1DDKQdaKOTKS8EdceGABkHUU-CqHwdHnRqDER16Emfs8rh3l9OfPZXFbmPxNE1uprQv1kihtem5fp2EXmrB4UB--i-JSnLkvZRYUXlEfU6lZBrtLsety48WwR7E2419EW8P4i1oW8XXwYvnG_thS-Hf2IvpCnw8AqNL1v3KsdiHn3WDrF8RUJNW4vORoOr3b6Rsi480ewoxk19sSPG1FE-GA59J</recordid><startdate>20111101</startdate><enddate>20111101</enddate><creator>Al Massadi, O.</creator><creator>Tschöp, M.H.</creator><creator>Tong, J.</creator><general>Elsevier Inc</general><scope>FBQ</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>7U5</scope><scope>8FD</scope><scope>L7M</scope><scope>7X8</scope></search><sort><creationdate>20111101</creationdate><title>Ghrelin acylation and metabolic control</title><author>Al Massadi, O. ; Tschöp, M.H. ; Tong, J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c456t-70be19e8ec34ad87d2017a0837127c632ae23a0eb3ee5ed275fbae47fd9341ce3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Activation</topic><topic>Acyl ghrelin</topic><topic>Acylation</topic><topic>Acyltransferases - antagonists & inhibitors</topic><topic>Acyltransferases - metabolism</topic><topic>Animals</topic><topic>Appetite Regulation - drug effects</topic><topic>Appetite Regulation - physiology</topic><topic>Blood Glucose - metabolism</topic><topic>Body Weight</topic><topic>Diabetes Mellitus, Type 2 - drug therapy</topic><topic>Diabetes Mellitus, Type 2 - metabolism</topic><topic>dietary fat</topic><topic>energy</topic><topic>Energy Metabolism - drug effects</topic><topic>Energy Metabolism - physiology</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Enzyme Inhibitors - therapeutic use</topic><topic>Enzymes</topic><topic>Fatty acids</topic><topic>Fatty Acids - metabolism</topic><topic>gastrointestinal system</topic><topic>Gene Expression</topic><topic>ghrelin</topic><topic>Ghrelin - genetics</topic><topic>Ghrelin - metabolism</topic><topic>ghrelin receptors</topic><topic>glucose</topic><topic>GOAT</topic><topic>Goats</topic><topic>homeostasis</topic><topic>Humans</topic><topic>Inhibitors</topic><topic>Insulin-Like Growth Factor I - genetics</topic><topic>Insulin-Like Growth Factor I - metabolism</topic><topic>MCFAs</topic><topic>medium chain fatty acids</topic><topic>Metabolism</topic><topic>Mice</topic><topic>Mice, Knockout</topic><topic>noninsulin-dependent diabetes mellitus</topic><topic>obesity</topic><topic>Obesity - drug therapy</topic><topic>Obesity - metabolism</topic><topic>Peptides</topic><topic>Peptides - pharmacology</topic><topic>Peptides - therapeutic use</topic><topic>Receptors</topic><topic>Receptors, Ghrelin - genetics</topic><topic>Receptors, Ghrelin - metabolism</topic><topic>Signal Transduction</topic><topic>starvation</topic><topic>Stomach - metabolism</topic><topic>tissues</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Al Massadi, O.</creatorcontrib><creatorcontrib>Tschöp, M.H.</creatorcontrib><creatorcontrib>Tong, J.</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><jtitle>Peptides (New York, N.Y. : 1980)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Al Massadi, O.</au><au>Tschöp, M.H.</au><au>Tong, J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ghrelin acylation and metabolic control</atitle><jtitle>Peptides (New York, N.Y. : 1980)</jtitle><addtitle>Peptides</addtitle><date>2011-11-01</date><risdate>2011</risdate><volume>32</volume><issue>11</issue><spage>2301</spage><epage>2308</epage><pages>2301-2308</pages><issn>0196-9781</issn><eissn>1873-5169</eissn><abstract>► Ghrelin acylation depends on the function of GOAT and the availability of substrates. ► GOAT plays a distinct role in the regulation of energy and glucose homeostasis. ► GOAT may function as a modifier for the adaptive response to feeding and fasting. ► GOAT inhibition is a promising therapeutic target for weight and glucose control.
Since its discovery, many physiologic functions have been ascribed to ghrelin, a gut derived hormone. The presence of a median fatty acid side chain on the ghrelin peptide is required for the binding and activation of the classical ghrelin receptor, the growth hormone secretagogue receptor (GHSR)-1a. Ghrelin O-acyl transferase (GOAT) was recently discovered as the enzyme responsible for this acylation process. GOAT is expressed in all tissues that have been found to express ghrelin and has demonstrated actions on several complex endocrine organ systems such as the hypothalamus–pituitary–gonadal, insular and adrenal axis as well as the gastrointestinal (GI) tract, bone and gustatory system. Ghrelin acylation is dependent on the function of GOAT and the availability of substrates such as proghrelin and short- to medium-chain fatty acids (MCFAs). This process is governed by GOAT activity and has been shown to be modified by dietary lipids. In this review, we provided evidence that support an important role of GOAT in the regulation of energy homeostasis and glucose metabolism by modulating acyl ghrelin (AG) production. The relevance of GOAT and AG during periods of starvation remains to be defined. In addition, we summarized the recent literature on the metabolic effects of GOAT specific inhibitors and shared our view on the potential of targeting GOAT for the treatment of metabolic disorders such as obesity and type 2 diabetes.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>21893140</pmid><doi>10.1016/j.peptides.2011.08.020</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0196-9781 |
| ispartof | Peptides (New York, N.Y. : 1980), 2011-11, Vol.32 (11), p.2301-2308 |
| issn | 0196-9781 1873-5169 |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Activation Acyl ghrelin Acylation Acyltransferases - antagonists & inhibitors Acyltransferases - metabolism Animals Appetite Regulation - drug effects Appetite Regulation - physiology Blood Glucose - metabolism Body Weight Diabetes Mellitus, Type 2 - drug therapy Diabetes Mellitus, Type 2 - metabolism dietary fat energy Energy Metabolism - drug effects Energy Metabolism - physiology Enzyme Inhibitors - pharmacology Enzyme Inhibitors - therapeutic use Enzymes Fatty acids Fatty Acids - metabolism gastrointestinal system Gene Expression ghrelin Ghrelin - genetics Ghrelin - metabolism ghrelin receptors glucose GOAT Goats homeostasis Humans Inhibitors Insulin-Like Growth Factor I - genetics Insulin-Like Growth Factor I - metabolism MCFAs medium chain fatty acids Metabolism Mice Mice, Knockout noninsulin-dependent diabetes mellitus obesity Obesity - drug therapy Obesity - metabolism Peptides Peptides - pharmacology Peptides - therapeutic use Receptors Receptors, Ghrelin - genetics Receptors, Ghrelin - metabolism Signal Transduction starvation Stomach - metabolism tissues |
| title | Ghrelin acylation and metabolic control |
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