A Family of Acrp30/Adiponectin Structural and Functional Paralogs
Biochemical, genetic, and animal studies in recent years have established a critical role for the adipokine Acrp30/adiponectin in controlling whole-body metabolism, particularly by enhancing insulin sensitivity in muscle and liver, and by increasing fatty acid oxidation in muscle. We describe a wide...
Gespeichert in:
| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2004-07, Vol.101 (28), p.10302-10307 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 10307 |
|---|---|
| container_issue | 28 |
| container_start_page | 10302 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 101 |
| creator | Wong, Guang W. Wang, Jin Hug, Christopher Tsao, Tsu-Shuen Lodish, Harvey F. |
| description | Biochemical, genetic, and animal studies in recent years have established a critical role for the adipokine Acrp30/adiponectin in controlling whole-body metabolism, particularly by enhancing insulin sensitivity in muscle and liver, and by increasing fatty acid oxidation in muscle. We describe a widely expressed and highly conserved family of adiponectin paralogs designated as C1q/tumor necrosis factor-α-related proteins (CTRPs) 1-7. In the present study, we focus on mCTRP2, the mouse paralog most similar to adiponectin. At nanomolar concentrations, bacterially produced mCTRP2 rapidly induced phosphorylation of AMP-activated protein kinase, acetyl-CoA carboxylase, and mitogen-activated protein kinase in C2C12 myotubes, which resulted in increased glycogen accumulation and fatty acid oxidation. The discovery of a family of adiponectin paralogs has implications for understanding the control of energy homeostasis and could provide new targets for pharmacologic intervention in metabolic diseases such as diabetes and obesity. |
| doi_str_mv | 10.1073/pnas.0403760101 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_66704281</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>3372886</jstor_id><sourcerecordid>3372886</sourcerecordid><originalsourceid>FETCH-LOGICAL-c638t-49aefd0e7cdf9dea419bf5ca03e0a0bfa69c5cc0a143078f55316a07a5716ba83</originalsourceid><addsrcrecordid>eNqF0c1rFDEUAPAgit1Wz15EBg8FD9N9-Zh8HHoYiqtCQUE9h2wmqbPMJmMyI_a_N8MuXfXS0yMvv_d4yUPoFYYrDIKux2DyFTCgggMG_AStMChcc6bgKVoBEFFLRtgZOs95BwCqkfAcneGGUKwUW6G2rTZm3w_3VfRVa9NIYd12_RiDs1Mfqq9Tmu00JzNUJnTVZg4lHUM5fjElGe_yC_TMmyG7l8d4gb5v3n-7-Vjffv7w6aa9rS2ncqqZMs534ITtvOqcYVhtfWMNUAcGtt5wZRtrwWBGQUjfNBRzA8I0AvOtkfQCXR_6jvN27zrrwlQG0GPq9ybd62h6_e9N6H_ou_hLMyEbLkr95bE-xZ-zy5Pe99m6YTDBxTlrzgUwIvGjkICkBOMFvv0P7uKcyt8sBlOqFCcFrQ_Ipphzcv5hYgx62aFedqhPOywVb_5-6Mkfl1bAuyNYKk_tsCayBApE-3kYJvd7KrZ6xBby-kB2eYrpwVAqiJSc_gGk4Lmb</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>201339962</pqid></control><display><type>article</type><title>A Family of Acrp30/Adiponectin Structural and Functional Paralogs</title><source>MEDLINE</source><source>Jstor Complete Legacy</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Wong, Guang W. ; Wang, Jin ; Hug, Christopher ; Tsao, Tsu-Shuen ; Lodish, Harvey F.</creator><creatorcontrib>Wong, Guang W. ; Wang, Jin ; Hug, Christopher ; Tsao, Tsu-Shuen ; Lodish, Harvey F.</creatorcontrib><description>Biochemical, genetic, and animal studies in recent years have established a critical role for the adipokine Acrp30/adiponectin in controlling whole-body metabolism, particularly by enhancing insulin sensitivity in muscle and liver, and by increasing fatty acid oxidation in muscle. We describe a widely expressed and highly conserved family of adiponectin paralogs designated as C1q/tumor necrosis factor-α-related proteins (CTRPs) 1-7. In the present study, we focus on mCTRP2, the mouse paralog most similar to adiponectin. At nanomolar concentrations, bacterially produced mCTRP2 rapidly induced phosphorylation of AMP-activated protein kinase, acetyl-CoA carboxylase, and mitogen-activated protein kinase in C2C12 myotubes, which resulted in increased glycogen accumulation and fatty acid oxidation. The discovery of a family of adiponectin paralogs has implications for understanding the control of energy homeostasis and could provide new targets for pharmacologic intervention in metabolic diseases such as diabetes and obesity.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0403760101</identifier><identifier>PMID: 15231994</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Acetyl-CoA Carboxylase - metabolism ; Adiponectin ; Amino acids ; AMP-Activated Protein Kinases ; Animals ; Biological Sciences ; Cellular biology ; COS Cells ; Diabetes ; Fatty acids ; Fatty Acids - metabolism ; Glycogen ; Glycogen - metabolism ; Intercellular Signaling Peptides and Proteins ; Metabolism ; Mice ; Mitogen-Activated Protein Kinase 1 - metabolism ; Mitogen-Activated Protein Kinase 3 ; Mitogen-Activated Protein Kinases - metabolism ; Multienzyme Complexes - metabolism ; Muscle fibers ; Muscle Fibers, Skeletal - metabolism ; Oxidation ; Oxidation-Reduction ; Phosphorylation ; Protein Processing, Post-Translational ; Protein-Serine-Threonine Kinases - metabolism ; Proteins ; Proteins - chemistry ; Proteins - genetics ; Proteins - metabolism ; Recombinant Proteins - genetics ; Signal Transduction - physiology ; Structure-Activity Relationship ; Type 2 diabetes mellitus</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2004-07, Vol.101 (28), p.10302-10307</ispartof><rights>Copyright 1993/2004 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Jul 13, 2004</rights><rights>Copyright © 2004, The National Academy of Sciences 2004</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c638t-49aefd0e7cdf9dea419bf5ca03e0a0bfa69c5cc0a143078f55316a07a5716ba83</citedby><cites>FETCH-LOGICAL-c638t-49aefd0e7cdf9dea419bf5ca03e0a0bfa69c5cc0a143078f55316a07a5716ba83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/101/28.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3372886$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3372886$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,725,778,782,801,883,27911,27912,53778,53780,58004,58237</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15231994$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wong, Guang W.</creatorcontrib><creatorcontrib>Wang, Jin</creatorcontrib><creatorcontrib>Hug, Christopher</creatorcontrib><creatorcontrib>Tsao, Tsu-Shuen</creatorcontrib><creatorcontrib>Lodish, Harvey F.</creatorcontrib><title>A Family of Acrp30/Adiponectin Structural and Functional Paralogs</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Biochemical, genetic, and animal studies in recent years have established a critical role for the adipokine Acrp30/adiponectin in controlling whole-body metabolism, particularly by enhancing insulin sensitivity in muscle and liver, and by increasing fatty acid oxidation in muscle. We describe a widely expressed and highly conserved family of adiponectin paralogs designated as C1q/tumor necrosis factor-α-related proteins (CTRPs) 1-7. In the present study, we focus on mCTRP2, the mouse paralog most similar to adiponectin. At nanomolar concentrations, bacterially produced mCTRP2 rapidly induced phosphorylation of AMP-activated protein kinase, acetyl-CoA carboxylase, and mitogen-activated protein kinase in C2C12 myotubes, which resulted in increased glycogen accumulation and fatty acid oxidation. The discovery of a family of adiponectin paralogs has implications for understanding the control of energy homeostasis and could provide new targets for pharmacologic intervention in metabolic diseases such as diabetes and obesity.</description><subject>Acetyl-CoA Carboxylase - metabolism</subject><subject>Adiponectin</subject><subject>Amino acids</subject><subject>AMP-Activated Protein Kinases</subject><subject>Animals</subject><subject>Biological Sciences</subject><subject>Cellular biology</subject><subject>COS Cells</subject><subject>Diabetes</subject><subject>Fatty acids</subject><subject>Fatty Acids - metabolism</subject><subject>Glycogen</subject><subject>Glycogen - metabolism</subject><subject>Intercellular Signaling Peptides and Proteins</subject><subject>Metabolism</subject><subject>Mice</subject><subject>Mitogen-Activated Protein Kinase 1 - metabolism</subject><subject>Mitogen-Activated Protein Kinase 3</subject><subject>Mitogen-Activated Protein Kinases - metabolism</subject><subject>Multienzyme Complexes - metabolism</subject><subject>Muscle fibers</subject><subject>Muscle Fibers, Skeletal - metabolism</subject><subject>Oxidation</subject><subject>Oxidation-Reduction</subject><subject>Phosphorylation</subject><subject>Protein Processing, Post-Translational</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Proteins - genetics</subject><subject>Proteins - metabolism</subject><subject>Recombinant Proteins - genetics</subject><subject>Signal Transduction - physiology</subject><subject>Structure-Activity Relationship</subject><subject>Type 2 diabetes mellitus</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0c1rFDEUAPAgit1Wz15EBg8FD9N9-Zh8HHoYiqtCQUE9h2wmqbPMJmMyI_a_N8MuXfXS0yMvv_d4yUPoFYYrDIKux2DyFTCgggMG_AStMChcc6bgKVoBEFFLRtgZOs95BwCqkfAcneGGUKwUW6G2rTZm3w_3VfRVa9NIYd12_RiDs1Mfqq9Tmu00JzNUJnTVZg4lHUM5fjElGe_yC_TMmyG7l8d4gb5v3n-7-Vjffv7w6aa9rS2ncqqZMs534ITtvOqcYVhtfWMNUAcGtt5wZRtrwWBGQUjfNBRzA8I0AvOtkfQCXR_6jvN27zrrwlQG0GPq9ybd62h6_e9N6H_ou_hLMyEbLkr95bE-xZ-zy5Pe99m6YTDBxTlrzgUwIvGjkICkBOMFvv0P7uKcyt8sBlOqFCcFrQ_Ipphzcv5hYgx62aFedqhPOywVb_5-6Mkfl1bAuyNYKk_tsCayBApE-3kYJvd7KrZ6xBby-kB2eYrpwVAqiJSc_gGk4Lmb</recordid><startdate>20040713</startdate><enddate>20040713</enddate><creator>Wong, Guang W.</creator><creator>Wang, Jin</creator><creator>Hug, Christopher</creator><creator>Tsao, Tsu-Shuen</creator><creator>Lodish, Harvey F.</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20040713</creationdate><title>A Family of Acrp30/Adiponectin Structural and Functional Paralogs</title><author>Wong, Guang W. ; Wang, Jin ; Hug, Christopher ; Tsao, Tsu-Shuen ; Lodish, Harvey F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c638t-49aefd0e7cdf9dea419bf5ca03e0a0bfa69c5cc0a143078f55316a07a5716ba83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Acetyl-CoA Carboxylase - metabolism</topic><topic>Adiponectin</topic><topic>Amino acids</topic><topic>AMP-Activated Protein Kinases</topic><topic>Animals</topic><topic>Biological Sciences</topic><topic>Cellular biology</topic><topic>COS Cells</topic><topic>Diabetes</topic><topic>Fatty acids</topic><topic>Fatty Acids - metabolism</topic><topic>Glycogen</topic><topic>Glycogen - metabolism</topic><topic>Intercellular Signaling Peptides and Proteins</topic><topic>Metabolism</topic><topic>Mice</topic><topic>Mitogen-Activated Protein Kinase 1 - metabolism</topic><topic>Mitogen-Activated Protein Kinase 3</topic><topic>Mitogen-Activated Protein Kinases - metabolism</topic><topic>Multienzyme Complexes - metabolism</topic><topic>Muscle fibers</topic><topic>Muscle Fibers, Skeletal - metabolism</topic><topic>Oxidation</topic><topic>Oxidation-Reduction</topic><topic>Phosphorylation</topic><topic>Protein Processing, Post-Translational</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Proteins</topic><topic>Proteins - chemistry</topic><topic>Proteins - genetics</topic><topic>Proteins - metabolism</topic><topic>Recombinant Proteins - genetics</topic><topic>Signal Transduction - physiology</topic><topic>Structure-Activity Relationship</topic><topic>Type 2 diabetes mellitus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wong, Guang W.</creatorcontrib><creatorcontrib>Wang, Jin</creatorcontrib><creatorcontrib>Hug, Christopher</creatorcontrib><creatorcontrib>Tsao, Tsu-Shuen</creatorcontrib><creatorcontrib>Lodish, Harvey F.</creatorcontrib><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS 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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wong, Guang W.</au><au>Wang, Jin</au><au>Hug, Christopher</au><au>Tsao, Tsu-Shuen</au><au>Lodish, Harvey F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Family of Acrp30/Adiponectin Structural and Functional Paralogs</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2004-07-13</date><risdate>2004</risdate><volume>101</volume><issue>28</issue><spage>10302</spage><epage>10307</epage><pages>10302-10307</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Biochemical, genetic, and animal studies in recent years have established a critical role for the adipokine Acrp30/adiponectin in controlling whole-body metabolism, particularly by enhancing insulin sensitivity in muscle and liver, and by increasing fatty acid oxidation in muscle. We describe a widely expressed and highly conserved family of adiponectin paralogs designated as C1q/tumor necrosis factor-α-related proteins (CTRPs) 1-7. In the present study, we focus on mCTRP2, the mouse paralog most similar to adiponectin. At nanomolar concentrations, bacterially produced mCTRP2 rapidly induced phosphorylation of AMP-activated protein kinase, acetyl-CoA carboxylase, and mitogen-activated protein kinase in C2C12 myotubes, which resulted in increased glycogen accumulation and fatty acid oxidation. The discovery of a family of adiponectin paralogs has implications for understanding the control of energy homeostasis and could provide new targets for pharmacologic intervention in metabolic diseases such as diabetes and obesity.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>15231994</pmid><doi>10.1073/pnas.0403760101</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 2004-07, Vol.101 (28), p.10302-10307 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_66704281 |
| source | MEDLINE; Jstor Complete Legacy; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Acetyl-CoA Carboxylase - metabolism Adiponectin Amino acids AMP-Activated Protein Kinases Animals Biological Sciences Cellular biology COS Cells Diabetes Fatty acids Fatty Acids - metabolism Glycogen Glycogen - metabolism Intercellular Signaling Peptides and Proteins Metabolism Mice Mitogen-Activated Protein Kinase 1 - metabolism Mitogen-Activated Protein Kinase 3 Mitogen-Activated Protein Kinases - metabolism Multienzyme Complexes - metabolism Muscle fibers Muscle Fibers, Skeletal - metabolism Oxidation Oxidation-Reduction Phosphorylation Protein Processing, Post-Translational Protein-Serine-Threonine Kinases - metabolism Proteins Proteins - chemistry Proteins - genetics Proteins - metabolism Recombinant Proteins - genetics Signal Transduction - physiology Structure-Activity Relationship Type 2 diabetes mellitus |
| title | A Family of Acrp30/Adiponectin Structural and Functional Paralogs |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-15T17%3A00%3A56IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=A%20Family%20of%20Acrp30/Adiponectin%20Structural%20and%20Functional%20Paralogs&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Wong,%20Guang%20W.&rft.date=2004-07-13&rft.volume=101&rft.issue=28&rft.spage=10302&rft.epage=10307&rft.pages=10302-10307&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.0403760101&rft_dat=%3Cjstor_proqu%3E3372886%3C/jstor_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=201339962&rft_id=info:pmid/15231994&rft_jstor_id=3372886&rfr_iscdi=true |