Adiponectin inhibits leptin signalling via multiple mechanisms to exert protective effects against hepatic fibrosis

Adiponectin is protective against hepatic fibrosis, whereas leptin promotes fibrosis. In HSCs (hepatic stellate cells), leptin signals via a JAK2 (Janus kinase 2)/STAT3 (signal transducer and activator of transcription 3) pathway, producing effects that enhance ECM (extracellular matrix) deposition....

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Biochemical journal 2011-12, Vol.440 (3), p.385-395
Hauptverfasser: Handy, Jeffrey A, Fu, Ping P, Kumar, Pradeep, Mells, Jamie E, Sharma, Shvetank, Saxena, Neeraj K, Anania, Frank A
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 395
container_issue 3
container_start_page 385
container_title Biochemical journal
container_volume 440
creator Handy, Jeffrey A
Fu, Ping P
Kumar, Pradeep
Mells, Jamie E
Sharma, Shvetank
Saxena, Neeraj K
Anania, Frank A
description Adiponectin is protective against hepatic fibrosis, whereas leptin promotes fibrosis. In HSCs (hepatic stellate cells), leptin signals via a JAK2 (Janus kinase 2)/STAT3 (signal transducer and activator of transcription 3) pathway, producing effects that enhance ECM (extracellular matrix) deposition. SOCS-3 (suppressor of cytokine signalling-3) and PTP1B (protein tyrosine phosphatase 1B) are both negative regulators of JAK/STAT signalling, and recent studies have demonstrated a role for adiponectin in regulating SOCS-3 expression. In the present study we investigate mechanisms whereby adiponectin dampens leptin signalling and prevents excess ECM production. We treated culture-activated rat HSCs with recombinant adiponectin, leptin, both or neither, and also treated adiponectin knockout (Ad-/-) and wild-type mice with leptin and/or carbon tetrachloride (CCl4) or saline. We analyse JAK2 and Ob-Rb (long form of the leptin receptor) phosphorylation, and PTP1B expression and activity. We also explore potential mechanisms through which adiponectin regulates SOCS-3-Ob-Rb association. Adiponectin inhibits leptin-stimulated JAK2 activation and Ob-Rb phosphorylation in HSCs, whereas both were increased in Ad-/- mice. Adiponectin stimulates PTP1B expression and activity in vitro, whereas PTP1B expression was lower in Ad-/-mice than in wild-type mice. Adiponectin also promotes SOCS-3-Ob-R association and blocks leptin-stimulated formation of extracellular TIMP-1 (tissue inhibitor of metalloproteinases-1)-MMP-1 (matrix metalloproteinase-1) complexes in vitro. These results suggest two novel mechanisms whereby adiponectin inhibits hepatic fibrosis: (i) by promoting binding of SOCS-3 to Ob-Rb, and (ii) by stimulating PTP1B expression and activity, thus inhibiting JAK2/STAT3 signalling at multiple points.
doi_str_mv 10.1042/BJ20102148
format Article
fullrecord <record><control><sourceid>pubmed_cross</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3226855</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>21846328</sourcerecordid><originalsourceid>FETCH-LOGICAL-c377t-b78eb7083a3a20ad4fb7fc39c7cdba483e9b509ca80846a2d9fbd4e64e3e29843</originalsourceid><addsrcrecordid>eNpVkE1PwzAMhiMEYmNw4QegnJEKaZK16QVpTHxqEhc4V0nqtkZtWjXZBP-eToMBJ9t67cf2S8h5zK5iJvn17TNnMeOxVAdkGsuURSrl6pBMGU9klIzKhJx4_85YLJlkx2TCYyUTwdWU-EWBfefABnQUXY0Gg6cN9NvaY-V006Cr6AY1bddNwL4B2oKttUPfeho6Ch8wBNoPXdhSNkChLMfMU11pdD7QGnod0NISzdB59KfkqNSNh7PvOCNv93evy8do9fLwtFysIivSNEQmVWBSpoQWmjNdyNKkpRWZTW1htFQCMjNnmdWKjd9oXmSlKSQkEgTwTEkxIzc7br82LRQWXBh0k_cDtnr4zDuN-X_FYZ1X3SYXnCdqPh8BlzuAHe_2A5T72ZjlW-vzX-vH5ou_2_atP16LLyTug2A</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Adiponectin inhibits leptin signalling via multiple mechanisms to exert protective effects against hepatic fibrosis</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><creator>Handy, Jeffrey A ; Fu, Ping P ; Kumar, Pradeep ; Mells, Jamie E ; Sharma, Shvetank ; Saxena, Neeraj K ; Anania, Frank A</creator><creatorcontrib>Handy, Jeffrey A ; Fu, Ping P ; Kumar, Pradeep ; Mells, Jamie E ; Sharma, Shvetank ; Saxena, Neeraj K ; Anania, Frank A</creatorcontrib><description>Adiponectin is protective against hepatic fibrosis, whereas leptin promotes fibrosis. In HSCs (hepatic stellate cells), leptin signals via a JAK2 (Janus kinase 2)/STAT3 (signal transducer and activator of transcription 3) pathway, producing effects that enhance ECM (extracellular matrix) deposition. SOCS-3 (suppressor of cytokine signalling-3) and PTP1B (protein tyrosine phosphatase 1B) are both negative regulators of JAK/STAT signalling, and recent studies have demonstrated a role for adiponectin in regulating SOCS-3 expression. In the present study we investigate mechanisms whereby adiponectin dampens leptin signalling and prevents excess ECM production. We treated culture-activated rat HSCs with recombinant adiponectin, leptin, both or neither, and also treated adiponectin knockout (Ad-/-) and wild-type mice with leptin and/or carbon tetrachloride (CCl4) or saline. We analyse JAK2 and Ob-Rb (long form of the leptin receptor) phosphorylation, and PTP1B expression and activity. We also explore potential mechanisms through which adiponectin regulates SOCS-3-Ob-Rb association. Adiponectin inhibits leptin-stimulated JAK2 activation and Ob-Rb phosphorylation in HSCs, whereas both were increased in Ad-/- mice. Adiponectin stimulates PTP1B expression and activity in vitro, whereas PTP1B expression was lower in Ad-/-mice than in wild-type mice. Adiponectin also promotes SOCS-3-Ob-R association and blocks leptin-stimulated formation of extracellular TIMP-1 (tissue inhibitor of metalloproteinases-1)-MMP-1 (matrix metalloproteinase-1) complexes in vitro. These results suggest two novel mechanisms whereby adiponectin inhibits hepatic fibrosis: (i) by promoting binding of SOCS-3 to Ob-Rb, and (ii) by stimulating PTP1B expression and activity, thus inhibiting JAK2/STAT3 signalling at multiple points.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/BJ20102148</identifier><identifier>PMID: 21846328</identifier><language>eng</language><publisher>England</publisher><subject>Adiponectin - genetics ; Adiponectin - pharmacology ; Adiponectin - physiology ; Animals ; Carbon Tetrachloride ; Cells, Cultured ; Cytoprotection ; Gene Knockout Techniques ; Hepatic Stellate Cells - metabolism ; Humans ; Janus Kinase 2 - metabolism ; Leptin - pharmacology ; Leptin - physiology ; Liver Cirrhosis - chemically induced ; Liver Cirrhosis - physiopathology ; Male ; Matrix Metalloproteinase 1 - metabolism ; Mice ; Mice, Knockout ; Phosphorylation ; Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism ; Rats ; Rats, Sprague-Dawley ; Receptors, Leptin - metabolism ; Recombinant Proteins - pharmacology ; Suppressor of Cytokine Signaling 3 Protein ; Suppressor of Cytokine Signaling Proteins - metabolism ; Tissue Inhibitor of Metalloproteinase-1 - metabolism</subject><ispartof>Biochemical journal, 2011-12, Vol.440 (3), p.385-395</ispartof><rights>2011 Portland Press Limited 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c377t-b78eb7083a3a20ad4fb7fc39c7cdba483e9b509ca80846a2d9fbd4e64e3e29843</citedby><cites>FETCH-LOGICAL-c377t-b78eb7083a3a20ad4fb7fc39c7cdba483e9b509ca80846a2d9fbd4e64e3e29843</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3226855/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3226855/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,315,728,781,785,886,27929,27930,53796,53798</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21846328$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Handy, Jeffrey A</creatorcontrib><creatorcontrib>Fu, Ping P</creatorcontrib><creatorcontrib>Kumar, Pradeep</creatorcontrib><creatorcontrib>Mells, Jamie E</creatorcontrib><creatorcontrib>Sharma, Shvetank</creatorcontrib><creatorcontrib>Saxena, Neeraj K</creatorcontrib><creatorcontrib>Anania, Frank A</creatorcontrib><title>Adiponectin inhibits leptin signalling via multiple mechanisms to exert protective effects against hepatic fibrosis</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>Adiponectin is protective against hepatic fibrosis, whereas leptin promotes fibrosis. In HSCs (hepatic stellate cells), leptin signals via a JAK2 (Janus kinase 2)/STAT3 (signal transducer and activator of transcription 3) pathway, producing effects that enhance ECM (extracellular matrix) deposition. SOCS-3 (suppressor of cytokine signalling-3) and PTP1B (protein tyrosine phosphatase 1B) are both negative regulators of JAK/STAT signalling, and recent studies have demonstrated a role for adiponectin in regulating SOCS-3 expression. In the present study we investigate mechanisms whereby adiponectin dampens leptin signalling and prevents excess ECM production. We treated culture-activated rat HSCs with recombinant adiponectin, leptin, both or neither, and also treated adiponectin knockout (Ad-/-) and wild-type mice with leptin and/or carbon tetrachloride (CCl4) or saline. We analyse JAK2 and Ob-Rb (long form of the leptin receptor) phosphorylation, and PTP1B expression and activity. We also explore potential mechanisms through which adiponectin regulates SOCS-3-Ob-Rb association. Adiponectin inhibits leptin-stimulated JAK2 activation and Ob-Rb phosphorylation in HSCs, whereas both were increased in Ad-/- mice. Adiponectin stimulates PTP1B expression and activity in vitro, whereas PTP1B expression was lower in Ad-/-mice than in wild-type mice. Adiponectin also promotes SOCS-3-Ob-R association and blocks leptin-stimulated formation of extracellular TIMP-1 (tissue inhibitor of metalloproteinases-1)-MMP-1 (matrix metalloproteinase-1) complexes in vitro. These results suggest two novel mechanisms whereby adiponectin inhibits hepatic fibrosis: (i) by promoting binding of SOCS-3 to Ob-Rb, and (ii) by stimulating PTP1B expression and activity, thus inhibiting JAK2/STAT3 signalling at multiple points.</description><subject>Adiponectin - genetics</subject><subject>Adiponectin - pharmacology</subject><subject>Adiponectin - physiology</subject><subject>Animals</subject><subject>Carbon Tetrachloride</subject><subject>Cells, Cultured</subject><subject>Cytoprotection</subject><subject>Gene Knockout Techniques</subject><subject>Hepatic Stellate Cells - metabolism</subject><subject>Humans</subject><subject>Janus Kinase 2 - metabolism</subject><subject>Leptin - pharmacology</subject><subject>Leptin - physiology</subject><subject>Liver Cirrhosis - chemically induced</subject><subject>Liver Cirrhosis - physiopathology</subject><subject>Male</subject><subject>Matrix Metalloproteinase 1 - metabolism</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Phosphorylation</subject><subject>Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Receptors, Leptin - metabolism</subject><subject>Recombinant Proteins - pharmacology</subject><subject>Suppressor of Cytokine Signaling 3 Protein</subject><subject>Suppressor of Cytokine Signaling Proteins - metabolism</subject><subject>Tissue Inhibitor of Metalloproteinase-1 - metabolism</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkE1PwzAMhiMEYmNw4QegnJEKaZK16QVpTHxqEhc4V0nqtkZtWjXZBP-eToMBJ9t67cf2S8h5zK5iJvn17TNnMeOxVAdkGsuURSrl6pBMGU9klIzKhJx4_85YLJlkx2TCYyUTwdWU-EWBfefABnQUXY0Gg6cN9NvaY-V006Cr6AY1bddNwL4B2oKttUPfeho6Ch8wBNoPXdhSNkChLMfMU11pdD7QGnod0NISzdB59KfkqNSNh7PvOCNv93evy8do9fLwtFysIivSNEQmVWBSpoQWmjNdyNKkpRWZTW1htFQCMjNnmdWKjd9oXmSlKSQkEgTwTEkxIzc7br82LRQWXBh0k_cDtnr4zDuN-X_FYZ1X3SYXnCdqPh8BlzuAHe_2A5T72ZjlW-vzX-vH5ou_2_atP16LLyTug2A</recordid><startdate>20111215</startdate><enddate>20111215</enddate><creator>Handy, Jeffrey A</creator><creator>Fu, Ping P</creator><creator>Kumar, Pradeep</creator><creator>Mells, Jamie E</creator><creator>Sharma, Shvetank</creator><creator>Saxena, Neeraj K</creator><creator>Anania, Frank A</creator><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>5PM</scope></search><sort><creationdate>20111215</creationdate><title>Adiponectin inhibits leptin signalling via multiple mechanisms to exert protective effects against hepatic fibrosis</title><author>Handy, Jeffrey A ; Fu, Ping P ; Kumar, Pradeep ; Mells, Jamie E ; Sharma, Shvetank ; Saxena, Neeraj K ; Anania, Frank A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c377t-b78eb7083a3a20ad4fb7fc39c7cdba483e9b509ca80846a2d9fbd4e64e3e29843</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Adiponectin - genetics</topic><topic>Adiponectin - pharmacology</topic><topic>Adiponectin - physiology</topic><topic>Animals</topic><topic>Carbon Tetrachloride</topic><topic>Cells, Cultured</topic><topic>Cytoprotection</topic><topic>Gene Knockout Techniques</topic><topic>Hepatic Stellate Cells - metabolism</topic><topic>Humans</topic><topic>Janus Kinase 2 - metabolism</topic><topic>Leptin - pharmacology</topic><topic>Leptin - physiology</topic><topic>Liver Cirrhosis - chemically induced</topic><topic>Liver Cirrhosis - physiopathology</topic><topic>Male</topic><topic>Matrix Metalloproteinase 1 - metabolism</topic><topic>Mice</topic><topic>Mice, Knockout</topic><topic>Phosphorylation</topic><topic>Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>Receptors, Leptin - metabolism</topic><topic>Recombinant Proteins - pharmacology</topic><topic>Suppressor of Cytokine Signaling 3 Protein</topic><topic>Suppressor of Cytokine Signaling Proteins - metabolism</topic><topic>Tissue Inhibitor of Metalloproteinase-1 - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Handy, Jeffrey A</creatorcontrib><creatorcontrib>Fu, Ping P</creatorcontrib><creatorcontrib>Kumar, Pradeep</creatorcontrib><creatorcontrib>Mells, Jamie E</creatorcontrib><creatorcontrib>Sharma, Shvetank</creatorcontrib><creatorcontrib>Saxena, Neeraj K</creatorcontrib><creatorcontrib>Anania, Frank A</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Handy, Jeffrey A</au><au>Fu, Ping P</au><au>Kumar, Pradeep</au><au>Mells, Jamie E</au><au>Sharma, Shvetank</au><au>Saxena, Neeraj K</au><au>Anania, Frank A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Adiponectin inhibits leptin signalling via multiple mechanisms to exert protective effects against hepatic fibrosis</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>2011-12-15</date><risdate>2011</risdate><volume>440</volume><issue>3</issue><spage>385</spage><epage>395</epage><pages>385-395</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>Adiponectin is protective against hepatic fibrosis, whereas leptin promotes fibrosis. In HSCs (hepatic stellate cells), leptin signals via a JAK2 (Janus kinase 2)/STAT3 (signal transducer and activator of transcription 3) pathway, producing effects that enhance ECM (extracellular matrix) deposition. SOCS-3 (suppressor of cytokine signalling-3) and PTP1B (protein tyrosine phosphatase 1B) are both negative regulators of JAK/STAT signalling, and recent studies have demonstrated a role for adiponectin in regulating SOCS-3 expression. In the present study we investigate mechanisms whereby adiponectin dampens leptin signalling and prevents excess ECM production. We treated culture-activated rat HSCs with recombinant adiponectin, leptin, both or neither, and also treated adiponectin knockout (Ad-/-) and wild-type mice with leptin and/or carbon tetrachloride (CCl4) or saline. We analyse JAK2 and Ob-Rb (long form of the leptin receptor) phosphorylation, and PTP1B expression and activity. We also explore potential mechanisms through which adiponectin regulates SOCS-3-Ob-Rb association. Adiponectin inhibits leptin-stimulated JAK2 activation and Ob-Rb phosphorylation in HSCs, whereas both were increased in Ad-/- mice. Adiponectin stimulates PTP1B expression and activity in vitro, whereas PTP1B expression was lower in Ad-/-mice than in wild-type mice. Adiponectin also promotes SOCS-3-Ob-R association and blocks leptin-stimulated formation of extracellular TIMP-1 (tissue inhibitor of metalloproteinases-1)-MMP-1 (matrix metalloproteinase-1) complexes in vitro. These results suggest two novel mechanisms whereby adiponectin inhibits hepatic fibrosis: (i) by promoting binding of SOCS-3 to Ob-Rb, and (ii) by stimulating PTP1B expression and activity, thus inhibiting JAK2/STAT3 signalling at multiple points.</abstract><cop>England</cop><pmid>21846328</pmid><doi>10.1042/BJ20102148</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0264-6021
ispartof Biochemical journal, 2011-12, Vol.440 (3), p.385-395
issn 0264-6021
1470-8728
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3226855
source MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central
subjects Adiponectin - genetics
Adiponectin - pharmacology
Adiponectin - physiology
Animals
Carbon Tetrachloride
Cells, Cultured
Cytoprotection
Gene Knockout Techniques
Hepatic Stellate Cells - metabolism
Humans
Janus Kinase 2 - metabolism
Leptin - pharmacology
Leptin - physiology
Liver Cirrhosis - chemically induced
Liver Cirrhosis - physiopathology
Male
Matrix Metalloproteinase 1 - metabolism
Mice
Mice, Knockout
Phosphorylation
Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism
Rats
Rats, Sprague-Dawley
Receptors, Leptin - metabolism
Recombinant Proteins - pharmacology
Suppressor of Cytokine Signaling 3 Protein
Suppressor of Cytokine Signaling Proteins - metabolism
Tissue Inhibitor of Metalloproteinase-1 - metabolism
title Adiponectin inhibits leptin signalling via multiple mechanisms to exert protective effects against hepatic fibrosis
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-11T16%3A28%3A44IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-pubmed_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Adiponectin%20inhibits%20leptin%20signalling%20via%20multiple%20mechanisms%20to%20exert%20protective%20effects%20against%20hepatic%20fibrosis&rft.jtitle=Biochemical%20journal&rft.au=Handy,%20Jeffrey%20A&rft.date=2011-12-15&rft.volume=440&rft.issue=3&rft.spage=385&rft.epage=395&rft.pages=385-395&rft.issn=0264-6021&rft.eissn=1470-8728&rft_id=info:doi/10.1042/BJ20102148&rft_dat=%3Cpubmed_cross%3E21846328%3C/pubmed_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/21846328&rfr_iscdi=true