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....
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Veröffentlicht in: | Biochemical journal 2011-12, Vol.440 (3), p.385-395 |
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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 |
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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> |
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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 |
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