Activation of myocardial neutral triglyceride lipase and neutral cholesterol esterase by cAMP-dependent protein kinase
Lipolysis of intracellular triglycerides in the heart has been shown to be regulated by hormones. However, activation of myocardial triglyceride lipase in a cell-free system has not been directly demonstrated. In the present studies, initial attempts to demonstrate cAMP-dependent activation of trigl...
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Veröffentlicht in: | The Journal of biological chemistry 1985-05, Vol.260 (10), p.5879-5882 |
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description | Lipolysis of intracellular triglycerides in the heart has been shown to be regulated by hormones. However, activation of myocardial triglyceride lipase in a cell-free system has not been directly demonstrated. In the present studies, initial attempts to demonstrate cAMP-dependent activation of triglyceride lipase using the 1,000 X g supernatant fraction (S1) of mouse heart homogenate were unsuccessful, presumably due to the masking effects of high levels of lipoprotein lipase activity even when assayed at pH 7.4 and in the absence of apolipoprotein C-II. Myocardial lipoprotein lipase in the 40,000 X g supernatant fraction was then removed by heparin-Sepharose affinity chromatography. The lipoprotein lipase-free fractions were shown to contain neutral triglyceride lipase and neutral cholesterol esterase of about equal activities. The triglyceride lipase and cholesterol esterase activities fell progressively during preincubation in the presence of 5 mM Mg2+. Additions of cAMP and ATP resulted in 40-70% activation of both triglyceride lipase and cholesterol esterase. The activation was blocked by protein kinase inhibitor and was restored by the addition of exogenous cAMP-dependent protein kinase. Since lipoprotein lipase has no activity toward cholesteryl oleate, activation of cholesterol esterase in untreated S1 was readily demonstrable. Both triglyceride lipase and cholesterol esterase activities were present in homogenates prepared from isolated rat heart myocytes. We conclude that the myocardium contains a hormone-sensitive lipase that is regulated in a fashion similar to that of the adipose tissue enzyme. |
doi_str_mv | 10.1016/S0021-9258(18)88908-6 |
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However, activation of myocardial triglyceride lipase in a cell-free system has not been directly demonstrated. In the present studies, initial attempts to demonstrate cAMP-dependent activation of triglyceride lipase using the 1,000 X g supernatant fraction (S1) of mouse heart homogenate were unsuccessful, presumably due to the masking effects of high levels of lipoprotein lipase activity even when assayed at pH 7.4 and in the absence of apolipoprotein C-II. Myocardial lipoprotein lipase in the 40,000 X g supernatant fraction was then removed by heparin-Sepharose affinity chromatography. The lipoprotein lipase-free fractions were shown to contain neutral triglyceride lipase and neutral cholesterol esterase of about equal activities. The triglyceride lipase and cholesterol esterase activities fell progressively during preincubation in the presence of 5 mM Mg2+. Additions of cAMP and ATP resulted in 40-70% activation of both triglyceride lipase and cholesterol esterase. The activation was blocked by protein kinase inhibitor and was restored by the addition of exogenous cAMP-dependent protein kinase. Since lipoprotein lipase has no activity toward cholesteryl oleate, activation of cholesterol esterase in untreated S1 was readily demonstrable. Both triglyceride lipase and cholesterol esterase activities were present in homogenates prepared from isolated rat heart myocytes. We conclude that the myocardium contains a hormone-sensitive lipase that is regulated in a fashion similar to that of the adipose tissue enzyme.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)88908-6</identifier><identifier>PMID: 2987207</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Adenosine Triphosphate - pharmacology ; Animals ; Biological and medical sciences ; Carboxylic Ester Hydrolases - metabolism ; Carrier Proteins - pharmacology ; Cell physiology ; Cell-Free System ; Cyclic AMP - pharmacology ; Enzyme Activation - drug effects ; Fundamental and applied biological sciences. Psychology ; Hormonal regulation ; In Vitro Techniques ; Intracellular Signaling Peptides and Proteins ; Kinetics ; Lipase - metabolism ; Lipoprotein Lipase - metabolism ; Mice ; Molecular and cellular biology ; Myocardium - enzymology ; Protein Kinases - pharmacology ; Sterol Esterase - metabolism</subject><ispartof>The Journal of biological chemistry, 1985-05, Vol.260 (10), p.5879-5882</ispartof><rights>1985 © 1985 ASBMB. 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However, activation of myocardial triglyceride lipase in a cell-free system has not been directly demonstrated. In the present studies, initial attempts to demonstrate cAMP-dependent activation of triglyceride lipase using the 1,000 X g supernatant fraction (S1) of mouse heart homogenate were unsuccessful, presumably due to the masking effects of high levels of lipoprotein lipase activity even when assayed at pH 7.4 and in the absence of apolipoprotein C-II. Myocardial lipoprotein lipase in the 40,000 X g supernatant fraction was then removed by heparin-Sepharose affinity chromatography. The lipoprotein lipase-free fractions were shown to contain neutral triglyceride lipase and neutral cholesterol esterase of about equal activities. The triglyceride lipase and cholesterol esterase activities fell progressively during preincubation in the presence of 5 mM Mg2+. Additions of cAMP and ATP resulted in 40-70% activation of both triglyceride lipase and cholesterol esterase. The activation was blocked by protein kinase inhibitor and was restored by the addition of exogenous cAMP-dependent protein kinase. Since lipoprotein lipase has no activity toward cholesteryl oleate, activation of cholesterol esterase in untreated S1 was readily demonstrable. Both triglyceride lipase and cholesterol esterase activities were present in homogenates prepared from isolated rat heart myocytes. We conclude that the myocardium contains a hormone-sensitive lipase that is regulated in a fashion similar to that of the adipose tissue enzyme.</description><subject>Adenosine Triphosphate - pharmacology</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Carboxylic Ester Hydrolases - metabolism</subject><subject>Carrier Proteins - pharmacology</subject><subject>Cell physiology</subject><subject>Cell-Free System</subject><subject>Cyclic AMP - pharmacology</subject><subject>Enzyme Activation - drug effects</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hormonal regulation</subject><subject>In Vitro Techniques</subject><subject>Intracellular Signaling Peptides and Proteins</subject><subject>Kinetics</subject><subject>Lipase - metabolism</subject><subject>Lipoprotein Lipase - metabolism</subject><subject>Mice</subject><subject>Molecular and cellular biology</subject><subject>Myocardium - enzymology</subject><subject>Protein Kinases - pharmacology</subject><subject>Sterol Esterase - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkFFrFDEUhYNY6rb6EwoBRfRhNMlkMsmTLMWq0KKggm8hk9zpRmeSbTK7Zf-9md1lX5uX-3C-m3PuQeiKkg-UUPHxJyGMVoo18h2V76VURFbiGVpQIuuqbuif52hxQl6gi5z_kvK4oufonCnZMtIu0HZpJ781k48Bxx6Pu2hNct4MOMBmSmVOyd8POwvJO8CDX5sM2AR30u0qDpAnSHHA-zkD3Q7b5d2PysEagoMw4XWKE_iA__lQgJforDdDhlfHeYl-33z-df21uv3-5dv18rayXPCpqp1pZdfUolXKyLahjDPGSMM6RoQgxrmidXXP-g56q5Tk0HFGVWfBQS_q-hK9Pfxb7B82JZ4efbYwDCZA3GTdCkppo1QBmwNoU8w5Qa_XyY8m7TQleu5b7_vWc5maSr3vW4uyd3U02HQjuNPWseCivznqJlsz9MkE6_MJk5wTzlnBXh-wlb9fPfoEuvPRrmDUTMz-upHtHPLTgYJS2dZD0tl6COXYsmEn7aJ_Iu5_AhSqHA</recordid><startdate>19850525</startdate><enddate>19850525</enddate><creator>Goldberg, D I</creator><creator>Khoo, J C</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><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>7X8</scope></search><sort><creationdate>19850525</creationdate><title>Activation of myocardial neutral triglyceride lipase and neutral cholesterol esterase by cAMP-dependent protein kinase</title><author>Goldberg, D I ; Khoo, J C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c464t-3da78b536799a875124222052b20660add536b3f2fbefc9984eb4219bcedef633</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Adenosine Triphosphate - pharmacology</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Carboxylic Ester Hydrolases - metabolism</topic><topic>Carrier Proteins - pharmacology</topic><topic>Cell physiology</topic><topic>Cell-Free System</topic><topic>Cyclic AMP - pharmacology</topic><topic>Enzyme Activation - drug effects</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hormonal regulation</topic><topic>In Vitro Techniques</topic><topic>Intracellular Signaling Peptides and Proteins</topic><topic>Kinetics</topic><topic>Lipase - metabolism</topic><topic>Lipoprotein Lipase - metabolism</topic><topic>Mice</topic><topic>Molecular and cellular biology</topic><topic>Myocardium - enzymology</topic><topic>Protein Kinases - pharmacology</topic><topic>Sterol Esterase - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Goldberg, D I</creatorcontrib><creatorcontrib>Khoo, J C</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Goldberg, D I</au><au>Khoo, J C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Activation of myocardial neutral triglyceride lipase and neutral cholesterol esterase by cAMP-dependent protein kinase</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1985-05-25</date><risdate>1985</risdate><volume>260</volume><issue>10</issue><spage>5879</spage><epage>5882</epage><pages>5879-5882</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Lipolysis of intracellular triglycerides in the heart has been shown to be regulated by hormones. However, activation of myocardial triglyceride lipase in a cell-free system has not been directly demonstrated. In the present studies, initial attempts to demonstrate cAMP-dependent activation of triglyceride lipase using the 1,000 X g supernatant fraction (S1) of mouse heart homogenate were unsuccessful, presumably due to the masking effects of high levels of lipoprotein lipase activity even when assayed at pH 7.4 and in the absence of apolipoprotein C-II. Myocardial lipoprotein lipase in the 40,000 X g supernatant fraction was then removed by heparin-Sepharose affinity chromatography. The lipoprotein lipase-free fractions were shown to contain neutral triglyceride lipase and neutral cholesterol esterase of about equal activities. The triglyceride lipase and cholesterol esterase activities fell progressively during preincubation in the presence of 5 mM Mg2+. Additions of cAMP and ATP resulted in 40-70% activation of both triglyceride lipase and cholesterol esterase. The activation was blocked by protein kinase inhibitor and was restored by the addition of exogenous cAMP-dependent protein kinase. Since lipoprotein lipase has no activity toward cholesteryl oleate, activation of cholesterol esterase in untreated S1 was readily demonstrable. Both triglyceride lipase and cholesterol esterase activities were present in homogenates prepared from isolated rat heart myocytes. We conclude that the myocardium contains a hormone-sensitive lipase that is regulated in a fashion similar to that of the adipose tissue enzyme.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>2987207</pmid><doi>10.1016/S0021-9258(18)88908-6</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Adenosine Triphosphate - pharmacology Animals Biological and medical sciences Carboxylic Ester Hydrolases - metabolism Carrier Proteins - pharmacology Cell physiology Cell-Free System Cyclic AMP - pharmacology Enzyme Activation - drug effects Fundamental and applied biological sciences. Psychology Hormonal regulation In Vitro Techniques Intracellular Signaling Peptides and Proteins Kinetics Lipase - metabolism Lipoprotein Lipase - metabolism Mice Molecular and cellular biology Myocardium - enzymology Protein Kinases - pharmacology Sterol Esterase - metabolism |
title | Activation of myocardial neutral triglyceride lipase and neutral cholesterol esterase by cAMP-dependent protein kinase |
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